UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
Q3AZE8
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MRLSISSTNVKEWSGDVLVVGLPKGDPSTTAVNLESRFPGVSSALNQQAFEGKTGQKLVLHPLANGNPQRLVLIGLGDADAIDLDGIRAAAAAAAQASIGCKGCLGLQLPWDSHHPDHAARISAEAVRLSLYADQRFQKEPEERRLPTALELIGLPASAAAGLEPVNATCAGVELARELVAAPPNYVTPAALAETAAALAHDYGMELTILERADCEARGMGAFLAVSQGSDLPPKFIHLIYRPEGAVKRRLALVGKGLTFDSGGYNLKVGGAQIDMMKFDMGGSASVLGAMRSIGELKPAGVEVHMVVASCENMVNGSAVHPGDIVTAANGTTIEINNTDAEGRLTLADALLYACEQKPDAVVDLATLTGACVVALGDEMAGYWSNNEALAEALDTAADAGGEGLWRMPLRQSYKKGLKSLLADMKNTGPRPGGSITAALFLKEFVSQDTAWAHIDIAGPVWSDKGKGVNPAGATGYGVRTLVNWVCAQA
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q3AHT4
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MRFSLSSADLQEWNGDVLAVGLPQGDVDATATALEQRFAGITDALKQQEFKGKPGDQLVITPLGGGPQRLVVLGLGESDAIDTERLRGAAARAAKAAIGCEGSLGLQLPCAGSDAQEAARICAEAVRLCLYKDQRFRKEPDPRRIPEALELIDLSPAAESGFAAVNATCAGVELARELVAAPPNVVTPAALADTAAGIAKDHGLELKVLERSDCEAKGMGAFLAVSQGSDLPPKFIHLIYRPEGEVKRRVALVGKGLTFDSGGYNLKVGAAQIDMMKFDMGGSAAVLGAMRSIAELKPAGVEVHMVVASCENMVNGSAVHPGDIVMAANGMTIEINNTDAEGRLTLADALLYACEQKPDAVVDLATLTGACVIALGDEMAGLWSNNDDLAEALDAAAQTGGEGLWRMPLRQSYKDGLKSLLADMKNTGPRPGGSITAALFLKEFVAKDTAWAHIDIAGPVWSDKGKGVNPAGATGYGVRTLVNWVLAQS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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P73971
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MQIRGTDYTALTWQGDALALGFFENATEITGDLTQLDDRLEGVLRELIEEKEFKGKAGQKLVSRVGSKTPIKKLILVGLGEIEKFNSQVLGDGAAAIARLAKGEKVKTLGVSLPQREHDPAQTAAILTEGILLALHQDNRFKSDPEDKEIKLTTVELLGLGEQSTAIGKAEKIVSGVILAREMVAAPANEVTPLTFTEIATELAQTYGLELEVLGQTECEALGMGAFLGVAKASELPPQFIHLTYRPANPVKKLAIIGKSLTFDSGGLNIKGAGSGIETMKMDMGGGGATLGAAKAIAQLKPNVEIHFICAATENMISGTAMHPGDILTASNGKTIEVNNTDAEGRLTLADALVFAEKLGVEAIVDLATLTGACIVALGDDIGGLWSPNQELADELKVAADKAGEKFWQMPMESKYFEGLKSPIADMKNTGPRSGGSITAALFLQQFIKETPWAHLDIAGPVWTDKQNGVHNAGATGYPVRTLVQWVLGLAE
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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C5BMG6
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MKFLTQKTDALSRASGCSVVFALDNALLTTALALDDALGGVLSQVIKSGDLKAKPGQSCWIPVPAASGVKAARVLLVHLGETSEKKSKIASGSVISALQSAAAALSASPAKDTTVFIDDLFADGAPTIEHFGEPADASWVAEQMAKLFVTASYRYTETFSKPEPAPALGKVTYASDDATRTRAVKSALLKGAAIGEGMNLTRQLGNLPGNICTPAYLVEQAKQLAAACPKLTTKSLNEKQIEKLGMGAFHSVAKGSDLDAQLIIMEYKGAGGAKSQPHVLVGKGITFDTGGISLKPGANMDEMKFDMGGAASVFGAMKALIEMDAKVHVIGVIAAAENMPSGRASKPGDIVTSMSGQTIEILNTDAEGRLVLCDTLTYVERFKPKSVVDIATLTGACVIALGNHATGLYSNEQALADKLLAAGVGANDRAWQMPLWDDYQKQLDSNFADMANIGGPAGGSVTAACFLSRFTKSYPWAHLDIAGTAWQSGAKKGSTGRPVSLLVNYLLNA
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q8DI46
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MQLQTVPTAIPDWSGDLLAIAVFQTEGTLTLTDPYTTLDQRLNGLLQELINEGEFQGKSGTSLLMRLLPNFPLKKLLLVGLGNREDFNLEALRRTAATIARTARRERAKTLGMALPHETLEAADAAQAIAEGVILALHSDVRFKTDPEARKLLPYPEVVTLLGLGEQTAALTRAQQICDGVILARELVNAPANEVTPVTLAETAQQLAATYGLTAKILEREDCGALGMGAFLGVAQASDLPPKFIHLTYTSPGTVHRKIALVGKGLTFDSGGLNLKTQGGIETMKMDMGGAAAVLGTAKVLGQLKPPGIEVHFIIAATENMISGRALHPGDILTASNGKTIEVNNTDAEGRLTLADALVYAEKLGVDAIVDLATLTGACIVALGDNIAGLWSNNAELAQALQKASDRCGEKFWQMPLENKYFEAMKSQVADMKNTGPRSAGSITAALFLQQFVDHTPWAHLDIAGPVWTEKEDGYNNPCGTGYPVRTLVEWLCSLSS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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B8GTX6
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MEFSVKSGNPEKQRSACVVVGVFDRRKLSSAARVLDKASGGALSTILRRGDMDGEKGQTLWLYNLPNTLCERVLLVGCGKERDFDEPAYRSVIATVARTVNKSGAVEAVNYLTDLPVKGRDTLWKISQAVTITQDSLYSFQQLKSKKEDTQRPLKRIILSVPSRADLLPGEDAVRVATAISVGTKLTRDLANLPGNICNPTYLAEQALQLKKTYKGLKVEILEEADMEKLGMGALLSVSRGSEQPAKLITLEYRGGRKDAKPVVLVGKGITFDTGGISLKPGAEMDEMKFDMCGAASVLGVMKAVAEMMLPINLVGVVAAAENMPDGKATRPGDVVTSMSGQTIEILNTDAEGRLVLCDALSYVERFDPDVVIDIATLTGACIIALGHQATGLLSNHSPLANDLLGAGKQSYDRAWELPLWDEYQEQLKSNFADMANIGGRPAGTITAACFLSRFTKKYKWAHLDIAGVAWKSGKEKGATGRPVPLLMQYLLNKAS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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C4LA51
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MEFGVKSGSPEKQRSACIVVGVFEPRRLSAVAEQLDRVSDGYLSSLLRRGDLEGKTGQMLLLHQVPGVLSERVLLVGCGKERELDERQFKQIIQKTISTLNETGSMEAVCFLTELHVKGRDAYWKVRQAVETAQNSLYTFDQFKTNKAELRRPLRKLVFNVATRRELSIGEKAIAHGLAISNGMKICRDVANMPPNICTPAYLASQARRLADSCQYITTKVIGEQQMAELGMNAYLAVAKGSSNEAMMSVMEYKGHPDAKPIVLVGKGLTFDSGGISIKPAEGMDEMKYDMGGAASVLGTMTALAELKPPINVIGVLAGAENMPDGKAYRPGDILTSMSGQTIEVLNTDAEGRLVLCDVLTYVERFEPESVVDIATLTGACVIALGSHASGLMSNHNPLAHELLNASELSGDKAWRLPLWDEYQEQIESPFADMVNTGGRPAGAITAGAFLSRFTKKYNWAHLDIAGTAWKSGKEKGSTGRPVPLLTQFLLNRAGVEVED
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q73QZ3
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MKFNIAKKGGVVAQLVFEEKIEGGYLNHLKEKELFSGKAEDVYYTLDSNLKAQLFIGLGKEEKIDLEVLRKTFFKAASELLKNKVEEVELNIPKLNNLCNYKTAEAIAEGMLHATYKYDKFKSDRKEQTEITVNYNPEKGKEDRAEKGINEAVKLMEAVFLTRDLVNQPANVIYPETLAKIAKEKLEAKGVKVTVHGKKEIEALKMEAFLNVARASTKEPKLIVMEYYNNPGSNEKIALVGKGLTYDSGGYAIKPATSMVDMFTDMGGSGTVIGAMHALADLKAKVNVVAVVASCENMISGDGYRNGDIIGSMSGKTIEIINTDAEGRLTLADAVYYATNNLGATKLIDLATLTGACVSALGEQVSGAVTNNDEFFSELVKANERAGEIVWRMPTIEYYKKMNESKVADLKNSGGKLGGMMTAGLFVGSFLAKEDIPWIHIDIAGTAYITEKFGYLKENATGTLVKSLYYMLSKEA
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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Q11A96
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MEIKVGNIPQLKWAGDALAIGLFEDAIKLTEDAIELTEEMAELDEMLSGTLSELIKETEFKGKANSSVSTRVGIKTSIRKIIVVGLGKLEKFKLDSLRQAAATCGRLAKKERCKTLGISLPMCQDADSTAIAITEGIELALHQDNRFKSEPENLGPDLEKVELIGLAASDEAIAHARKICSGVIFARELVAAPANSCTPITMAETAQTLAKEFGLTLEILEKEDCEKLGMGAFLGVAQGSDLPPKFIHVTYKPEVTPRRKLAIVGKGLTFDSGGLNLKVSGSGIEMMKIDMGGAGTTFGTIKAIAQLKPDVEVHFISAVTENMVSGHAIHPGDFLTASNGKIIEVNNTDAEGRLTLADALVFAEKLGVDAIIDLATLTGACVVALGNDIAGLWSPNDNLAAEITAAAEKAGEKMWRMPLEEKYFEGLKAMHADMKNTGPRPGGAITAALFLKQFVKNTPWAHLDIAGPVWVDTENGYNNQGATGYGVRTLVNWILS
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Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. Binds 2 manganese ions per subunit. Belongs to the peptidase M17 family.
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C1GEY4
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METVDTSQRLARLRELMKERNVDVYLVPSEDSHQSEYIAPCDGRREFISGFSGSAGCAIVSMTKAALSTDGRYFNQASKQLDNNWLLLKRGIESMPTWQEWTAEQLEGGKVVGVDPSLITASDARSLSETIKRSGGSLLGVQENLVDLVWGKDRPCRPSEKVTVHPVEFAGKSFEEKITDLRKELEKKKSAGFVVSMLDEVAWLFNLRGNDIPYNPVFFSYAIITPSTADLYIDEEKLSADVKKHLGDKVSLKPYTSIFEDAKALGQSAQAEVNGGASDPPRKFFISTKASWSLSLALGGANKVEEVRSPISDAKAIKNDTELEGMRACHIRDGAALTKYFAWLENELVNKKTVLNEVEASDKLEEIRSKQKNFVGLSFDTISSSGPNAAVVHYKAERNNCSIIDPEAVYLCDSGAQYLDGTTDTTRTLHFGEPTEKERKAYTLVLKGMIAIDTAIFPKGTTGFSLDTLARQFLWKEGLDYLHGTGHGVGSYLNVHEGPIGIGTRVQYSETPLSVGNVISDEPGYYEDGKFGIRIENIIMAREVKTTFSFGERPWLGFEHVTMTPLCRKLTDPSLLNDAEKKWINEYHSEVWEKTSGYFAEDELTRNWLKRETQPI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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C0SCV1
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METVDTSQRLARLRELMKERNVDVYLVPSEDSHQSEYIAPCDGRREFISGFSGSAGCAIVSMTKAALSTDGRYFNQASKQLDNNWLLLKRGIESMPTWQEWTAEQLEGGKVVGVDPSLITASDARSLSETIKKSGGSLLGVQENLVDLVWGKDRPCRPSEKVTVHPVEFAGKSFEEKITDLRKELEKKKSAGFVVSMLDEVAWLFNLRGNDIPYNPVFFSYAIITPSTADLYIDEEKLSADVKKHLGDKVSLKPYTSIFEDAKALGQSAQAEVNGGASDPPRKFFISTKASWSLSLALGGANKVEEVRSPISDAKAIKNDTELEGMRACHIRDGAALTKYFAWLENELVNKKTVLNEVEASDKLEEIRSKQKNFVGLSFDTISSSGPNAAVVHYKAERKNCSIIDPEAVYLCDSGAQYLDGTTDTTRTLHFGEPTEKERKAYTLVLKGMIAIDTAIFPKGTTGFSLDTLARQFLWKEGLDYLHGTGHGVGSYLNVHEGPIGIGTRVQYSETPLSVGNVISDEPGYYEDGKFGIRIENIIMAREVKTTFSFGERPWLGFEHVTMTPLCRKLIDPSLLNDAEKKWINEYHSEVWEKTSGYFAEDELTRNWLKRETQPI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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B6HQC9
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MGAVDTSERLSKLRQLMQQHKVDVYIVPSEDSHQSEYIAPCDARREFISGFSGSAGTAIISLSKAALSTDGRYFNQAAKQLDNNWQLLKGGVEGVPTWQEWTTEEAQGGKAVGVDPSLITASGARKLAETLKKNGSSLVGVRENLVDLVWGKERPARPSEKVRVHPEKYAGKTFQEKVAELRKELESKKKAGFVISMLDEIAWLFNLRGTDIPYNPVFFSYAVITPTTAEIYVEDDKLTPEVKAHLGQDVVVKPYESIFADAQALSTKSQSAGENAAKFLLSNKASWALSLSLGGEGQVEEARSPVADAKAIKNETELEGMRACHIRDGAALTEYFAWLENELINKKTVLDEVDGADKLEQIRSKHDLFAGLSFDTISSTGPNGAVIHYKPEKGSCAIIDPSAIYLCDSGCQYFDGTTDTTRTFHFGVPTEFEKRAFTLVLKGTIGIDMAVFPKGTSGFAIDVLARQHLWREGLDFLHGTGHGVGSYLNVHEGPIGIGTRVQYTEVPIAAGNVISDEPGYYEDGKFGIRIENIVMAREVKTAHNFGDKQWLGFEHVTMTPIGRNLIEPSLLSDAELKWVNDYHAEIWAKTEHFFREDNLTRSWLERETQPISK
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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Q0UFY4
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MPRDALSFELQLSAGLEATEHKLDMLTRLLRRTHVAVKHPLLASRAFHTSPALRAIDMAKVDTTERLAELRKLMKERKVDVYTYISGFTGSAGYAVVTHDKAALATDGRYFNQAEKQLDSNWELLKQGIQDVPTIQEWTADQVEGGKVVGVDPSVVTGADARKLAEKIKKKGGEYKAVDDNLVDLVWAAERPARPSEKVIVQPMEYSGKSFDEKVEDLRKELEKKKSLGFVVSMLDEVAWLFNLRGNDIPYNPVFFSYAVITPTVVTLYVDESKLPKEVKDHLGDKVAIRPYEAIFGDITALSKDAFEAADADATKKFLTSNRASWALNKALGGDDKVEEIRSPIGDAKAVKNEVELEGMRQCHIRDGAAISEYFAWLEDQLLNKKATLDEVDGADKLEAIRKKHDKFMGLSFDTISSTGPNGAVIHYKPEKGACSIIDPNAIYLCDSGAQYHDGTTDTTRTLHFTKPTDMEKKAYTLVLKGNIALERVKFPKGTTGFALDSIARQFLWAEGLDYRHGTGHGVGSFLNVHEGPIGIGTRVQYSEVSLAVGNVISDEPGYYEDGKFGIRIENMIMVKEVETNHKFGDKPYLGFEHVTLTPHCRNLVDMTLLTEDEKKFINDYHKEVFEKTSKFFENDKLTMDWLKRETAPY
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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A0A090CXB1
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MRHIWALPSLTALSLFQASAASAVPRARQAINTSSPLAPFRTKRRFRTQAQLLSNSATKTTLVEEMVTVDTTSRLAALRSLMKERNLHVYVVPSEDSHASEYIADCDARRTFISGFSGSAGTAIVTLDKAALATDGRYFNQASKQLDSNWYLLKTGMQDVPTWQEWATQEAEGGKLIGVDPQLISSAIAEKLDEDIKNAGGGGLVGIKENLVDLVWGSEQPPRPSNSVFLLGQQYAGKDTAAKLADLRKELDKKKAAGFVLSMLDEIAWLFNLRGSDIAYNPVFFSYAIVTQASATLYIDEAKLTDECKTYLERNKVTIKPYGALFEDSEELARRAEADSKDAKPRKYLISSKGSWALKLALGGNKFVDEVRSPVGDAKAVKNDVELNGMRNCHIRDGAALTEFFAWLEDQLVNQKAQLDEVDAADKLEQIRSKHKDFVGLSFDTISSTGANAAVIHYKPEKGACKIIDPNAIYLCDSGAQYLDGTTDTTRTLHFGTPTAKEKKAYTLVLKGNIALDSVVFPKGTSGFAIDVMARQFLWKYGLDYRHGTGHGVGSFLNVHEGPIGIGTRKQYIDVALAAGNVLSIEPGYYEDEAFGIRIENLAIVKEVKTEHSFGDKPYLGFEHVTMVPYARNLIDETLLTPDEKDWLNRANKKILEKTLGYFENDPLTKAWLLRETQPF
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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B2VUU7
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MAKVDTSHRLAELRKLMKERNVDIYTYISGFTGSAGYAVITHDKAALSTDGRYFNQAEKQLDSNWELLKQGIQDVPTIQEWTADQAEGGKVVGVDPSVVTAGDARKLAEKIKKKGGEYKAIDENLVDLVWSSERPARPSEKVIVQPERYACKGFEDKIDDLRKELEKKKSLGFVVSMLDEVAWLFNLRGSDIPYNPVFFSYAVVTPTAATLYVDENKLPEDVKEHLGNKITIRPYEAIFGDVTALSKELFEASDKNETQKKFLTSNRASWALNKALGGDDKVEETRSPVGDSKAVKNEVELEGMRQCHIRDGAALSEYFAWLEDQLINKKATLDEVDGADKLEEIRKKHDMFMGLSFDTISSTGANAAVIHYKPEKGECATIDPKAIYLCDSGAQYRDGTTDTTRTLHFTEPTEMERKAYTLVLKGNMALERVKFPKGTTGFALDALARQFLWAEGLDYRHGTGHGVGSFLNVHEGPIGIGTRVQYSEVSLAVGNVVSDEPGYYEDGKFGIRIENMVMVKEVETKHKFGDKPYLGFEHVTMTPHCRNLVDMSLLTEDEKKFINEYHKEVYEKTSKYFENDALTLEWLKRETAPY
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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E3S7K9
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MLLPRIPQLSHATRAAYVAAKSPFSPVPVRPFHASAALRAIDMAKVDTTHRLAELRKLMKERNVDIYMVPSEDSHQSEYIAPCDARRAYISGFTGSAGYAVITHEKAALSTDGRYFNQAEKQLDSNWELLKQGIQDVPTIQQWTADQAGGGKVVGVDPSVVTAGDARKLAEKIKKKGGEYKAIDENLVDLVWGSERPARPSEKVIVQPKKYAGKGFEDKIDDLRKELEKKKSLGFVVSMLDEVAWLFNLRGSDIPYNPVFFSYAVVTPTTATLYVDENKLPEDVKEHLGDKITIRPYEAIFGDVTALSKELFEANDKNETQKKFLTSNTASWALNKALGGDDKVEETRSPVGDSKAVKNEVELEGMRQCHIRDGAALSEYFAWLEDQLINKKATLDEVDGADKLEEIRKKHDMFMGLSFDTISSTGANAAVIHYKPEKGECATIDSKAIYLCDSGAQYRDGTTDTTRTLHFTEPTEMERKAYTLVLKGNMALERVKFPKGTTGFALDALARQFLWAEGLDYRHGTGHGVGSFLNVHEGPIGIGTRVQYSEVSLAVGNVVSDEPGYYEDGKFGIRIENMVMVKEVETKHKFGDKPYLGFEHVTMTPYCRNLVDMKLLTEDEKKFINDYHKEVYEKTSKYFDKDALTLEWLKRETAPY
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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A7E4T8
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METINTTERLAALRDLMKKNKVDIYIVPSEDSHSSEYIAACDARREFISGFSGSAGCAVVTLDKAALATDDNWLLLKQGLQDVPTWQEWAAEQSESGKVVGVDSTIISAPDARKLLEKVKKRGGSDLVAVEENLVDLVWGDNRPSRPKEPVKVLARGFSGKDVKTKLEDLRKELQKKKSSGFIVSMLDEIAWLFNLRGSDIPYNPVFFSYASVTPSSATLYVDSSKLSEECITHLNDNGVSIREYSKIFSDVEVLSQSLDSEDAKLKKFLVSSRASWALKRALGGDAKVDEVRSPIGDAKSIKNETELEGMRACHIRDGAALIEYFAWLEHQLVVEKVEMDEVIAADKLEQLRSKQKHFVGLSFDTISSTGANAAVIHYKPEPGNCSIIDPKAVYLCDSGAQYFDGTTDTTRTLHFGEPTEMEKKAYTLVLKGNIALDVAVFPKGTSGFALDALARQFLWEEGLDYRHGTGHGVGSYLNVHEGPIGIGTRIQYSEVPLAPGNVISNEPGYYEDGSFGIRIENIIMVKEVETKHQFGDKPYLGFEHVTMVPYCRKLIDETLLTRREKHWLNEYHADIYSKTKDFFKGDELTMSWLEREIEPL
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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F7W9H7
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MTVNTTDRLAALRSLMKERSVDIYVVPSEDSHASEYITDCDARRTFISGFSGSAGTAVVTLDKAALATDGRYFNQASKQLDENWHLLKTGLQDVPTWQEWTADESAGGKTVGIDPTLISPAVAEKLNGDIKKHGGSGLKAVTENLVDLVWGESRPPRPSEPVFLLGAKYAGKGAAEKLTDLRKELEKKKAAAFVVSMLDEIAWLFNLRGNDITYNPVFFSYAIVTKDSATLYVDESKLTDEVKQYLAENGTEIKPYTDLFKDTEVLANAAKSTSESEKPTKYLVSNKASWALKLALGGEKHVDEVRSPIGDAKAIKNETELEGMRKCHIRDGAALIKYFAWLEDQLVNKKAKLNEVEAADQLEKFRSEQSDFVGLSFDTISSTGPNGAIIHYKPERGACSVIDPNAIYLCDSGAQFYDGTTDVTRTLHFGQPTAAEKKSYTLVLKGNIALDTAVFPKGTSGFALDALARQFLWKYGLDYRHGTGHGVGSFLNVHEGPIGIGTRKAYIDVPLAPGNVLSIEPGYYEDGNYGIRIENLAIVREVKTEHQFGDKPYLGFEHITMVPYCRKLIDESLLTQEEKDWLNKSNEEIRKNMAGYFDGDQLTTDWLLRETSPF
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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Q05813
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MAEELTPENPAIPETPEETEEPIKQRKNGLYPGVSDELAENMQSGWADTELHDLEPIAQAAETAARRAALSARFPGERLVIPAGNLKTRSNDTEYSFRASVEYAYLTGNQTEDGVLVMEPEGDGHAATIYLLPRSDRENGEFWLDGQGELWVGRRHSLAEAGELYGIPASDVRELAGSLREATGPVRVVRGFDAGIEAALTDKVTAERDEELRVFLSEARLVKDEFEIGELQKAVDSTVRGFEDVVKVLDRAEATSERYIEGTFFLRARVEGNDVGYGSICAAGPHACTLHWVRNDGPVRSGDLLLLDAGVETHTYYTADVTRTLPISGTYSELQKKIYDAVYDAQEAGIAAVRPGAKYRDFHDASQRVLAERLVEWGLVEGPVERVLELGLQRRWTLHGTGHMLGMDVHDCAAARVESYVDGTLEPGMVLTVEPGLYFQADDLTVPEEYRGIGVRIEDDILVTADGNRNLSAGLPRRSDEVEEWMAALKG
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Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Homodimer. S.lividans has two genes (pepP1 and pepP2) which encode aminopeptidase P. Belongs to the peptidase M24B family.
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B6QG01
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MLFLCRASPLLQRTALSSPLRFFAPPKSSFNRTFANTAVRLSIEMETVDTSERLVQLRELMKRNNLDVYIVPSEDSHQSEYIAHCDARREFISGFTGSAGTAVISSTAAALSTDGRYFNQAAKQLDSNWTLLKRGLEGVPTWQEWTTEQAEGGKTVGVDPSVITAASARKLSETLEKSGSKLIGIEQNLVDQIWGDKRPARPNETVKIHPAEYAGKPFQEKIADLRKELKTKKRAGFIVSVLDEIAWLFNLRGNDIPYNPVFFSYAVITPETVDLYINDEKLSPEVKAHLGSDVVVKPYESIFADARALSVNAPLTENGSPMKYLTSNKASWALSLSFGGEKKLDEARSPISDAKAIKNEVELKGMRNCHIRDGAALSEYFAWLENELINKKSTLDEVDGADKLEQIRSKHDKFVGLSFDTISSTGPNAAVIHYKPEKGICSVIDPNAIYLCDSGGQYLDGTTDTTRTFHFGTPTEMEKKAFTLVLKGLIALDTAVFPKGTSGFALDALARQHLWRYGLDYLHGTGHGVGAYLNVHEGPIGVGTRIQYSEVSLSPGNVISDEPGYYEDGKFGIRIENIIMAREVETPYKFGEKSWLGFEHVTMTPIGQNLIETSLLSEEERQWVNNYHAEVWEKTSGYFKQDELTLNWLKKETKPLK
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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B8M9W2
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MLFSCRAPSLLQRTALSSPLRLFAPCRPSFSRTFVTTTVRFSVEMETVNTSERLAQLRELMKQNNLDVYIVPSEDSHQSEYIAHCDARREFISGFTGSAGTAVISTTAAALSTDGRYFNQAAKQLDSNWKLLKRGLEGVLTWQEWTAEQAEGGKIVGVDPSVITAASARKLSETLEKGGSKLVGIEQNLVDQIWGTHRPQRPSEKVKIHPIEYAGKPFQEKIADLRKELKTKKRAGFIVSVLDEIAWLFNLRGNDIPYNPVFFSYAVITPDTVDLYIDDEKLSPEVKVHLGSDVVIKPYESIFADAKALSAKAPLTESGAPMKYLTSNKASWALSLSFGGEKKLDEARSPISDAKAIKNEVELKGMRDCHIRDGAALTEYFAWLENELINKKSTLDEVDGADKLEQIRSKHDKFVGLSFDTISSTGPNAAVIHYKPEKGVCSVIDPNAIYLCDSGAQYLDGTTDTTRTFHFSTPTEMEKKAFTLVLKGLIALDTAVFPKGTSGFALDALARQHLWRQGLDYLHGTGHGVGAYLNVHEGPIGVGTRIQYSEVSLSPGNVISDEPGYYEDGKFGIRIENIIMAREVETPYKFGDKPWLGFEHVTMTPIGQNLIETSLLSKEERQWVDNYHAEVWEKTSGFFKQDELTLNWLKKETQPLK
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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D4D891
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MTIFRPHLRFLFKPHFLYFQSPAGQSSRPFSTSQILRTALDMPPPPVDTTQRLAKLRELMAQNKVDVYSMQFRYTIKAPLIITVVYSFFFFLLLALKLCLRKTAISQSTLLHVMGVETLIRITAAFISSFTGSAGCAIVSMSKAALSTDGRYFSQAAKQLDSNWTLLKRGVEGVPTWEEWTAEQAENGKVVGVDPSLITAGENLHYTPLTSVVVTNCSYVIADARKLSQTLKTTGGSLVGIDQNLIDAVWGNERPARPANQITVQPVERAGKPFEEKVEDLRKELAAKKRSAMVISTLDEIAWLFNLRGSDIPYNPVFFSYAIVTPSVAELYVDESKLSPEARKHLEGKVVLKPYDSIFQASKVLAESKASASSGSSGKFLLSNKASWSLSLALGGEQNVVEVRSPITDAKAIKNEVELEGFRKCHIRDGAALIEYFAWLENALIKEGAQLDEVDGADKLFEIRKKYDLFVGNSFDTISSTGANGATIHYKPEKSTCAVIDPKAMYLCDSGGQYLDGTTDTTRTLHFGEPTEFQKKAYALVLKGHISIDNAIFPKGTTGYAIDSFARQHLWKEGLDYLHGTGHGVGSFLYAEVPLSASNVLSNEPGYYEDGNFGIRLENLVICKEVQTAHKFGDKPFLGFESITLVPFCQKLLDASLLTEAERKWVNDYHARVWEKTSPFFEKDELTTAWLKRETQPI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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D5GAC6
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METVDTTSRLAKLRELMKRERVDVYVVPSEDAHSSEYICAADARRAFISGFTGSAGCAIVTQEKAALSTDGRYFNQAARQLDENWELLKQGLPDVPTWQEWVAQQAEGGKNVGVDATVITAQQAKSLETRIKKKGGTSLLGIPNNLIDEVWGADRPNRPNNPVMVLDEKYSGKEFPLKIEAVRKELENKKSPGFVVSMLDEIAWLFNLRGTDIPYNPVFFSYAFISPESTTLYIDSSKLDEKVIAHLGSAVKIRPYHEIFDEIDLLAQKLKVGQPETDSKASEDGGKWLVSNKTSWALSKALGGDDAIEVIRSPVEEEKAVKNDTEKEGMKRCHIRDGAALTEYFAWLEDELLKGTKIDEVQAADKLEQIRSRGENFMGLSFDTISSTGPNAAVIHYKPEAGNCSVIDPKAIYLCDSGAQYLDGTTDTTRTLHFGEPTDMERKSYTLVLKGMIALDRAIFPKGTSGFALDILARQFLWSEGLDYRHGTGHGVGSFLNVHEGPFGIGTRIQYSEVALSPGMFVSNEPGYYEDGSFGIRIENIIMVKEVKTSHSFGDRPYFGFERVTMVPMCRKLIDAGLLTPAETEWLNSYHAEVFEKTHGFFEKDSLASKWLKRETTPI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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C9SR45
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MEKVDTSGRLSKLRELMRAHSIDVYVVPSEDSHSSEYIAACDARREFISGFSGSAGCAVITLDKAALATDGRYFNQASKQLDHNWLLLKQGLQDVPTWQDWSAEQSAGGKIVAVDPELIAAAAAKKLAAKIHKFGGSELVALERNLVDVVWGKDRPDRPRNPVVILDTAFSGKNVETKLRDLRQELVKKDSLGMVVSMLDEVAWLLNLRGSDIPYNPVFFSYAVITLDTATLFVDDTKLHPDSLEYLRKNGIVTKPYSCIFDDVKALTSSKGVQGREKRTLLSSKASWALKRALGGDDLVEEVRSFIGDAKAVKNEAELAGMRACHIRDGIALIEYFAWLEDQLVAKRIVLDEVEAADKLEELRQKQENYVGLSFDTISSTGANAAVIHYKPERGSCPAIDPEAIYLCDSGAQYLDGTTDVTRTVHFGCPTAAEKLAYTLVLKGNIALDSAIFPKGTTGFALDCLARQHLWREGLDYRHGTGHGVGSYLNVHEGPIGIGTRVQFAEVSLASGNVVSIEPGFYEDGAFGIRIENLAIVREVQTQHSFGDKPYLGFEHVTMAPYCKNLIDISILTTAEKEWLNAHNTDIFNKTKDAFKDDALTLAWLTRETQPI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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C0NF18
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MGPPLAQELTQACNQPLAATSNLQPDDGYKIELRAENTVDKYPAKQHARRVAAQIRQGKGLIFLMGQKSTLHEDSDQERSLRQRRYFFYLSGVDEADCDLTYDIKTDKLTLYVPDFDLRRAIWMGPTLERKAALQKFDVDEVNYHSSLDEDVKKWAKNQDPGSTIYLLHGSQGPAENPPNVIIDSKALKLAMDACRVIKDEHEIQLIRRANDISAAAHLEILRGITSMSNESHIEGSFLNTCVSLGAHNQAYQIIAASGSNAATLHYSKNNEPLKGRQFVCLDAGAEWNCYASDVTRTFPITHQWPSIEAKQIYQLVQEMQESCIALVKEGVRYLDLHFLAHNILIKGFLTLGIFKGGTLDEVKKSGASLLFFPHGLGHHIGLEVHDVSPQSIMAQGINDDSNNKLILPTCVSPCTTSSPALTSGMVITIEPGIYFSQLALDNAKPEQLKYIDMARVKNYMAVGGVRIEDDILVTKTGHENLTKVPKGDDMLEIIRQGKKGNDSHHV
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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C6HNY5
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MAIYSQVPWTLPRYKFEVKVHPLAATSNLQPDDGYKIELRAENTVDKYPAKQHARRVAAQIRQGLGLIFLMGQKSTLHEDSDQERSLRQRRYFFYLSGVDEADCDLTYDIKTDKLTLYVPDFDLRRAIWMGPTLERKAALRKFDVDEVNYHSALDEDVKKWAKNQDTGSTIYLLHGSQGPAENPPNVTIDSKALKLAMDACRVIKDEHEIQLIRRANDISAAAHLEILRGIKSMSNESHIEGSFLNTSVSLGAHKQAYQIIAASGSNAATLHYSKNNEPLKGRQFVCLDAGAEWNCYASDVTRTFPITHQWPSIEAKQIYQLVQEMQESCIALVKEGVRYLDLHFLAHSILIKGFLTLGIFKGGTLDEVKKSGASLLFFPHGLGHHIGLEVHDVSPQSIMAQGINDDSNNILILPTCVSPCTTSSPALISGMVITIEPGIYFSQLALDNAKPEQLKYIDMARVKNYMAVGGVRIEDDILVTKTGYENLTKVPKGDDMLEIIRQGKKGNDSPCVDRPTW
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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A6QYF6
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MGPPLAQELTQACNQPLAATSNLQPDDGYKIELRAENGVDKYPAKQHARKVAAQIRQGKGLIFLMGQKSTLHEDSDQERSLRQRRYFFYLSGVDEADCDLTYDIKTDKLTLYVPDFDLRRAIWMGPTLERKSALQKFDVDEVNYHSALDEDVKKWAKNQGPGSTIYLLHGSQGPTDNPSNVIIDTKTLKLAMDACRVIKDEHEIQLIRRANDISAAAHIEILRGITSMSNESHVEGSFLNTCVSLGAHKQAYQIIAASGSNAATLHYSKNNEPLRGRQFVCLDAGAEWNCYASDVTRTFPITHQWPSIEAKQIYQLVQEMQESCIALVKEGVRYLDLHFLAHNILIKGFLTLGIFKGGTLDEVKKSGASLLFFPHGLGHYIGLEVHDVSPQSIMAQGINDDSNNMLILPTCVSPCTTSSPALTSGMVITIEPGIYFSQLALENAKPEQLKYIDMARVKNYMAVGGVRIEDDILVTKTGHENLTKVPKGDDMLEIIRQGKKGNDSHHV
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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C5GKT2
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MISAIEPKNLLRPHSQPVVTTSTLQPDDECNIELRIEDTTVDKYPAKQHARRVAAEIHRDRGLVYLMGQKSTLYEDSDQERTFRQRRYFFYMSGVDEPDCDLTYDINADKLTLYVPDFDLKRTIWMGPTLGREEALQRFDIDEVKYQSSLDEDVKQWAQNQGRGSTLYLLHESQKPAEKVPNVFIDSKTLKHAMDTSRAIKDEHEIGLIRRANEVSAAAHIDVLRGIRKMSNERDIEASFLNTSVSLGAHKQAYHIIAASGSNAATLHYSKNNEPLKGRQFVCLDAGAEWNCYASDVTRTFPMTSQWPSAEAKHIYKLVEHMQESCIVRVKEGVRYLDLHILAHRSLIRGFLTLGIFKGGTLEEIQNSGASNLFFPHGLGHHIGLEVHDVSPESIMAQDNGDYSDNVLISPNNLSPCTTSSPTLKSGMVVTIEPGIYFSQIALDNAKPEQLKYVDLELVKTYMPVGGVRIEDDILVTKTGYENLTTAPKGDGMLEIIRQGDGSCNI
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Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Binds 2 manganese ions per subunit. Belongs to the peptidase M24B family.
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Q8TL01
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MRLNLEHFDIKIGQHKVMFNVADAKELGVNPGDRVRIRGHQSISAIVDTTEDMVPPGTLGVFSEVYEHFEDWDKPVEVVPALRSKSSGVIKKMLDKKSVLQDEIKLLVNDIVEENLSDVELSAFITASYIHGMTDDEVEWLTRAMIDTGDTIEFDTHPVMDKHSIGGVPGNKISLLVVPIVAANGLLIPKTSSRAITGAGGTADLMEVLSPVEFSSEEVKEIAEKVGGALVWGGATNIAPADDKLIRVEYPLSIDPYYQMLASIMAKKGAIGAENVVMDIPIGPSTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRRVGPCLEVREAMKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDRGKELALETLRNGKALEKMKQIIEAQGGDPNIKSDDIQVGQYTADIYASTDGYVIEFDNKWIIEIARLAGAPNDKGAGVAIHKKMGEQVKKGDAILTIYAEKEFKLDLALTTAQRTNPIIVEGMLLKRIPGIYGFQ
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q0W5A8
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MKLRAQPYDIEVGRYEVIINSADAEELGVLAGDRVQVKDKDTITAVVETTDAIVSPGKIGIYREAWESIKVVPDEVVEVLPAAKPKSVSFIRKKMDKQKLTSEEMHAIIEDIVDGNLTEVELTAFVTASYIYTMDSDEIEWMTRAMVKTGDQISFDVHPVMDHHSIGGVPGNKISLCIVPIIAAAGLLIPKTSSRAITGAGGSADLMEILCPVSFRADEIKKMTTKVGGCLVWGGATNIAPADDKIINVEYPLSIDPKSQLLASVMAKKFAVGADTMVLDIPCGNETKIPTVQEGRKLARDFMELGDRLGMKIECALTYGGTPLGRAIGGGVEVREAMVMLEKFEGPRSLLEKTIAISGMMLEMGGVAPKNEGAKMAVELVKSGKALQKFKEIIEVQGGDPKVTSDMVPIGDKVATVLSPQDGYVLEISNKRLVYMCRLAGAPHDKGVGVILHKKKGEYVKKGDGLFTLYADKEWKLDAAIKESLRNPIMMVEGMILEKIEVV
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A7I5N0
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MKYSVRILDIATRSGILLNYLDARNIGVLDGDRVQLINPKNSLAVTAVVTTTSTLEGQGTAGVYRGTNRRLNLTEGEEIEIREADRPASLDFIKKKMDGGRLTKEETLTIIKDVVNDEISAAELTAFITASYINPLDMEEVEHLTRAMVETGERIKFASRPIVDKHSIGGVPGNKISLLVVPIIAASGLKIPKTSSRAITGAGGTADLMEVLANVEFSAREVQEMTEKVGGTIVWGGATNIAPADDRIILQEYPFKIDARGQMLASVMAKKYAVGANLVVIDIPVGSHTKVPTVQEGRKLAREFIELGERLGMKVECALTYGDIPVGYSIGPNLEVREALRVLEGATEPNSFIQKSVSLAGIALEMSGKAARGTGAQMAQDILSSGKALEKFRQIIEIQGGDPKVKSEDILPGEHQFVVNAPASGYIVEMNNVSLITLARLAGAPHDRGAGILLHAKKGTLIKAGEPLFTIYAEREWRLQKAVEEGRHLVPVLVEGMLLDRVPSQSEV
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q466X0
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MQLKLEHFNIKIGQHKILLNIADAKELGVNPGDRVRIRGRESISAIADTTDDMVPPGTLGVFSEVYEHFVNWDKPVEVVPAFRSKSASVIKKMMDKKPVVQEEIKTLVNDIVEENLSEIELSAFITSSYIHGMTDDEVEWLTRAMIESGDTIEFDTHPIMDKHSIGGVPGNKISLLVVPIIAANGLLIPKTSSRAITGAGGTADLMEVLCPVEFSSQEVKEITEKVGGALVWGGATNIAPADDKLIRVEYPLSIDPYYQMLASIMAKKGAIGADNVVMDIPVGPSTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRKVGPSLEVREALKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDRGKEIALETLRSGKALEKMKQIIEAQGGDPKITSADIQVGQYTADILASADGYVIEFDNKWIIEIARLAGAPNDKGAGVAIHKKMGESVKKGDPILTIYAEKEFKLETALATAQRTNPIVVEGMLLKRIPGTYGFQ
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q12Z64
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MQLKVQPIDVKVGKYKVILNTIDAKELGVHEGDRVRIKNHVTLTAIVDFTEDMISPGMIGLYHEVKEALSKEWTETVEVFPAEKPKSTYIIRKTMDGQKLTKEEIDILVKDIVEENLAEIEIAAFLTATYINDMTDDETEWLTRAMIDSGDKLEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEILAPVEFDAAEIKRMTEEVGGVLVWGGATNIAPADDKLIKVEYPLSIDPHCQMLASIMAKKGAIGADHVVMDIPTGPGTKIKNVQEGRKLARDLINLGDRLGMDVDCALTYGASPVGRTIGPALEVIEALKVLESFEGPNSLIEKSASLAGMLLEMGNVAGKDKGYDLAIETLKNGKALTKFKEIIKIQGGNPDVTHKDISVGEFTEDIIAPNNGYILEMDNKRLVQIARLAGAPNDKGAGILLHRKQGEPLKEGDPVMTIYAEKKSKLENAVKSAKERPPFIVEGMMLERIQSFKEI
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q2FTS5
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MRLTVRLVDIAARGILLHHNDAKSLGVLAGDRIVISSPVTGKATVDYVETTGTLIDQGRIGVYHHTNEQLTLTENEVVEVRVADRPVSLDYIKKKMEGEKLTREDIRAIVADIVQDTLSPSEITAFVVSSYINQLDMDEIESLTRAMVETGDQLSFHAGPIVDKHSIGGVPGNKISLIVVPIIAASGLLIPKTSSRAITGAGGTADLMEVLAPVEFSASEVQEMTIKTGGVIVWGGATNIAPADDKIIIQEYPFKIDQIGQMIASVMAKKFAVGADVVAIDIPVGKYCKVHTIEEGKKLARQFIDLGERLNMRVECALTYGDAPVGRAIGPKLEIKEALSVLEGSDSPRSLIQKSCVIAGIALELAGKANRGEGANLALEILRSGKALKKFLDIIAVQGGTPDVSSEKITVGEHFYTVRADSTGYVIDLNNHSLITIARTAGAPADHGAGLYLHAKHGTSLSKGDPIFTIYADRKWRLEKAIEEARRLRPVMVEGMLIDRVPNVREWVPGRSRNLE
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q58081
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MLFLKVRVLDIDLENLVLINSEDLKSSQYFPQDRVVVEFKGKEVIGILHSSTTLINRGEIGLPQKVVKELGVKEGDIVTIKHAEKPKSLPYIRKKMDGNKLKKEEIFEIIDEMVDGKLTNIEISAFVTSLYINGMDMDEIEAMTIRMAETGEMVNWEGHIFDVHSIGGVPGNKYALLVVPIVASAGLKIPKTSSRAITSAAGTADVVEVLTRVDLTIEEIKRVVKETNGCMVWGGALDLAPADDITINVERPLGIDPEPLLLSSVMAKKLAMGVNKLLIDIPTGYGAKVKSIKEASSLARKFIELSDRLRIVTECAITYGGQPIGRAIGPALEAKEALLALEDYTQAPTSLVEKSISLAGILLEMGGVAPTGEGKELAEDLLARGKAHDKFMEIIVAQGGKEVSSDEIEVGKYKADIHSPIDGYVTRISNAGITKIAKEAGAPNDKKAGIYLNVKVGNKVEKGDVLYTIYSDSEERLKSAIKLARILYPIKVEGMLLQKISRF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A2SPI9
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MNLILDMIDISTPVILLNDTDARQIGVLEGDRVTITRIKTKHTIAAPVSITKTLTSQGTATISLGTNENLAAEKGDEIEIRAAPRPASIAFIRKKMDGGKFTREETATIISDMSSNVLSPSEITAYITAAYINGLDMDEVEFLTREMVASGEQITFSKKPVVDKHSIGGVPGNKITLLVVPVIAASGLLIPKTSSRAITGAGGTADLMEALAPVAFSAAEIKTMTEKAGGVIVWGGATNIAPADDMIVTYEYPLKIDARGQMLASIMAKKMAVGSDTCVIDIPIGPGTKIPDEAEGRVLANELITLGNRLGIRVECAVTFGGSPIGRNIGVNLEVSEALSLLEGKRGANSLVQKSVAIAGIALEMTGKTGADSGAEAAYDIIKKGKALKKMLDIIEIQGGDPKVKSTDFPVGEHTFVVPAASDGYVVSVKNQALISIARAAGSPVDHGAGLHLHKKPGEYVKRGEPLLTIYAERGWRLTRAIEEARTSYPVLVEGMLLERISSNR
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A4FZL0
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MLFLNAKFIDLDLGENAVIVNEEDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVNKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMIAWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITVPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGESLNIKVECVLTYGGQPLGRAIGPALEAREAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGKALEKFNQIITEQGGTPKKPEEIELGDYVEEILAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNKVKQGDVLYTIYSGSEERLVSAINLARRVYPVKVEGMLIERISKF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A9A6M7
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MLFLNAKFIDLDLGENAVIVNDEDLKGTSYYPQDRVLIESHAGAVIGNIYSTKTMVKKGEVGMLVKELKEVSISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAREAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQKLAWEILESGRALEKFNQIITEQGGTPKKPEEIELGEYVEEIIAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNQVKQGDILYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A6VIW6
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MLFLNAKFIDLDLGESAVIVNEEDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELSEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEISEMTKRIAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITVPKTSSRAITSPAGTADVMEVLTNVELKEEEIKRIVKTTNGCLAWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYTVIDIPVGKGVKIKNEAEGAKLARKFIELGEMLNIKVECVLTYGGQPLGRAIGPALEAKEAIESLQDPKNAPKSLIEKSLSLAGILLELGGAAQIGEGQNLAWEILESGKALEKFNQIIVEQGGTPKKPEEIELGEYVEEILAPIDGYITDISNTAITNVVKEAGAPRDKKAGILLNSKIGNKVTQGDVLYTIYSGSEERLISAVNLARRVYPVKVEGMLIERISKF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q8Q0P9
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MMQLKLEHYNIKIGQHKVLLNIVDAKELGVNPGDRVRIRGHQSLSAIVDTTDDMVPPGTLGVFTEVYEHFEDWDKPVEVVPSFRSKSAAVIKKMLDKKPVVQDEIKMLVSDIVDENLSDVELSAFITASYIHGMTDDEVEWLTRAMIDTGDTIEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEVLSPVEFSSQEVKEITEKVGGALVWGGATNIAPADDKLIKIEYPLSIDPYYQMLASIMAKKGAIGADNVVMDIPVGPGTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGSSPIGRRVGPSLEVKEAMKVLESMEGPNSLIEKSAALAGILLEMGGAAPRDQGKELALETLRSGKALEKMKQIIEAQGGDPNIKSDDIQTGQYTADIFASTDGYVMEFDNKWIIEIARLAGAPNDKGAGVAIHKKRGEQVKKGDPILTIYAEKEIKLDNALATAQRTNPIIVEGMLLRRIPGTYGFQ
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A3CSY4
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MKLTVKLLDIENRGVLLHCTDARSMRVRDGDRVQIVDEATGKTAQAHVDTTGSLIEPGVIGVYRPVNATLAVDEGTPVEVRGAERPASLEHIKKKMDGGRFTKDDTVDIVRDIVDDVLSPGEITAYVTASYINGLDMDEVEYLTRATVETGERLHFTRHPIVDKHSIGGVPGNKITLLIAPIIAASGLLIPKTSSRAITGAGGTADLMEVLAPVSFPALEVQQMTEKVGGAIVWGGATNIAPADDKIITYEYPLRIDARGQMIASVMAKKFAVGADLVVIDIPVGRNTKIATAQEGRKLAREFIDLGERLGMRVECALSYGESLVGHTIGPNLEVREALAVLEGATEPNSLIQKSLSLAGIALEMAGKAGPGQGARAAADILRSGKALEKMRQIIEIQGGDPNVKAEDIVPGECRFDVNAPQDGYVIELNNSALVTLARLAGSPYDHGAGLLVHAKKGTRVRKGDPIFTIYADREWRLERAIEVGRTLMPVLVEGMVLERIPHERWV
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q6M0E4
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MLFLNAKFIDLDLGENAVIVNEDDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEIGEMTKRIAETGDMISWEKNLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEDEIKRIVKTTNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYSVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAKEAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGRALEKFNQIIIEQGGTPKKPEEIELGDYIEEIIAPIDGYVTDINNTGITNVVKEAGAPRDKKAGLLLNSKIGNKVKKGDVLYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A0B6C9
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MFEVVPFDIEIGQYKVMLNIADARAMGLNPGDRVRVRTRGASLTAILDVTGQMIGQGQVGIFTEAFRDLKEAKSVEISPAPRPASISYIKMLMDRQKLSEDQIRSIVRDIVYNNLSEIELSAYITASYIHNLDPQETEWLTRAMIETGERIYFDKHPVVDKHSIGGVPGNKVSMLVVPIVAASGLLIPKTSSRAITGAGGTADLMEVLAPVEFTADEIKEITETVGGVIAWGGATNIAPADDRLIKAEYALAIDPYSQMLASIMAKKGAVGADAVVVDMPTGPGTKLETPEKARVLAKDLTDLGERLGIRVECAMTFGGSPVGRTVGPALEVREALKMLETGEGPNSLREKSLALAGILLEMGGVAARGEGYRAAEEILVSGKAHRKLMEIVEAQGGDPKIRSEDIQIGEHQKQILSPTNGYVVAFYNKRIIEIARAAGAPGDKRAGVIIHKKMGEIVKKGEPLLTICSSTDWELECAVKMCSMRDALEQPPIVVEGMLLERYPTERYPRTI
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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A6URW3
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MLFLNAKFIDLDLGANAVIVNEEDLKGTSYYPQDRVLIESHSGSVLGILYSTKTMVQKGEVGIPVRKMKGISLKEGEEVNLRHAEKPESIQFIKKKMDGQVLSPNEIRTIIDEIVSKKLSNIELAAFVTSTYVNGMNMEEIVEMTKRMAETGDMISWEKSLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELDEEELKRVVKATNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKVATGIKYAVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIRVECVLTYGGQPLGRAIGPALEAKEALEALTDPKSAPKSLIEKAISLAGILLELGGSAQIGDGQKLAWEILESGRALEKFNQIIVEQGGTPKKPEEIELGKYVEEVRSPIDGYIVGINNTSITNVVKEAGAPRDKKAGLLLNAKIGNKVKRGDILYTIYSGSEERLNSAVNLARRVYPVNVEGMMIERISKF
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q3IP82
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MELTVEPIDIGTERPVVLLNCADAETLGVHSLDRVEIDWDGTTEVGIVKVTDELVAAGRIGASHGFPEITDGTVVAVTPAGQPESVESIRRKLDGRELDSDELGAIVADIEADRLSDLELSAYVCASHANGLSLEETKQLTERMAEVGKQLSWEQPVVADKHSIGGVAGNRVTPVVVAIVAAAGLTIPKTSSRAVTSPAGTADTMEVFCPVEFSREEIRDIVTETGGCLVWGGAVDLSPVDDKVIRAQRPLSLDPPGQVIASVLSKKQSAGSSHIVVDIPYGAGAKVTSLSEARDLADDFRRVGDHLGLTIECALTRGSDPIGHGIGPVLEARDVLAVLEGEGPEPLRIKSLRLADIIFDMAREAGMPVDDRSAADILDSGAALSKFRDIVAVQGGDPDVSRDDLQPGDRTETVTADTDGLVVDVDNQAVSQLARRAGAPNDHGAGVVIHRRTGDKAVAGDVLYTIHAESSDRLEAAREYAAGDEIVRVGGRDEALVERR
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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G8ZJ29
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MRAKVRILNIRSGHFDVFINPKDAQEWKLHPNDLVKIESGKRSIYGSVVIGDFVESGEVGLSLDILDAYQFSEGELVSITPSETPESVRYIKKKMRGEKLRKVEIETIVRDIVDRKLRNTEISALVTAIEVNGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNIIVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFTNVTLSLDEIKRIVEKIGACLVWGGALNLAPADDLTIHVERRLSLDPRGLMLASIMSKKYAIGSQYILIDIPTGKGAKVETMEEARSLAKDFIELGKKLGQYVEVAITYGGQPIGYTVGPALEAKEALETLMTGKGPGSLVEKALGLAGILLEMGGVAPRGMGKKVAREILESGKAYEKIKEIIEEQGGDPNIKPEDIPIGDKTYTIHAQTSGYVTGIDNKAITAIAREAGAPEDKGAGVKLHVKVGEKVKEGDPLFTIHAESESRLDKAIILARRLEPIKIEGMVLQVLGNL
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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Q8U0I2
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MRGKIKILDIETGNLAIFINPEDAEQWRIHPNDLVKIESGKRYIYGSAFIGNIVEKGEIGISKDVLSIHQFSNGEIVSLSPAGTPESVKYIKKKMRGEKLKKVEIETIVRDIVDRKLRNTEISAFVSAIEINGLDMEEIAALTIAMAETGDMLDIERKPIMDIHSIGGVPGNKTNVIVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVLTNVTLTLEEIKRIVEKIGACLVWGGALNLAPADDLMIHVERRLSLDPRGLMLASIMAKKYAIGSQYILIDIPTGKGAKVESMEEARSLARDFIELGKRLGQYVEVAITYGGQPIGYTVGPALEAKEALETLMTGRGPGSLVEKAIGLAGLLLEMGGAAPKGKGKIIAREILEKGKAYQKMREIIEEQGGDPDIKPEDIPIGDKTYTIHAQTNGYVTAIDNRGITAIAREAGAPEDKGAGIRLHVKVGDKVKEGDPLFTIHAESESRLDKAIVLARRLEPIKIEGMVLQVIENL
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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O59251
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MRAKVKILKIKTGSFNVFISPRDAEEWKLHPNDLVKIESGKRSIYASVAIGDFIEDGEVGLSQDILSSYQFSEGEVVSITPSGTPESVKYIKKKMKGEKLRKVEIETIIRDIVDRKLRNTEISAFITAIEINGLSMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVLTNVKLSLDEIKRIVEKIGACLVWGGALNLAPADDLTIHVERRLSLDPRGLMLASIMSKKYAIGSQYILIDIPTGKGAKVETMDEARTLAKDFIELGKKLGQYVEVAITYGGQPIGYAIGPALEAKEALETLMTGKGPGSLVEKATGLAGILLEMGGVAPKGMGKKVAKEILESGKAYEKMKEIIEEQGGDPNIKPEDIPIGDKTYTIHAQTGGYVTGIDNRAITAIAREAGAPEDKGAGVRLHVKVGEKVKEGDPLITIHAESESRLEKAIVLARRLEPIKIEGMVLQVIGNI
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Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
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C0HJE4
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MLVGKKVQTF
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Because of the indeterminate molecular weight of starch, an approximate KM value of 0.975 mg/ml was determined. Optimum pH is 5.0. Optimum temperature is 60 degrees Celsius. On the 2D-gel the determined pI of this protein is: 5.0, its MW is: 155 kDa. Belongs to the glycosyl hydrolase 13 family.
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B5YDK4
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MTKSIYFSLGIHNHQPVGNFDFVIERAYEMSYKPLINFFFKHPDFPINVHFSGFLLLWLEKNHPEYFEKLKIMAERGQIEFVSGGFYEPILPIIPDKDKVQQIKKLNKYIYDKFGQTPKGMWLAERVWEPHLVKYIAEAGIEYVVVDDAHFFSVGLKEEDLFGYYLMEEQGYKLAVFPISMKLRYLIPFADPEETITYLDKFASEDKSKIALLFDDGEKFGLWPDTYRTVYEEGWLETFVSKIKENFLLVTPVNLYTYMQRVKPKGRIYLPTASYREMMEWVLFPEAQKELEELVEKLKTENLWDKFSPYVKGGFWRNFLAKYDESNHMQKKMLYVWKKVQDSPNEEVKEKAMEEVFQGQANDAYWHGIFGGLYLPHLRTAIYEHLIKAENYLENSEIRFNIFDFDCDGNDEIIVESPFFNLYLSPNHGGSVLEWDFKTKAFNLTNVLTRRKEAYHSKLSYVTSEAQGKSIHERWTAKEEGLENILFYDNHRRVSFTEKIFESEPVLEDLWKDSSRLEVDSFYENYDYEINKDENKIRVLFSGVFRGFELCKSYILYKDKSFVDVVYEIKNVSETPISLNFGWEINLNFLAPNHPDYYFLIGDQKYPLSSFGIEKVNNWKIFSGIGIELECVLDVEASLYRYPIETVSLSEEGFERVYQGSALIHFYKVDLPVGSTWRTTIRFWVK
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This amylase is a highly liquefying-type: oligomers appeared at the beginning of incubation, followed by a graded decrease in the amounts of maltotriose, maltose and glucose in prolonged incubation. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Optimum pH is 5.5. Stable above pH 5.5. Optimum temperature is about 90 degrees Celsius. Highly thermostable. Retains 70% of its maximal activity after heating 1 hour at 90 degrees Celsius, but no decrease in activity was observed within the same time at 80 degrees Celsius. Belongs to the glycosyl hydrolase 57 family.
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Q9GN73
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MFLAKSIVCLALLAVANAQFNTNYASGRSGMVHLFEWKWDDIAAECENFLGPYGYAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMVRRCNNVGVRIYVDVVFNHMAADGGTYGTGGSTASPSSKSYPGVPFSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIVEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGSLKNLNTDHGFESGAKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLQYLVNWGVSWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFTDTDQGPPTTDGQNIASPSFNSDNSCSGGWVCEHRWKQIYNMVGFRNAVGSDAIQNWWDNGSNQIAFSRGSKGFVAFNNDNYDLNSSVQTGLPAGTYCDVISGSKSGSSCTGKTVTVGSDGRANISIGSSEDDGVLAIHVNAKL
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Binds 1 Cl(-) ion per subunit. Monomer. Belongs to the glycosyl hydrolase 13 family.
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Q2M7N4
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MKLAACFLTLLPGFAVAASWTSPGFPAFSEQGTGTFVSHAQLPKGTRPLTLNFDQQCWQPADAIKLNQMLSLQPCSNTPPQWRLFRDGEYTLQIDTRSGTPTLMISIQNAAEPVASLVRECPKWDGLPLTVDVSATFPEGAAVRDYYSQQIAIVKNGQIMLQPAATSNGLLLLERAETDTSAPFDWHNATVYFVLTDRFENGDPSNDQSYGRHKDGMAEIGTFHGGDLRGLTNKLDYLQQLGVNALWISAPFEQIHGWVGGGTKGDFPHYAYHGYYTQDWTNLDANMGNEADLRTLVDSAHQRGIRILFDVVMNHTGYATLADMQEYQFGALYLSGDEVKKSLGERWSDWKPAAGQTWHSFNDYINFSDKTGWDKWWGKNWIRTDIGDYDNPGFDDLTMSLAFLPDIKTESTTASGLPVFYKNKMDTHAKAIDGYTPRDYLTHWLSQWVRDYGIDGFRVDTAKHVELPAWQQLKTEASAALREWKKANPDKALDDKPFWMTGEAWGHGVMQSDYYRHGFDAMINFDYQEQAAKAVDCLAQMDTTWQQMAEKLQGFNVLSYLSSHDTRLFREGGDKAAELLLLAPGAVQIFYGDESSRPFGPTGSDPLQGTRSDMNWQDVSGKSAASVAHWQKISQFRARHPAIGAGKQTTLLLKQGYGFVREHGDDKVLVVWAGQQ
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Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through the cytoplasmic membrane via the membrane-bound complex of three proteins, MalF, MalG, and MalK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the MalS protein. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Monomer. Under the regulatory control of the MalT protein. Belongs to the glycosyl hydrolase 13 family.
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P00693
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MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAATFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWEKNGAAATLQRS
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Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 3 Ca(2+) ions per subunit. Redox-insensitive. Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate. Monomer. Production of alpha-amylase is hormonally regulated. Germinating embryos produce the hormone gibberellic acid, which within 10 hours stimulates the aleurone cells covering the endosperm of the seed to produce alpha-amylase. The enzyme then degrades the starch within the endosperm for use by the developing plant embryo. There are at least 4 types of alpha-amylase in barley. Mutagenesis experiments indicate that His-117 and His-314 participate in transition state stabilization but not directly in catalysis. Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity. Belongs to the glycosyl hydrolase 13 family.
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Q01117
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MLLINFFIAVLGVISLSPIVVARYILRRDCTTVTVLSSPESVTGSNHVQLASYEMCGSTLSASLYVYNDDYDKIVTLYYLTSSGTTGSTLALILPVWSNNWELWTLSAIAAGAVEITGASYVDSDTSVTYTTSLDLPLTTTSASVPTGTAANWRGRSIYQVVTDRFARTDGSITYSCDVTDRVYCGGSYRGIINMLDYIQGMGFTAIWISPIVENIPDDTGYGYAYHGYWMKDIFALNTNFGGADDLIALATELHNRGMYLMVDIVVNHFAFSGNHADVDYSEYFPYSSQDYFHSFCWITDYSNQTNVEECWLGDDSVPLVDVNTQLDTVKSEYQSWVKQLIANYSIDGLRIDTVKHVQMDFWAPFQEAAGIYTVGEVFDGDPSYTCPYQENLDGVLNYPVYYPVVSAFQRVGGSISSLVDMIDTLKSECIDTTLLGSFLENQDNPRFPSYTSDESLIKNAIAFTILSDGIPIIYYGQEQGLNGGNDPYNREALWPTGYSTTSTFYEYIASLNQIRNHAIYIDDTYLTYQNWVIYSDSTTIAMRKGFTGNQIITVLSNLGSSGSSYTLTLSNTGYTASSVVYEILTCTAVTVDLSGNLAVPMSGGLPRVFYPESQLVGSGICSM
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. Belongs to the glycosyl hydrolase 13 family. Truncated N-terminus.
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Q921Y7
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MKFFLLLSLIGFCWAQYDPHTQYGRTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKWDGEKMSYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYYWPRNFQNGKDVNDWVGPPNNNGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVVNGQPFANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISGDKVDGNCTGIKVYVGNDGKAHFSISNSAEDPFIAIHAESKI
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Binds 1 Cl(-) ion per subunit. Monomer. Expressed in liver and saliva. Hepatic and salivary alpha-amylases are encoded by the same gene; however, their mRNAs have different 5'-UTR sequences. Belongs to the glycosyl hydrolase 13 family.
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Q6Z317
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MQVLNTMVNKHFLSLSVLIVLLGLSSNLTAGQVLFQGFNWESWKENGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVGEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDPYGDGTGNPDTGADFAAAPDIDHLNKRVQRELIGWLDWLKMDIGFDAWRLDFAKGYSADMAKIYIDATEPSFAVAEIWTSMANGGDGKPNYDQNAHRQELVNWVDRVGGANSNATAFDFTTKGILNVAVEGELWRLRGEDGKAPGMIGWWPAKATTFVDNHDTGSTQHLWPFPSDKVMQGYAYILTHPGNPCIFYDHFFDWGLKEEIERLVSIRNRQGIHPASELRIMEADSDLYLAEIDGKVITKIGPRYDVEHLIPEGFQVVAHGDGYAIWEKI
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Important for breakdown of endosperm starch during germination. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 3 Ca(2+) ions per subunit. Monomer. More abundant in germinating seeds, than in callus, young roots and leaves. Expressed at a high level during germination in the aleurones cells under the control of the plant hormone gibberellic acid and in the developing grains at a low level. Only cereal amylase known to be glycosylated. Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity. Belongs to the glycosyl hydrolase 13 family.
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P21567
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MQISKAALLASLAALVYAQPVTLFKRETNADKWRSQSIYQIVTDRFARTDGDTSASCNTEDRLYCGGSFQGIIKKLDYIKDMGFTAIWISPVVENIPDNTAYGYAYHGYWMKNIYKINENFGTADDLKSLAQELHDRDMLLMVDIVTNHYGSDGSGDSIDYSEYTPFNDQKYFHNYCLISNYDDQAQVQSCWEGDSSVALPDLRTEDSDVASVFNSWVKDFVGNYSIDGLRIDSAKHVDQGFFPDFVSASGVYSVGEVFQGDPAYTCPYQNYIPGVSNYPLYYPTTRFFKTTDSSSSELTQMISSVASSCSDPTLLTNFVENHDNERFASMTSDQSLISNAIAFVLLGDGIPVIYYGQEQGLSGKSDPNNREALWLSGYNKESDYYKLIAKANAARNAAVYQDSSYATSQLSVIFSNDHVIATKRGSVVSVFNNLGSSGSSDVTISNTGYSSGEDLVEVLTCSTVSGSSDLQVSIQGGQPQIFVPAKYASDICS
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. Belongs to the glycosyl hydrolase 13 family.
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P19269
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MRFSTEGFTSKVVAAILAFSRLVSAQPIIFDMRDVSSSADKWKDQSIYQIVTDRFARSDGSTTADCLVSDRKYCGGSYKGIIDKLDYIQGMGFTAIWISPVVEQIPDNTAYGYAYHGYWMKNIDELNTNFGTADELKQLASELHSRSMLLMVDVVYNHYAWNGDGSSVDYSSFTPFNQQSYFHDYCLITNYNDQTNVEDCWEGDTEVSLPDLSTEDNEVIGVFQTWVSDFVQNYSIDGLRIDSAKHVDTASLTKFEDASGVYNLGEVYQGDPTYTCPYQNYMKGVTNYPLYYPVYRFFSDTSATSSELTSMISTLQSSCSDVSLLGNFIENHDQVRFPSVTSDTSLIKNDMAFIILGDGIPIIYYGQEQGLNGGSDPANREALWLSGYNTDSEYYELISKLNQIRNQAIKKDSAYSTYKSSVVSSSDHYIATRKGSDANQLISIFNNLGSNGSQDITVSNTGYSSGDKVIDIISCNSVLAGDSGSLSVSISGGMPQVYAPSSVLSGSGICNQ
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. Alpha-amylase expression underlies catabolite repression by glucose. Belongs to the glycosyl hydrolase 13 family.
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O74922
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MGFSKIALFSLFALFGLPTSLAKSSEEWRDRIIYQVITDRFAVDSDNTPDCSFDDSSYCGGTWSGIRSKLDYIQGMGFNAIWISPVEKNLEGSYGSDGEAYHGYWNTDFTQLNEHFGSEDDLIDLITDMHNRDMWIMFDALANSMAIPGPTDNISYSNLVPFNDSSYFHPYCWIDYGSNNNTDIEDCWTGDDNVILADLDIESTNVADYLHEHIHDMVERYQIDGIRIDAVKQMNPEFFPNYTSAAGVFAIGEMFSYDPNVSCSVRNYLDSITSYPIRQGIEFAFNYTGAAFEYLQEIDTQFQQACEGQDMSVIGNFLENHDLPRYTSITNDTSQDIGAIVFLLLHTGIPIIYYGEEQRLPGGSDTPENRAALWNYGYDTDANYYQTIRTAIALRKQAISDSDSWTTDSHSYLDYDLRHAVVRKGDVLGVYTNYESSSDNVTYDVSSNFDDGTVLREVLSNTTTTVGSSGALHVTVVSGLPQVYYPEASLTSFGNFLGTATSYSSASASYPSTSMSASLSSVHTSSATSSSKSSSSSSSRSGSSSSSSSRSGSTSSSGSSHTITSTSQSVHTSGSSTSTSSVAVTSTAYSSSSSSSSSSSIESSANAVRVSILGVAAFIAIVLFI
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations. Belongs to the glycosyl hydrolase 13 family.
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Q5Z7T8
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MATGRRLSMILLLLLLGLASGDKILFQGFNWESWRQSGGWYNLLMGKVDDIVAAGVTHVWLPPPSHSVSTQGYMPGRLYDLDASRYGTSMELKSLISALHGKGIQAIADVVINHRCADYKDSRGIYCIFEGGTPDGRLDWGPHMICRDDTQFSDGTGNLDTGADFAAAPDIDHLNGVVQRELTDWLLWLKSDEVGFDAWRLDFARGYSPEVAKVYIEGTTPVGLAVAELWDSMAYGGDGKPEYNQDAHRQALVDWVDRVGGTASAGMVFDFTTKGIMNTAVEGELWRLIDQQGKAPGVIGWWPAKAVTFVDNHDTGSTQQMWPFPSDKVMQGYAYILTHPGNPCIFYDHFFDWGLKEQIAALVAVRQRNGVTATSSLKIMLHDADAYVAEIDGKVVMKIGSRYDVSSLIPPGFHLAAHGNGYAVWEKIAAAAAAADHRTSSSASL
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Important for breakdown of endosperm starch during germination. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 3 Ca(2+) ions per subunit. Monomer. Expressed at a high level during germination in the aleurones cells under the control of the plant hormone gibberellic acid and in the developing grains at a low level. Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity. Belongs to the glycosyl hydrolase 13 family.
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Q9UBH3
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MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Binds 1 Cl(-) ion per subunit. Monomer. Binds to the sea anemone inhibitor helianthamide (PubMed:27066537). Detected in pancreas (at protein level). Belongs to the glycosyl hydrolase 13 family. Amylase entry
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Q9SGS0
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MGYYNNVFDECNDQTDIGRVIRDGREVILQAYNWESHKYDWWRNLDGKVPDIAKSGFTSAWLPPPSQSLAPEGYLPQDLYSLNSAYGSEHLLKSLLRKMKQYKVRAMADIVINHRVGTTRGHGGMYNRYDGISLPWDEHAVTSCTGGLGNRSTGDNFNGVPNVDHTQHFVRKDIIGWLRWLRNTVGFQDFRFDFARGYSANYVKEYIGAAKPLFSVGECWDSCNYNGHGLDYNQDSHRQRIISWIDATGQISAAFDFTTKGILQEAVKGQYWRLCDAQGKPPGVMGWWPSRAVTFLDNHDTGSTQAHWPFPSHHVMEGYAYILTHPGIPCVFYDHFYDWGSSIHDQIVKLIDIRRRQDIHSRSTVRVLKAESNLYAAIVGEKICMKLGDGSWCPSGRDWTLATSGHRYAVWHK
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Probable alpha-amylase that does not seem to be required for breakdown of transitory starch in leaves. Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Expressed in developing siliques. Circadian-regulated, with a peak in expression at the beginning of the light period. No visible phenotype under normal growth conditions. Belongs to the glycosyl hydrolase 13 family.
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P86088
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MWPFPSDK
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 3 Ca(2+) ions per subunit. Monomer. Belongs to the glycosyl hydrolase 13 family.
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P14898
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MIYDDKIFGDLCHKEFLVEREVKKLEEIYLEEVLPEDPKPEDEIEFTFNCPLKFHITSGKIVKDNREIYTFNIQERKTQWNDSIFNFSEIIKIKIPPLKENGLYQIHLYEMNEKIYEQYLSIDNFEAPLWSEESIIYHIFIDRFAKDEKEVEYSENLKEKLGGNLKGILSRLDYIENLGINTIWISPIFKSTSYHGYDIEDYFEIDPIWGTKEDLKKLVREAFNRGIRIILDFVPNHMSYKNPIFQKALKDKNSNLRSWFIFKGEDYETFFGVKSMPKINLKNKEAIDYIINAAKYWIREFGISGYRMDHATGPDINFWSIFYYNLKSEFPETFYFGEIVETPKETKKYVGKFDGTLDFYLFKIIRDFFIGKRWSTKEFVKMIDLEEKFYGNKFKRISFLENHDSNRFLWVAKDKKLLRLASIFQFSINAIPIIYNGQEMGCSQYRDILEGNRTLHEHARLPIPWSDDKQDKELIDFYRQLVKIRKSHPALYKGTFIPIFSDMISFIKETQEESILVLINIEDKEEIFNLNGTYRDLFSGNIYTNSLKLGPMSAHLLLRIDH
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Monomer. When compared to AmyA, AmyB produced larger amounts of reducing sugar. Belongs to the glycosyl hydrolase 13 family.
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P78072
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MRNPTLLQCFHWYYPEGGKLWPELAERADGFNDIGINMVWLPPAYKGASGGYSVGYDSYDLFDLGEFDQKGSIPTKYGDKAQLLAAIDALKRNDIAVLLDVVVNHKMGADEKEAIRVQRVNADDRTQIDEEIIECEGWTRYTFPARAGQYSQFIWDFKCFSGIDHIENPDEDGIFKIVNDYTGEGWNDQVDDELGNFDYLMGENIDFRNHAVTEEIKYWARWVMEQTQCDGFRLDAVKHIPAWFYKEWIEHVQEVAPKPLFIVAEYWSHEVDKLQTYIDQVEGKTMLFDAPLQMKFHEASRMGRDYDMTQIFTGTLVEADPFHAVTLVANHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYPDLYGAHYEDVGGDGQTYPIDMPIIEQLDELILARQRFAHGVQTLFFDHPNCIAFSRSGTDEFPGCVVVMSNGDDGEKTIHLGENYGNKTWRDFLGNRQERVVTDENGEATFFCNGGSVSVWVIEEVI
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 1 Ca(2+) ion per subunit. Monomer. Belongs to the glycosyl hydrolase 13 family.
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P04063
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MANKHLSLSLFLVLLGLSASLASGQVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDGRGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDIDHLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSFAVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGIHNESKLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVWEKI
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Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Binds 3 Ca(2+) ions per subunit. Monomer. Production of alpha-amylase is hormonally regulated. Germinating embryos produce the hormone gibberellic acid, which within 10 hours stimulates the aleurone cells covering the endosperm of the seed to produce alpha-amylase. The enzyme then degrades the starch within the endosperm for use by the developing plant embryo. Type B isozyme mRNA is undetectable in unstimulated cells and increases a hundred-fold after stimulation with gibberellic acid. There are at least 4 types of alpha-amylase in barley. Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity. Belongs to the glycosyl hydrolase 13 family.
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A0A144A431
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MEKAIRDRVEKWKKEHTIDGKDATNEHAYESLNELILDGKKLTSIKNEEKELLKNFKNLERLCLNQTGIQTLENIPSIATLNVLELTDNHLSSVEVLKYIVQNFPNIKTLEIGGNHFKNINDFETLKELKNLVRLGVQFNPFADNPNYRKELFEFLPNVKIIDCYNKEGMEVLSSDEEEEEEYEEDNTLKNFYEADFKDEDDEDEEFVPNDNEDDDEDDELDDDLEDEDMEDLDKEDLDKEDYDIDTKETEGVNKDEKSNKRKQDALDNTNDMDLKKTKLE
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Belongs to the ANP32 family.
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Q86QS6
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MTLLQRIELERGKREPGEITELNLDNSKSVDIEGLTDEYSSLEVLSMMNVGLQSLAGLPCLAGLKTLELSNNLISGGLDALLKCPNIEQLNLSSNKIESMDVLIPLAKLSELKSLDLGNCPVTSTENYRKKAFAMIPSLKYLDGLDENNEEEVFGNDFLNGGLDEEADGVGIEALQQSGELEDDEDDYAPGEDEEAELDDYDDVDDEDEDDVEEDNGANLSAANVSGPRRPGTKRRHEDIQDGKNGGNAEHCGTKHKHTEDHVETHVENGSTADD
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Belongs to the ANP32 family.
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B3KSU3
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MLHTEGHALLRAVGQGKLRLARLLLEGGAYVNEGDAQGETALMAACRARYDDPQNKARMVRYLLEQGADPNIADRLGRTALMHACAGGGGAAVASLLLAHGADPSVRDHAGASALVHALDRGDRETLATLLDACKAKGTEVIIITTDTSPSGTKKTRQYLNSPPSPGVEDPAPASPSPGFCTSPSEIQLQTAGGGGRGMLSPRAQEEEEKRDVFEFPLPKPPDDPSPSEPLPKPPRHPPKPLKRLNSEPWGLVAPPQPVPPTEGRPGIERLTAEFNGLTLTGRPRLSRRHSTEGPEDPPPWAEKVTSGGPLSRRNTAPEAQESGPPSGLRQKLSRMEPVELDTPGHLCPDSPESSRLSLERRRYSASPLTLPPAGSAPSPRQSQESLPGAVSPLSGRRRSPGLLERRGSGTLLLDHISQTRPGFLPPLNVSPHPPIPDIRPQPGGRAPSLPAPPYAGAPGSPRTKRKLVRRHSMQTEQIRLLGGFQSLGGPGEPGR
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Methylated at Gln-15 by N6AMT1. Belongs to the ANKRD34 family.
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Q5BJT1
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MLHTEGHALLRAVGQGKLRLARLLLEGGAYVNEGDAQGETALMAACRARYDDPQNKARMVRYLLEQGADPNIADRLGRTALMHACAGGGGAAVASLLLAHGADPSVRDHAGASALVHALDRGDRETLATLLDACKAKGTEVIIITTDTSPSGTKKTRQYLNSPPSPGVEDPAPAPPSPGVCTSPSEVQLQTAGGGRGLLSPRAQEEEEKRDVFEFPLPKSPDDPSPSEPLPKPPRHPPKPLKRLNSEPWGLVAPPQPVPPAEGRPGLERLAAEFNGLTLTGRPRLSRRHSTEGPEDPPPWAEKVTGGGPLSRRNTAPEAQESGLPSGLRQKLSRMESVELDTPGHFCPDSPESSRLSLERRRYSASPLTLPPAGSVSSPRQSQESLPGAVSPLSGRRRSPGLLERRGSGTLLLDHISQTRPGFLPPLNVSPHPPIPDIRPQPGGRAPSLPAPPHSGAPGSPRTKRKLVRRHSMQTEQIRLLGGFQSLGGPGEPGR
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Methylated at Gln-15 by N6AMT1. Belongs to the ANKRD34 family.
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Q68D79
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MDEGMEISSEGNSLIKAVHQSRLRLTRLLLEGGAYINESNDRGETPLMIACKTKHVDHQSVSKAKMVKYLLENNADPNIQDKSGKTALMHACLEKAGPEVVSLLLKSGADLSLQDHSSYSALVYAINSEDTETLKVLLSACKAKGKEVIIITTAKLPCGKHTTKQYLNMPPVDIDGCHSPATCTTPSEIDIKTASSPLSHSSETELTLFGFKDLELAGSNDDTWDPGSPVRKPALAPKGPKLPHAPPWVKSPPLLMHQNRVASLQEELQDITPEEELSYKTNGLALSKRFITRHQSIDVKDTAHLLRAFDQASSRKMSYDEINCQSYLSEGNQQCIEVPVDQDPDSNQTIFASTLRSIVQKRNLGANHYSSDSQLSAGLTPPTSEDGKALIGKKKILSPSPSQLSESKELLENIPPGPLSRRNHAVLERRGSGAFPLDHSVTQTRQGFLPPLNVNSHPPISDINVNNKICSLLSCGQKVLMPTVPIFPKEFKSKKMLLRRQSLQTEQIKQLVNF
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Phosphorylated. Belongs to the ANKRD34 family.
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Q8BVH7
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MDEGSEVSTDGNSLIKAVHQSRLRLTRLLLEGGAYINESNDRGETPLMIACKTKHVDQQSVGRAKMVKYLLENSADPNIQDKSGKSALMHACLERAGPEVVSLLLKSGADLSLQDHSGYSALVYAINAEDRDTLKVLLSACQAKGKEVIIITTAKSPSGRHTTQHHLNMPPADMDGSHPPATPSEIDIKTASLPLSYSSETDLTLFGFKDKELCGGSDNTWDPDSPPRKPVIATNGPKLSQAPAWIKSTPSLKHQARVASLQEELQDITPEEEIAYKTNALALSKRFITRHQSIDVKDTAHLLRAFDQVNSRKMSYDEINYHSLFPEGSQTSVEIPTDRDPDSNQIFASTLKSIVQKRNSGANHYSSDSQLAEGVTPPTVEDGKAAKKKIFAPSPSLLSGSKELVEPAPPGPLSRRNHAVLERRGSGAFPLDHSLAQSRPGFLPPLNVNPHPPITDIGVNNKICGLLSCGQKALMPTAPIFPKEFKTKKMLLRRQSLQTEQIKQLVNF
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Specifically and constitutively expressed in brain (at protein level). Up-regulated in bone marrow upon differentiation (at protein level). Phosphorylated. Belongs to the ANKRD34 family.
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Q5PQ89
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MDEAVDVTTESNSLIKAVYQSRLRLTRLLLEGGAYINESNDRGETPLMIACKTKHVDHQSVSKVKMIKYLLENNADPNIQDKFGKTALMHACLENAGAEVVSLLLESGADPSLQDHTGFSALVYAVNSEDKETLRILLNACKAKGKEVIIITKDKSASGKQTTRQYLNVPPSPGIEGNNSPSPCTSPSDIELKTSPAPISNALETEKELFNFKEAASSCGFKGSSQPGSPTKKPHLSHVGGKLPLLQRLHSEPWLKIPPSLLHQHKVSSLQEELQDITPDEELSLQMNELMFSKRYFTRHQSIDVKDASHLLKTFDTAGARKLSYDEIHSHSIYPEANPNRPETLPVDQEPDLMHSISVSSLKSIVQRRNLGANHYSSDSQLTTRAGPAAAEDSKSLLEKKKMLCPQPLLTGSRESLESISVTALSRRNHAILERRGSGALLLDHIAHTRPGFLPPLNVNPHPPIPDISIHSKLISSGTKSLIPSAPHVPKEPKSKKMLLRRHSMHTEQIKQLMNLEEIFG
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Belongs to the ANKRD34 family.
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H3BNM1
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MMDDDTELRTDGNSLLKAVWLGRLRLTRLLLEGGAYINESNDKGETALMVACITKHVDQQSISKSKMVKYLLDNRADPNIQDKSGKTALIHACIRRAGGEVVSLLLENGADPSLEDRTGASALVYAINADDKDALKHLLDACKAKGKEVIIITTDKSSSGTKTTKQYLNVPPSPKVEDRHSPPLCASPSDIELKALGLDSPLTEKEDDFFSLQAGHPSSCNTSKAVNEPGSPTRKVSNLKRARLPQLKRLQSEPWGLIAPSVLAASTRQDETHGASTDNEVIKSISDISFPKRGPLSRTNSIDSKDPTLFHTVTEQVLKIPVSSAPASWKAAYEKGQAPHPRLARRGTLPVDQEKCGMGPSGPSALKEPASLKWLENDLYDLDIQPGPDPPNSISLESGKGPLDRKKLNSSHLSLFHGSRESLDTVPSTSPSSARRRPPHLLERRGSGTLLLDRISHTRPGFLPPLNVNLNPPIPDIRSSSKPSCSLASGLKSMVPVAPSSPKRVDLRSKKKLLRRHSMQIEQMKQLSDFEEIMT
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Belongs to the ANKRD34 family.
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Q8BLB8
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MMDDDTELRTDGNSLLKAVWLGRLRLTRLLLEGGAYINESNDKGETALMVACITKHVDQQSISKSKMVKYLLDNRADPNIQDKSGKTALIHACIRRAGGEVVSLLLENGADPSLEDRTGASALVYAINADDKDALKHLLDACKAKGKEVIIITTDKSSSGTKTTKQYLNVPPSPKVEDRQSPPLCTTPSDVELKTSGLASPPSEKDDDFFILQTGHQSGCSTSKVLNEPGSPTRKVSSLKRARLPQLKRLQSEPWGLIAPSVLAAATRQDETHGTSTDNEVIRSINDVTFPKRGPLSRTNSIDSKDPTLFPTVQEQVLKVSASTPASWKAAYEKGQAPHPRLARRGTLPLDQEKSGMCPPGPSTLKDPASLKLLENDLYDLDIQPVGDPPNSMSLESGKGPLDRKKLNSSHLSLFHGSRESLEVVPSTSPTSVRRRPPHLLERRGSGTLLLDRIAHTRPGFLPPLNVNLNPPIPDIRASSKPASPLASGLKSMAPVAPNSPKRVDLRSKKKLLRRHSMQIEQMKQLSDFEEIMA
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Belongs to the ANKRD34 family.
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Q9HCD1
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MEDGKRERWPTLMERLCSDGFAFPQYPIKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDLPINSNPVSSQKQPALKATSGKEDSISNIATEIKDGQKSGTVSSQKQPALKDTSDKDDSVSNTATEIKDEQKSGTVLPAVEQCLNRSLYRPDAVAQPVTENEFSLESEIISKLYIPKRKIISPRSIKDVLPPVEEAVDRCLYLLDRFAQPVTKDKFALESENISEPYFTNRRTISQQSAENLDAACGIDKTENGNMFEDQNVDKEGKALPATGQKANVSPEQPPLFTHTVKDRDHISTRFLGGMDSLTSSEESSERPPLSTLTLKEADPSSKAAMRRKDSPPPGKVSSQKQPAEKATSDDKDSVSNIATEIKEGPISGTVSSQKQPAEKATSDEKDSVSNIATEIKKGQQSGTVSPQKQSAWKVIFKKKVSLLNIATRIMGGGKSGTVSSQKQPASKATSDKTDSALNIATEIKDGLQCGTVSSQKQPALKATTDEEDSVSNIATEIKDGEKSGTVSSQKQPALKATTDEEDSVSNIATEIKDGEKSGTVSSQKQPALKATTDEKDSVSNIATEIKDGEKSGTVSSQKPPALTATSDEEGSVLSIARENKDGEKSRTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIARENKDGEKSRTVSSEKPPGLKASSAEKDSVLNIARGKKDGEKTKRVSSRKKPSLEATSDEKDSFSNITREKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSRTVSSEKPPGLKATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTVSSEKPSGLKATSAEKDSVLNIARGKKYGEKTKRVSSRKKPALKATSDEKDSVLYIAREKKDGEKSRTVSSPKQPALKAICDKEDSVPNMATEKKDEQISGTVSCQKQPALKATSDKKDSVSNIPTEIKDGQQSGTVSSQKQPAWKATSVKKDSVSNIATEIKDGQIRGTVSPQKQSAQKVIFKKKVSLLNIATRITGGWKSGTEYPENLPTLKATIENKNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDIIQSSQTVSEDGDSLCCNCKNVILLIDQHEMKCKDCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQVFES
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Belongs to the ANKRD36 family. Truncated N-terminus. Extended N-terminus.
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Q9H759
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MERLCSDGFAFPHYYIKPYHLKRIHRAVLRGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKNEYQPLLLAVSRRKVKMVEFLLKKKANVNAIDYLGRSALILAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAENRVIFDLIYEYKRKRYEDLPINSNPVSPQKQRAEKATSDDKDSVSNIATEIKEGPISGTVSSQKQPAEKATSDEKDSVSNIATEIKEGQQSGTVSPQKQSAQKVIFKKKVSLLNIATRIMGGGKSGTVSSQKQPASKTASDKTDSALNTATEIKDGLQCGTVSSQKQQALKATTDEEGSVSNIATEIKDGEKSGTVSSQKKPALKATSDEKDSFSNITREKKDGEISRTVSSQKPPALKATSVKEDSVLNIAREKKDGEKSRTVSFEQPPGLKATRDEKDSLLNIARGKKDGEKTRRVSSHKQPSLKATSDKEDSVPNMATETKDEQISGTVSCQKQPALKATSDKKDSVSNIPTEIKDGQQSGTVSSQKQPAWKATSVKKDSVSNIATEIKDGQIRGTVSSQRRPALKTTGDEKDSVSNIAREIKDGEKSGTVSPQKQSAQKVIFKKKVSLLNIATRITGGGKSGTEYPENLRTLKATIENKDSVLNTATKMKEVQTSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDIIQSSQTVSEDGDSLCCNCKNVILLIDQHEMKCKDCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYRCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQVFES
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Belongs to the ANKRD36 family. Truncated N-terminus. Truncated N-terminus. Extended N-terminus. Truncated N-terminus. Truncated N-terminus.
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Q658V2
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MDDKEPKRWPTLRDRLCSDGFLFPQYPIKPYHLKGIHRAVFYRDLEELKFVLLTRYDINKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGADPNITDVFGRTALHYAVYNEDTSMIEKLLSYGANIEECSEDEYPPLFLAVSQRKVKMVEFLLKKKANINAVDYLGRSALIHAVTLGEKDIVILLLQHNIDVFSRDVYGKLAEDYASEAKNRVIFELIYEYERKKHEELSINSNPVSSQKQPALKATSGKEDSISNIATEIKDGQKSGTVSSQKQPALKGTSDKNDSVSNTATEIKDEQKSGTVSSQKQPALKDTSDKNDSVSNTATEIKDEQKSGTVLPAVEQCLNRSLYRPDAVAQPVTEDEFALESEIISKLYIPKRKIISPRSIEDVLPPVEEAVDRCLYLLDRFAQAVTKDKFALESENISEPYFTNRRTISQQSAEKLDAACGIDKTENGTLFEDQNVDKEGKALPATGQKANVSPEQPPLFTHTVKDSDHISTRFLGSMDSLTSSEESSERPPLSTLTLKEADPSSKAAMRRKDSPPPGKVSSQKQPAEKATSDDKDSVSNIATEIKEGPISGTVSSQKQPAEKATSDEKDSVSNIATEIKEGQQSGTVSPQKQSAWKVIFKKKVSLLNIATRITGGGKSGTVSSQKQPPSKATSDKTDSALNIATEIKDGLQCGTVSSQKQPALKATTDEEDSVSNIATEIKDGEKSGTVSSQKQPALKATTDEEDSVSIIATEIKDGEKSGTVSSRKKPALKATSDEKDSFSNITREKKDGEISRTVTSEKPAGLKATSDEEDSVLNIARGKEDGEKTRRVSSRKKPALKATSDEKDSFSNITREKKDGETSRTVSSQKPPALKATSDEEDSVLNIAREKKDGEKSRTVSSEKPSGLKATSDEKDSVLNIARGKKHGEKTRRVSSHKQPALKATSDKENSVPNMATETKDEQISGTVSSQKQPALKATSDKKDSVSNIPTEIKDGQQSGTVSSQKQLAWKATSVKKDSVSNIATEIKDGQIRGTVSSQRQPALKATGDEKDSVSNIAREIKDGEKSGTVSPQKQSAQKVIFKKKVSLLNIATRITGGWKSGTEYPENLPTLKATIENKNSVLNTATKMKDVQTSTPEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDIIQSSQTVSEDGDSLCCNCKNVILLIDQHEMKCKDCVHLLKIKKTFCLCKRLTELKDNHCEQLRVKIRKLKNKASVLQKRLSEKEEIKSQLKHETLELEKELCSLRFAIQQEKKKRRNVEELHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNEETLAETIACYSGQLAALTDENTTLRSKLEKQRESGQRLETEMQSYRCRLNAALCDHDQSHSSKRDQELAFQGTVDKCCHLQENLNSHVLILSLQLSKAESKFRVLETELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVENLQAECRKHRLLLEEDNKMLVNELNHSKEKKCQYEKEKAEREVAVRQLQQKQDDVLNKRSATKALLDASSRHCIYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDAQKLEVENVMMRKIIKKQDEQIERFEKILQHSSLMLQVFES
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Belongs to the ANKRD36 family. Extended N-terminus. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence.
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Q9ZJD1
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MSNSMLDKNKAILTGGGALLLGLIVLFYLAYRPKAEVLQGFLEAREYSVSSKVPGRIEKVFVKKGDRIKKGDLVFSISSPELEAKLAQAEAGHKAAKAVSDEVKRGSRDETINSARDVWQAAKSQANLAKETYKRVQDLYDNGVASLQKRDEAYAAYESTKYNESAAYQKYKMALGGASSESKIAAKAKESAALGQVNEVESYLKDVKALAPIDGEVSNVLLSGGELSPKGFPVVLMIDLKDSWLKISVPEKYLNEFKVGKEFEGYIPALKRSAKFRVKYLSVMGDFATWKATNNSNTYDMKSYEVEAIPLEELENFRVGMSVLVTIKP
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Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
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P94851
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MSNSMLDKNKAILTGGGALLLGLIVLFYLAYRPKAEVLQGFLEAREYSVSSKVPGRIEKVFVKKGDHIKKGDLVFSISSPELEAKLAQAEAGHKAAKALSDEVKRGSRDETINSARDVWQAAKSQATLAKETYKRVQDLYDNGVASLQKRDEAYAAYESTKYNESAAYQKYKMALGGASSESKIAAKAKESAALGQVNEVESYLKDVKATAPIDGEVSNVLLSGGELSPKGFPVVLMIDLKDSWLKISVPEKYLNEFKVGKEFEGYIPALKKSTKFRVKYLSVMGDFATWKATNNSNTYDMKSYEVEAIPLEELENFRVGMSVLVTIKP
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Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
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A1DN11
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MTVTISFEPYVGSSVDALSIPLYLRCQLVFKLSKPLAAVPLLESGVNRLVQALPFLSGEFTAVPASDGGKEILLVRPVLNFELSRILKIKYHETSLRHVCKQMNRPSSQGGDLPHEPYMPYPRLPDPSRPQPIVGFQVNVHTDGIILSVATHHCSFDATGMGSIVQNLAACCRSPPSDEPDLTTSPAQEAEARKVLSQVRETPFDPKMFPEYRPLDSMLSYYKGVQSALQGRQTTIVNRCFTIAADKINALKRRCNQLIPEMVKKYGLSTEDAIGSAWVSSNDVVAALLWTCINRARYPEIRERSVHQLPPDLLHATSSLGVPVNVRSRLSPPLPKSTLGNAVCLLREKVPLQFFALPSHANMEATSSVCADHSGDDEWALSFCRVAYGLRAKLNAIDDDYIRDYISYVQKSPCHLSVTLDTENLYLSNWREIGVYDADFGGMLGKPLRMRAPDGYTDGLIFVMAQRSEDKSAPWEFNISLEASTMKRIVHDPLWCKYVELDAFWHGEE
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O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptide synthetase anaPS (PubMed:19001367). The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367, PubMed:20165805). The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367, PubMed:20165805). Alkaloid biosynthesis. Monomer. Belongs to the fumigaclavine B O-acetyltransferase family.
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P54802
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MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW
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Involved in the degradation of heparan sulfate. Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. Monomer and homodimer. Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 89 family. A MPS3B mutation at position 100 was erroneously reported (PubMed:9950362) as an amino acid change from Arg to His. The right amino acid change is from His to Arg.
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O22293
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MTSKVQLVFLFLFLCVMWASPSAASCDEPSDPMMKQFEEWMAEYGRVYKDNDEKMLRFQIFKNNVNHIETFNNRNGNSYTLGINQFTDMTNNEFVAQYTGLSLPLNIKREPVVSFDDVDISSVPQSIDWRDSGAVTSVKNQGRCGSCWAFASIATVESIYKIKRGNLVSLSEQQVLDCAVSYGCKGGWINKAYSFIISNKGVASAAIYPYKAAKGTCKTNGVPNSAYITRYTYVQRNNERNMMYAVSNQPIAAALDASGNFQHYKRGVFTGPCGTRLNHAIVIIGYGQDSSGKKFWIVRNSWGAGWGEGGYIRLARDVSSSFGLCGIAMDPLYPTLQSGPSVEVI
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Cysteine protease. Displays a high level of diversity in substrate specificity at the P1-P1' cleavage site. A hydrophilic P1 residue is preferred, with Gln or Arg strongly preferred. Favors an Ile/Leu residue at the P2 position of substrates, with an overall higher preference for Leu. The optimal tripeptide for cleavage is Pro-Leu-Gln, with cleavage occurring after the Gln residue. Another optimal tripeptide is Val-Leu-Arg, which may imply that a hydrophobic residue at the P3 position of substrates is preferred. Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain. Strongly inhibited by chicken egg-white cystatin (Probable). Inhibited by iodoacetamide and the active-site-directed inhibitor trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64) (PubMed:31306685). kcat is 13.9 sec(-1) for Z-Phe-Val-Arg-AMC. kcat is 1.58 sec(-1) for Z-Phe-Arg-AMC. kcat is 0.16 sec(-1) for Z-Arg-Arg-AMC. kcat is 9.80 sec(-1) for Pro-Leu-Gln. kcat is 7.13 sec(-1) for Val-Leu-Arg. kcat is 5.62 sec(-1) for Pro-Leu-Arg. kcat is 4.96 sec(-1) for Ala-Leu-Arg. kcat is 6.29 sec(-1) for Val-Leu-Lys. kcat is 6.08 sec(-1) for Pro-Leu-Lys. kcat is 3.58 sec(-1) for Ala-Leu-Lys. kcat is 0.36 sec(-1) for Pro-Leu-Asn. Stem (at protein level). Belongs to the peptidase C1 family.
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Q7M0J9
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GFIGWGNNIFGHYSGDF
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Competitive antagonist of atrial natriuretic peptide NPR-A receptors. It binds competitively to atrial natriuretic peptide (ANP) receptors from bovine adrenal cortex and inhibits the ANP-induced intracellular cGMP accumulation in bovine aorta smooth muscle cells. Can also reduce the increase in cGMP produced by ANP or BNP (brain natriuretic peptide) in pregnant guinea pig myometrium, but has no effect on relaxation induced by either peptide. Blocks the ANP-induced human sperm acrosome reaction without affecting the acrosomal exocytosis or sperm motility. Also exhibits major and deleterious nonspecific (and even cytotoxic) effects on human fat cells, as it displays noncompetitive antagonism and exerts an inhibitory action on basal and beta-adrenergic receptor-induced lipolytic response. Anantin has been tested for antimicrobial activity against a broad variety of bacteria and fungi, but no antibiotic activity has been found. Inhibits the binding of ANP by 50% (IC(50)) at 1.0 uM. The isopeptide linked residue 8 is shown as Asn rather than Asp as mentioned in PubMed:1826288, because it is not known whether Asp or Asn is encoded and the isopeptide bonds are almost always formed between the amides Asn or Gln and N6-lysine or alpha amino groups, with the liberation of an ammonia that makes the reaction essentially irreversible.
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Q6TMA8
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MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGTDPKDRVPEGQAPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLTPTHLDNGVDKTSRGKRLPKMAQLIGLTPNATRLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGDRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQQRKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS
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Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (By similarity). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (By similarity). Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. Has higher activity in LPL inactivation than the uncleaved protein. Homooligomer; disulfide-linked via Cys residues in the N-terminal part of the protein. The homooligomer undergoes proteolytic processing to release its carboxyl fibrinogen-like domain, which circulates as a monomer (PubMed:14570927). The homooligomer unprocessed form is able to interact with the extracellular matrix (By similarity). The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. N-glycosylated. Forms disulfide-linked dimers and tetramers. Cleaved into a smaller N-terminal chain and a larger chain that contains the fibrinogen C-terminal domain; both cleaved and uncleaved forms are detected in the extracellular space. The cleaved form is not present within the cell.
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Q86VR9
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MMSPSQASLLFLNVCIFICGEAVQGNCVHHSTDSSVVNIVEDGSNAKDESKSNDTVCKEDCEESCDVKTKITREEKHFMCRNLQNSIVSYTRSTKKLLRNMMDEQQASLDYLSNQVNELMNRVLLLTTEVFRKQLDPFPHRPVQSHGLDCTDIKDTIGSVTKTPSGLYIIHPEGSSYPFEVMCDMDYRGGGRTVIQKRIDGIIDFQRLWCDYLDGFGDLLGEFWLGLKKIFYIVNQKNTSFMLYVALESEDDTLAYASYDNFWLEDETRFFKMHLGRYSGNAGDAFRGLKKEDNQNAMPFSTSDVDNDGCRPACLVNGQSVKSCSHLHNKTGWWFNECGLANLNGIHHFSGKLLATGIQWGTWTKNNSPVKIKSVSMKIRRMYNPYFK
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Mainly expressed in adult heart.
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Q9BZZ0
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MGKPWLRALQLLLLLGASWARAGAPRCTYTFVLPPQKFTGAVCWSGPASTRATPEAANASELAALRMRVGRHEELLRELQRLAAADGAVAGEVRALRKESRGLSARLGQLRAQLQHEAGPGAGPGADLGAEPAAALALLGERVLNASAEAQRAAARFHQLDVKFRELAQLVTQQSSLIARLERLCPGGAGGQQQVLPPPPLVPVVPVRLVGSTSDTSRMLDPAPEPQRDQTQRQQEPMASPMPAGHPAVPTKPVGPWQDCAEARQAGHEQSGVYELRVGRHVVSVWCEQQLEGGGWTVIQRRQDGSVNFFTTWQHYKAGFGRPDGEYWLGLEPVYQLTSRGDHELLVLLEDWGGRGARAHYDGFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCALYQRGGWWYHACAHSNLNGVWHHGGHYRSRYQDGVYWAEFRGGAYSLRKAAMLIRPLKL
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May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure.
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Q8R0Z6
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MGTARLRKLQLLLLLGAWRALGGAARCRVTLVLSPQKATSAVCRSSEATQDSELATLRMRLGRHEELLRALQRRAAEGGALADEVRALREHSLTLNTRLGQLRAQLQQEARAEPDLGAEPAAALGLLAERALDAEAEARRTTARLQQLDAQLREHAQLMSQHSSLLGRLQRACAGPERGQQQVLPLPLAPLVPLSLVGSASNTSRRLDQTPEHQREQSLRQQGPPSSLLPTGHLAVPTRPVGPWRDCAEAHGAGHWQSGVYDLRLGRRVVAVWCEQQQEGGGWTVIQRRQDGSVNFFTNWQHYKAGFGRPEGEYWLGLEPVHQVTSRGDHELLILLEDWGGRAARAHYDSFSLEPESDHYRLRLGQYHGDAGDSLSWHNDKPFSTVDRDRDSYSGNCALYHRGGWWYHACAHSNLNGVWYHGGHYRSRYQDGVYWAEFRGGAYSLKKAVMLTRLVRL
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May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure. Highly expressed in the liver, specifically in hepatocytes, and weakly in the heart. Expressed in hematopoietic cells, platelets and mast cells, and detected at wounded skin.
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B2Z4B5
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MLKKTLSAVAWLCIFLVAFVSHPVWPQKPPKRKTPAELTAATCCEEAKALQAQIANLSSLLSDLGKKQERDWVSVVMQVMELESSAKSMETRLTEAESKYSEMNNQIGIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDDFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNDHIHRLSRRPTRLRVEMQDWEGNMRYAEYSHFVLGNELNSYRLFLGNYSGDVGNDALIYHNNTAFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHNKHLDGITWYGWHGSSYSLKRVEMKIRPEDFQP
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Has a role in the formation and organization of the extracellular matrix. In the eye, it functions as a mediator of dexamethasone-induced matrix deposition in the trabecular meshwork, the tissue responsible for the outflow of the ocular aqueous humor and for the maintenance of intraocular pressure. Is a negative regulator of angiogenesis in the cornea, and plays a major role in maintaining corneal avascularity and transparency. Homotetramer; disulfide-linked.
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Q4ZGK4
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MLKKPLSAVTWLCIFIVAFVSHPAWLQKLSKHKTPAQPQLKAANCCEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEMNNQIDIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDDFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEHIHRLSRQPTRLRVEMEDWEGNLRYAEYSHFVLGNELNSYRLFLGNYTGNVGNDALQYHNNTAFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHNKHLDGITWYGWHGSTYSLKRVEMKIRPEDFKP
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Has a role in the formation and organization of the extracellular matrix. In the eye, it functions as a mediator of dexamethasone-induced matrix deposition in the trabecular meshwork, the tissue responsible for the outflow of the ocular aqueous humor and for the maintenance of intraocular pressure (PubMed:21199193). Is a negative regulator of angiogenesis in the cornea, and plays a major role in maintaining corneal avascularity and transparency (PubMed:25622036). Homotetramer; disulfide-linked. Higly expressed in the cornea (at protein level) (PubMed:11682471). Expression is restricted to the stromal layer (PubMed:11682471). Also detected at the junction between the corneal stromal layer and the conjuctiva. Not detected in the sclera (PubMed:11682471). Expression is up-regulated by dexamethasone.
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Q8R1Q3
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MLRETWLCVILVAFVSHPVWLQKPHKRKTQLKAAGCCEEMRELKAQVANLSSLLGELSRKQESDWVSVVMQVMELESSSKHMESRLSTAESKYSEMNNQIDIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDEFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYQDWRQYKQGFGSIRGDFWLGNEHIHRLTRQPSRLRVELEDWEGNARYAEYSYFALGNELNSYRLFLGNYSGNVGKDALLYHNNTVFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHRKHMDGISWYGWHGANYSLKRVEMKIRPEAFKP
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Has a role in the formation and organization of the extracellular matrix. In the eye, it functions as a mediator of dexamethasone-induced matrix deposition in the trabecular meshwork, the tissue responsible for the outflow of the ocular aqueous humor and for the maintenance of intraocular pressure (By similarity). Is a negative regulator of angiogenesis in the cornea, and plays a major role in maintaining corneal avascularity and transparency (PubMed:25622036). Homotetramer; disulfide-linked.
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Q9NQZ1
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MPVPALCLLWALAMVTRPASAAPMGGPELAQHEELTLLFHGTLQLGQALNGVYRTTEGRLTKARNSLGLYGRTIELLGQEVSRGRDAAQELRASLLETQMEEDILQLQAEATAEVLGEVAQAQKVLRDSVQRLEVQLRSAWLGPAYREFEVLKAHADKQSHILWALTGHVQRQRREMVAQQHRLRQIQERLHTAALPA
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Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (By similarity). Interacts with ANGPTL3. Predominantly expressed in liver. Also expressed in adipose tissues. Transcripts are up-regulated by 100 fold during adipogenesis. In response to food intake. Stimulated by insulin. Proteolytically cleaved at the N-terminus. The gene represented in this entry may be involved in disease pathogenesis. Increased protein levels are observed in the serum of patients. This result should however be reinvestigated in light of recent advances that suggest that this protein is not promoting pancreatic beta cell proliferation. The gene represented in this entry may be involved in disease pathogenesis. Increased protein levels are observed in the serum of patients and are associated with insulin resistance (PubMed:25024395, PubMed:25303484, PubMed:24963292, PubMed:24852694). According to another report, protein levels are decreased in the serum of patients (PubMed:25050901). Discrepancies between increased and decreased levels of proteins levels in NIDDM patients may be explained by the use of different kits developed on the market that either use antibodies recognizing the N-terminal or the C-terminal part of the protein (PubMed:25099942). These results should however be reinvestigated in light of recent advances that suggest that this protein is not promoting pancreatic beta cell proliferation. Belongs to the ANGPTL8 family. Initially reported to specifically promote pancreatic beta cell proliferation without insulin resistance and to promote beta cell mass expansion, thereby improving glucose tolerance (PubMed:23623304). However, this result could not be confirmed by further studies and the original paper was later retracted (PubMed:28038792). The lack of a role in beta cell proliferation was also confirmed in another study (PubMed:25417115). Extended N-terminus.
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Q8R1L8
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MAVLALCLLWTLASAVRPAPVAPLGGPEPAQYEELTLLFHGALQLGQALNGVYRATEARLTEAGHSLGLYDRALEFLGTEVRQGQDATQELRTSLSEIQVEEDALHLRAEATARSLGEVARAQQALRDTVRRLQVQLRGAWLGQAHQEFETLKARADKQSHLLWALTGHVQRQQREMAEQQQWLRQIQQRLHTAALPA
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Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577, PubMed:24043787). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (PubMed:24043787). According to a report, may act by promoting ANGPTL3 cleavage (PubMed:23150577). According to another study, not required for cleavage of ANGPTL3 (PubMed:24043787). Interacts with ANGPTL3. Expressed in liver and fat. Enriched in white and brown adipose tissues. Expressed during adipogenesis. Highly up-regulated following high-fat diet treatment. Down-regulated upon fasting. Strongly induced in the cold environment (4 Degrees Celsius for 4 hours). Proteolytically cleaved at the N-terminus. Reduced levels of serum triglyceride (PubMed:20562862, PubMed:24043787). Mice gain weight more slowly than wild-type littermates due to a reduction in adipose tissue accretion. Plasma levels of triglycerides are similar to wild-type animals in the fasted state but decreased after refeeding. The lower triglyceride levels are associated with a reduction in very low density lipoprotein secretion and an increase in lipoprotein lipase (LPL) activity (PubMed:24043787). Glucose and insulin tolerance are not affected and no alterations in glucose homeostasis are observed in mice fed either a chow or high fat diet (PubMed:24043787). Moreover, deletion does not affect the compensatory proliferation of pancreatic beta cells in response to insulin resistance induced by a high-fat diet or treatment with the insulin antagonist S961 (PubMed:25417115). Belongs to the ANGPTL8 family. Initially reported to specifically promote pancreatic beta cell proliferation without insulin resistance and to promote beta cell mass expansion, thereby improving glucose tolerance (PubMed:23623304). However, this result could not be confirmed by further studies and the original paper was later retracted (PubMed:28038792). The lack of a role in beta cell proliferation was also confirmed in another study (PubMed:25417115).
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Q4R1I9
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MGGDAIVLYPYPGLGHLISMVELGKLLLTHHPSFSITILASTAPTTIAATAKLVASSNDQLTNYIKAVSADNPAINFHHLPTISSLPEHIEKLNLPFEYARLQIPNILQVLQTLKSSLKALILDMFCDALFDVTKDLNIPTFYFYTSAGRSLAVLLNIPTFHRTTNSLSDFGDVPISISGMPPIPVSAMPKLLFDRSTNFYKSFLSTSTHMAKSNGIILNTFDLLEERALKALRAGLCLPNQPTPPIFTVGPLISGKSGDNDEHESLKWLNNQPKDSVVFLCFGSMGVFSIKQLEAMALGLEKSGQRFLWVVRNPPIEELPVEEPSLEEILPKGFVERTKDRGLVVRKWAPQVEVLSHDSVGGFVTHCGWNSVLEAVCNGVPMVAWPLYAEQKLGRVFLVEEMKVAVGVKESETGFVSADELEKRVRELMDSESGDEIRGRVSEFSNGGVKAKEEGGSSVASLAKLAQLWKQK
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Sequentially catalyzes two glycosylation steps at the 5-OH and 3-OH positions of anthocyanidin. Unglycosylated anthocyanidin or anthocyanidin 5-O-glucoside, but not anthocyanidin 3-O-glucoside, can be used as glucosyl acceptor. Pigment biosynthesis; anthocyanin biosynthesis. In roses, anthocyanidin 3,5-O-diglucoside is the first stable anthocyanin, and therefore responsible for flower coloration, whereas this is usually anthocyanidin 3-O-glucoside in other plants. Belongs to the UDP-glycosyltransferase family. The color of the rose - Issue 63 of October 2005
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Q08DP8
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MTVFLSFAFLAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEQDFSSQKLQHLEHVMENYTQWLQKIENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKIFEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEVLLKGGKKEEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDLNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYTLRIELLDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development (By similarity). Found to be expressed throughout the ovarian cycle.
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Q60FC1
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MTVFLSFAFLAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVGPDFSSQKLQHLEHVMENYTQWLQKIENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEEWDTLKEERENLQVLVTRQTYIIQELEKQLNRATNNNSVLQKQQLELMDTVHNLVNLCTKEVLLKGGKKEEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYTLRIELMDCEGNRAYSQYDRFHIGNEKQNYRLYLKCHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development (By similarity). Glycosylated.
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Q5HYA0
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MTVFLSFAFLAAILTHIGCSNQRRSPENSGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Homooligomer (PubMed:28601681). Interacts with TEK/TIE2 (PubMed:28601681, PubMed:30689269). Glycosylated. The disease is caused by variants affecting the gene represented in this entry. It may have a potential therapeutic utility since it can be used for specifically targeting tumor vasculature or for promoting angiogenic processes in certain organs such as an ischemic heart. Angiopoietin entry
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Q6NWV7
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MTVFLSFAFFAAILTHIGCSNQRRNPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTVHNLISLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme (By similarity). Homooligomer. Interacts with TEK/TIE2 (By similarity). Early in development, at 9 dpc to 11 dpc, it is found most prominently in the heart myocardium surrounding the endocardium. Later, it becomes more widely distributed, most often in the mesenchyme surrounding developing vessels, in close association with endothelial cells. Embryonically lethal. Embryos die at about 12.5 dpc, due to important developmental defects of the endocardium and myocardium, plus generalized defects in vascular development.
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Q9BDY8
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MTVFLSFAFLAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEQDFSSQKLQHLEHVMENYTQWLQKIENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELKKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEGVLLKGGKKEEVKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDLNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYTLRTELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHSGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development (By similarity). Glycosylated.
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Q8K4Q4
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MTVFLSFAFFAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVETDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYELEKQLLQQTNEILKIQEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTFIIQELEKQLSRATSNNSVLQKQQLELMDTVHNLVSLCTKEVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNEGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNQKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development.
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