ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P81559 | MTMPLPNKTTGVTFLHQIQSSELETLTRPPLKISLERPLGEMYVENNRTGIFNYPEGTTYDFAAAAAPVYSSASLSYAASSETFGSSSLTGLHTLNNVPPSPVVFLAKLPQLSPFIHHHGQQVPYYLESEQGTFAVREAAPPTFYRSSSDNRRQSGRERMSSANDKGPPSMESTKETRYCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRLLKHKRQKEEQEQKNDVDPSEIRTASIWVNPSVKSMKLSPVLSLTAEQLISALMEAEAPIVY... | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 66081
Sequence Length: 586
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
O24618 | MASRMGMVAILSLFVCALVASTSVNANVWQTDEDAFYSTNKLGVNGNMEMAQQQGGFIGHRPRLASFNRASKQLDREKRPVPSGPDPIHHSIPSHAPQHPPSYGKAPYEDDKSIASPGLSNLIGPPPFLDRY | Function: Extracellular signal peptide that regulates cell fate.
PTM: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-85 enhances binding affinity of the ESR2Bp peptide for its receptor.
Sequence Mass (Da): 14358
Sequence Length: 132
Subcellular Location: Secreted
|
O24572 | TRTDDKPGVNRNMEMQQQQGGFIGHRPRLASFNRASKQLDREKRPVPSGPDPIHHSIPSHAPQHPPSYGKAPYEDDKSIASPGLSNLIGPPPFLDRY | Function: Extracellular signal peptide that regulates cell fate.
PTM: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-50 enhances binding affinity of the ESR2Cp peptide for its receptor.
Sequence Mass (Da): 10790
Sequence Length: 97
Subcellular Location: Secreted
|
O13012 | MAGSPGNELPLLQLQEVDSSKVGESGGSSGLLPTMYNGALPALSMESHAVCIPSPYTDSSHDYAALTFYSPPILSHGGPAVPESPAARQSLSPSLFWPAHGHHGHVSPLALHFQQPLVYREPAHSPWAEPKPLEHGQAQTSKLAGKRMAESEEGTSSVGGCFAGKGDMHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNGYICPATNQCTIDKNRRKSCQACRLRKCYEVGMMKCGVRRERCTYRGARHRRMPHIRELAGTGGGARTQRRGEGVVPQTQEAQSSALTPEQLINRIIEAEPPEIYLMKELKKPFTED... | Function: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.
Sequence Mass (Da): 63421
Sequence Length: 573
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding ... |
Q9C6I6 | MTRTVLLRALTKNKFVASNAPRSISISITSLSRCISTLILAEHESGTIKPQTVSTVVAANSLGESSSISLLLAGSGSSLQEAASQAASCHPSVSEVLVADSDKFEYSLAEPWAKLVDFVRQQGDYSHILASSSSFGKNILPRVAALLDVSPITDVVKILGSDQFIRPIYAGNALCTVRYTGAGPCMLTIRSTSFPVTPITANSESKKATVSQIDLSNFEDDSVSKSRYVGRSTQDTERPDLGSARVVITGGRALKSVENFKMIEKLAEKLGGAVGATRAAVDAGYVPNDLQVGQTGKIVAPELYMAFGVSGAIQHLAGIK... | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
Q2KJE4 | MFRAAAPGQLRRATSLLRFQSTLVIAEHANDTLAPITLNTITAAKHLGGEVSCLVAGTKCDKVAQDLCKVAGVAKVLVAQHDAYKGLLPEELTPLILATQKQFNHTHICAGASAFGKNLLPRIAAKLDVAPISDIIAIKSPDTFVRTIYAGNAICTVKCDEKVKVFSVRGTSFEAAAASGGSASSEKASSTSPVGISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVTNDLQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLF... | Cofactor: Binds 1 FAD per dimer.
Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone... |
Q93615 | MLSARTVLSRAGLISNASRLNSTLVVAEHDETKLAPITLNAITAASKLGNEVSVLVTGANATKVAEQVAKVNGVKRVLVAQDEKLKNNLPERVAPVILASQKQFNFTAITAGSSAFGRGVIPRVAAKLDVSSISDVTEVHSADSFTRTLYAGNAVKKVKSTAPIKLLTFRGTSFEPAKEGGSGAVENAPSADIKTDLSEFLGQELSKSERPDLATAKVVVSGGRGLKSGDNFKLIYDLADKLGAGVGASRAAVDAGYVPNDMQVGQTGKIVAPELYIAIGISGAIQHLAGMKDSKVIVAINKDPDAPIFQVADIGLKADL... | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
Q8J112 | MLYRSALRASCGFTPRLASTRSRLASSLVLLEHKAGRLNDASLSAVTAAKATGNDTHGILVGSMAEVEGVLKEAKKIKDLSKIYLATSDAYSHSLAEALAPLLASIVPTKDVSHVFAAHTAVGKNVFPRLAGMLDSSLVADIIALDPSRGTFTRPIYAGNAVLTVKSSPKDSVKIVTVRSTAFDKAAIADGSADVEDVEILAIESPTQFISEELTVSSRPDLASAARVVSGGRALKSKESFDKILDPLADSLGAAVGASRAAVDAGYADNSLQVGQTGKVVAPELYVAVGISGAIQHLAGMKESKMIVAINKDPDAPIFQ... | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
Q54FD7 | MIGRLNLITKSNLFKNVNNLNNKNYYSTCLVIAEHDNNQLLNSTLNTITAASKLGVTNISVLVAGSKCGPVADSVSKVSGVTNVVCVDHPTLEHSLAETITPIIVKLQSSSSKEGDEITHIFTPASNFGKNFLPRVAALLNVSQISEITKVKDAETFQRPIYAGNAIATVKSTDKCKVGTVRTTAFDKAPTSGGSAKVVSANDWAVPLIEKAISETNIKWESSEVKKSERPELTSARVVVSGGRGMKNGENFKMLEELADTLGGAVGASRAAVDSGFVSNDLQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKVIVAI... | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxi... |
P13804 | MFRAAAPGQLRRAASLLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLF... | Cofactor: Binds 1 FAD per dimer.
Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinon... |
P9WQK2 | MAEFIYTMKKVRKAHGDKVILDDVTLSFYPGAKIGVVGPNGAGKSSVLRIMAGLDKPNNGDAFLATGATVGILQQEPPLNEDKTVRGNVEEGMGDIKIKLDRFNEVAELMATDYTDELMEEMGRLQEELDHADAWDLDAQLEQAMDALRCPPADEPVTNLSGGERRRVALCKLLLSKPDLLLLDEPTNHLDAESVQWLEQHLASYPGAILAVTHDRYFLDNVAEWILELDRGRAYPYEGNYSTYLEKKAERLAVQGRKDAKLQKRLTEELAWVRSGAKARQAKSKARLQRYEEMAAEAEKTRKLDFEEIQIPVGPRLGNV... | Function: A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome... |
P50549 | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDNDEQFVPDYQAESLAFHGLPLKIKKEPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRTEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEP... | Function: Transcriptional activator that binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3' . Required for olfactory dopaminergic neuron differentiation; may directly activate expression of tyrosine hydroxylase (TH) (By similarity).
PTM: Sumoylated.
Sequence Mass (Da): 55131
Sequence Length:... |
Q9PUQ1 | MDYKMDGYLDQQVPYTLANRSQGNGPLNRLLMATKRKYMDAELPPQESEDLFQDLSQLQETWLTEAQVPDSDEQFVPDFHSENSVAFHSPPVKIKKEPQSPGSDPSQSCSHKQSFSYPNGEQCLYASAYEQKRAAVAGAGGSKSSCPATPMSPMQHYSPKPTVGTRQESGYMNPPSSSQSHACHSHSYPMNPSSRFPSGSAEMCPPFASQGQALQRIDPAHASGGGGGGYHRQHSDPCLPYPPQQTFKQEYMDPLYDRAAHINGPQPQRFPPAHMMVKQEPTDYTYEPDVPGCPSMYHHNEGYSNPQHNSEGYMFENDSR... | Function: Transcriptional activator that binds to the (5'-CCGGA[AT]-3') motif. May control the acquisition of specific cell fates at an early stage during development of the somites and nervous system. May mediate the cellular effects of the fibroblast growth factors on embryogenesis.
PTM: Phosphorylated.
Sequence Mass... |
P43268 | MERRMKAGYLDQQVPYTFSSKSPGNGSLREALIGPLGKLMDPGSLPPLDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENLAFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDPPRQIAIKSPAPGALGQSPLQPFPRAEQRNFLRSSGTSQPHPGHGYLGEHSSVFQQPLDICHSFTSQGGGREPLPAPYQHQLSEPCPPYPQQSFKQEYHDPLYEQAGQPAVDQGGVNGHRYPGAGVVIKQEQTDFAYDSDVTGCASMYLHTEGFSGPSPGDGAMGYGYEKPLRPFPDDVCVVPEKFEGD... | Function: Transcriptional activator . May play a role in keratinocyte differentiation .
PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation, it positively regulates the transcriptional activator capacity. Sumoylation at Lys-96 probably requires phosphorylation at Ser-101. Transiently polysumoylated and des... |
P28322 | MERRMKGGYLDQRVPYTFCSKSPGNGSLGEALMVPQGKLMDPGSLPPSDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENSFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDSPRQIAIKSPAPGAPGQSPLQPFSRAEQQQSLLRASSSSQSHPGHGYLGEHSSVFQQPVDMCHSFTSPQGGGREPLPAPYQHQLSEPCPPYPQQNFKQEYHDPLYEQAGQPASSQGGVSGHRYPGAGVVIKQERTDFAYDSDVPGCASMYLHPEGFSGPSPGDGVMGYGYEKSLRPFPDDVCIVPEKFEG... | Function: Transcriptional activator . May play a role in keratinocyte differentiation (By similarity).
PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation it positively regulates the transcriptional activator capacity. Sumoylation at Lys-95 probably requires phosphorylation at Ser-100. Transiently polysumo... |
A0A396JG59 | MHKKQLMALLMVPQTSDSQDATITKLESAYSDLESLLRSSKQMEQNIETMETRFDLLHGSITTASRRVHPLQSLSMSRKALDTRINRAISPALALLETFKLAESLQNNLLNLSSKLSTEKTHQKRLSKLLDYMDCVDQLNEAINSISEVVEPVIMRLQEVVEFISRTKAADQYRTQRLREALITLKALYETEVDEMRFEGLLDQALLHMQDEFEVLLLKLKHRKLGDMSHMQNGGEDCDDHFEVSFELGSELEIEVLRRISNTLAANDCLDICIDIYVKVRYKRAAKALMKLNPDYLRTYTPEGIDEMEWENLETSITLW... | Function: Component of an exocyst subcomplex specifically required for periarbuscular membrane (PAM) biogenesis during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme), especially critical during the early branching phase of arbuscule development; probably involved in STR and STR2 delivery i... |
B0BZ38 | MTSYQPNLLVPPEVLSVKGLTDYIQTLLEDDSYLVQVWVEGEVSSAARHRSGFFFTLQDQQEAASIHCVIWNSYCDQLVIEPEVGEQILALGRIRVYPQRGQYQLMAWQLFPAGEGLRSLRYQQLRERLTREGLFDPLQKQALPTYPQTVGVVTSHQAAAWGDIKRTLKAQHPGLKVLFSPTKVQGKQAPEAIVLAIERVIKDGRAEVLIVARGGGATEDLACFNDERVVRAIAECPIPVISGIGHQRDETLADLVADVCAHTPTAAAECIPRLTDWQTDYRNCIARLYIILTRQLDVAHEHLLYQKTRLRRLQIDRQFE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4740... |
A9NFG5 | MNEQKYLSVSALTEYIKVKLENDNHLKRVFLKGEISNFTHHGSGHLYFSLKDEDAAISAMMFKTYASTLSFKPKAGDKVLVEGYISLYKARGTYSISIFSMTLDGIGELFLKYEQNRKMFQELGYFDESLKKPIPKFPKIIAVITSETGAVIQDIKTTISRRYLLAKIELYPILVQGEGSKDDIVKTLARVNRESQADVIILGRGGGSIEDLWSFNEAEVVVAIHQSKIPVITAIGHETDTTLSDYVSDLRAPTPTAAAELATPNMADLIKEIKDKVQLSQYYMNERIKNYTALILNLDERLELASPKSKLELEHKQIDN... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5080... |
A0LW37 | MALTSSAESPVPVREVARQIGLWVGRLGRIWVDGQLTQIKIRPGTNTVFFNLRDPSANVTLLATCPRQVFECIEPKPTEGLRVAVLGKPEFYVPRGSLQLVVHDIRPIGIGDLLARLERLKKILAAEGLFAPERKRPLPFLPRVVGLICGRGSAAERDVVENARRRWPAVRFDIAAVAVQGPYAVPEIVAALRRLDDDPVVDVIVIARGGGSVEDLLPFSDETLLRAVAACRTPVVSAIGHETDTPLLDFVADVAASTPTDAARRIVPDVAEQYAQLAQLGDRLRNALRHRIDREQQVLDTLRSRPVLAHPVQDINRRGE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4529... |
Q0VNE8 | MTISSRAEPLSISQLNLDAQGLLESSFPLIWLQGELSNFSRPASGHWYFSLKDTRAQINGAMFRNRNRLLNFAPQNGEQVLVRAKITLYVPRGNFQIVVEHMEPAGQGALKAQFDALKAQLQSEGLFAQEHKRTLPAWPNQIGVITSPSGAAIRDILQVLQRRCPSIPVLIYPAAVQGAEAPAQLRQALALAVARNECDVLILGRGGGSLEDLWAFNDEGLARAVANCPIPIVSAVGHEVDTGLTDFAADLRAPTPSAAAELVSPDLSIVSQRLAGLHRRLRWVMAQELRTVQERLRHLSQRLRSPRQHLEQSSQRLDEL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4985... |
Q5WF60 | MAGNAGVAEAWTVSEATRYIKQLLEDDPHLPEIWIRGELSNFKQHTRGHMYFTIKDEGSRMQAVMFAGYNRFLRFKPENGMNVLIRGEINVYEPYGQYQFYAKEMQPDGIGSLFAEYERLKKALEAEGLFAEERKRPIPRFPTHIAIITSPTGAVIRDMMTTLKRRYPQIRVTLFPVLVQGEGAPLSISRALEQASMANIFDVVIVARGGGSIEELWAFNEEMVARAIAEAAVPVISAVGHETDFTISDFAADRRAPTPTAAAEFAVPDARELMEHIGHLKKRLERSLVEQVKTRRRELERLKRSYAFRYPVQLVHQKEQ... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5210... |
A8MFJ1 | MQIKALSVSEVNQYMKRILGSDPILSHIYVKGEISNYRLHSSGHMYFTLKDKNSKISCVMFKGNCEKLKFFPEEGMSLVCKGYVSIYEKDGQVQLYVNDMEPSGIGALHLAFQQLKDRLNKEGLFDTKYKQEIPLIPRRIALITSPTGAAIRDMVSIILRRFPQVELCIFPVLVQGEGAVETIVKAIELCNRYPGIDLAIVGRGGGSIEELWAFNEEKVARAIFNSRVPIISAVGHETDFTISDFVADLRAATPSSAAELAVPNRVELREYIDSMEKRMIHLMKTKLNTSYQKLSFIENSYFFRYPLNPIYDKQQYINDL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4646... |
B9KHB8 | MSLRSCSTEMIPEFTVTEITDLVRQVMHDTFYCIKIRGEISGLSRPSSGHVYLSLKDDNSVISAVCWHGTRLDVQFENGLEVICTGHISTYQSRYQLVIEGMVLAGQGKLAAMLEERRKKLEKEGLFDQARKKPLPLLPLKIGVITSPTGAVIRDILNRVKHRFPSHIIVWPVQVQGSQASAMVVQAILGFNNLEEPPDVIIVARGGGSIEDLWPFNDEELARTAAASKIPIVSAIGHETDFTIIDYAADVRAPTPTAAVEIVLPERQQLVSDIAHKLSKIRSAVRNVLGAKEHRLLQLYGVLTETKHKISEVGRSALAH... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4410... |
Q836W6 | MTQQYLTVTALTKYLKRKFDADPYLGRVYLTGEISNFRFRANAHQYFSLKDDHAKISAIMFKSAFQKLKFQPKEGMKVMVVGRISLYENSGSYQIYIEHMEPDGVGALYQALAELREKLGKEGLFEGPKQQLPRYPKRIAVVTSPSGAVIRDIITTVKRRYPIAQLVLFPTLVQGEQAADDIVRNIQRADAQSDFDTMIIGRGGGSIEDLWPFNEEKVARAIHAATTPIISSVGHETDVTIADMVADVRAATPTAAAELAVPVLNEELLRISERRSRLEQSFLYLLQQRTERFQRLQNSYVFKQPERLYEGQTIKLDRMT... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5111... |
B1YLQ2 | MTNPLQVSELVQYVKRELENDSLLQQVQVVGEVSNFKRHSSGHLYFTLKDEQSRMKAVMFARDASRVKTDIRDGARVIITARISVYVASGEMQLYVERMMEDGVGALYEAYVQLKEDVEARGWFEAEQKLPLPAFPQKIGIVTSPKGAALHDIATTLRRRYPQAAIVFAPVLVQGKEAAPQIVRAIEWMNEHQACDVMIIGRGGGSIEELWAFNEMPVVTAIHQSRIPIVSAVGHETDFTIADFVADVRAATPTAAAELVTPEAAELAKRLNELNRRLTRHYAQYITERKDQVQRLATSYGLKSPRVLLGLKQERLDRAE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5074... |
C4L3F5 | MANPLPVSEVVRYVKRQLDDDVLLRQVAVIGEISNFKRYSSGHCYFTLKDDASRMKAVMFSRDAKQLQFEPKDGMKVIAVSKVTMYEATGDVQLYVELMRQDGIGLLFERYEARKRELEEMGWFDDERKKPLPMFPERVGIVTSPKGAALHDIATTLRRRAPHVAITFAPVAVQGEMAAPQVASAIRWMNERTDCDVLIVGRGGGSIEELWAFNEDVVVEAIYASTIPIISAVGHETDFTLSDFVADVRAATPTAAAELATAMIDAQRKDVERLDNHLHKAVRSQLDESRSRVERMINSYGLKSPRYTISQKRERFAQSE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5085... |
Q8REN3 | MEKIYSVSEFNRMVKSYIDDIDDFQEFFIEGEISNITYYKSGHLYFSIKDSKSQIKCVAFNYKLKRIPEDLKEGDLVKLFGDVGFYEARGDFQVLARYIEKQNALGSLYAKLEKVKEKLTGLGYFNEEHKKDLPKFPKNIGVVTALTGAALQDIIKTTRKRFNSINIYIYPAKVQGIGAEQEIIKGIETLNKIKEIDFIIAGRGGGSIEDLWAFNEEEVAMAFFNSKKPIISAVGHEIDFLLSDLTADKRAATPTQAIELSVPEKESLLEDLKAREIYITKLLKSYVDSMKRELLLRIENYYLKNFPNTVNSLRESIVEK... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4646... |
Q75TC0 | MEVKYVTVGALTKYIKRKFDVDPHLRDLWVKGEISNFKQHSRGHMYFTLKDSQGRIAAVMFAGYNQHLPFRPEDGMNVLARGEISVYEPNGNYQLYVKEMQPEGVGSLYLAYEQLKQRLEAEGLFSPVHKKPLPAFPRCIGVVTSPTGAAVRDIMTTIRRRYPLAKVILFPALVQGDGAAPSIVRAIERANSFGGVDVLIVGRGGGSIEELWAFNEEIVARAIFASKIPIISAVGHETDFTIADFVADLRAPTPTAAAEMAAPHVGELAERLAERKWRLIRAMKEQLAADKEQLRRLQGSYAFRYPKRLYEQKEQQLDAL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5118... |
Q74CA7 | MDIFSEKRILTVSQLTSLIRGVLEENFEHVWVEGEVSNLATPASGHLYFTLKDGAAQIRCVMFRASSRALKFRPRDGMGLIVRGRVTVYDQRGEYQLLVEYLEPRGIGALQLAFIQLKEQLAREGLFADEHKKPIPPLPQKIGVVTSATGAAIHDILTVLNRRFANVEILIRPVKVQGEGAAEEIAAAIDDFNRYGVIDVMIVGRGGGSLEDLWAFNEEMVARAIHRSRIPVISAVGHEVDFTIADFVADLRAPTPSAAAELVVKSKEELAARLEFLRHRLVQGGRQVLAERRGELDSLNRSLRDPSMLVGHLSQRVDDL... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4959... |
Q30SS1 | MYTLSVSSLNEQIKALLEESFSRVLVEGELSRITFHSSGHIYFTLKDENSTIKAVIFKANAAKLKFQLQEGLKVILDGAITLYKPRGEYQINCFSISPAGHGALALAYEQLKNRLASKGYFESSRKKQLPKFPKRIALITSATGAAVADMLRVAMSRYRAIEIDIYDVLVQGDNAAPSIIRALSLADTKGYDIIVLGRGGGSIEDLWAFNEEIVADAIFSAITPIISAVGHEIDWVISDFVADLRAPTPSAAMEMCLPDEKELYQFIDSLVARYEQMISQKLYGVKQELEHISRLYQDHSIEKKISYKLEEIAQLKLSFT... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4677... |
Q3A3Z3 | MNISEGTVSVSRLVYLLKEVVEDNFVQVLVTGEIANFSAPSSGHYYFAVKDDQAQLRGVMFRSSNRLLKFTPENGMQVLCGGRVSLYPQRGELQLVVDRMEPLGVGSWQLAFEKLKTKLDAEGLFEVGRKRRLPSFPRTIGVVTSPTGAAIHDILNVLRRRGAGLHVLLSPVRVQGDGAADEIARAIADFNRHGQADVLIVGRGGGSPEDLWAFNEEVVARAVFASRIPVISAVGHEVDVTISDLVADLRAPTPSAAAELVVQGRQELERHVDHLVMRLSGQMQGRLSLLKERLDGLRRRLRSPVDDLRRQYRDLEQLRK... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4421... |
B9M0X4 | MAVEKFETALKKLEEVVKKLEGGELSLEDSLKAFEEGIKQAAFCSKKLNEAEKRVEVLLKQKDGRFITEQFQPEDE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8703... |
Q75TB9 | MTDVKKNENMTFEEAMKKLEEIVEKLEEGNVPLEEAIAFFQEGMKLSKLCHDKLQHVEKQLEYMLREDGELVPFSPEEE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9302... |
Q74CA8 | MAVEKFETALKKLEDVVRKLEGGDLSLDDSLKAFEEGVKMASFCTKKLDEAEKKVELLLKKKDGTFVREDFRLDDE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8698... |
A9HIR6 | MTEDLSQLSFEDALAQLEEIVRQLEGGQLRLQDAIASYERGAALRRYCDTKLNEADARVQAIIQRADGALETKSMD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8500... |
Q5FUB3 | MPEPIDAMSFEDALSELERIVRGLEGGQMKLEDAISAYERGAALRRHCDAKLGEAEMRVRAIVQNDDGTTGTEPLADTGESGR | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9006... |
Q7VLU0 | MAKKPTQNFETTLQELESIVNHLEAGDLPLEQALTEFETAIKLVQQGQQRLQQAEQRIQILLNKDEQAELADYE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8509... |
P43914 | MARKPASSQDFETTLVQLENIVTHLENGDLPLEEALKEFEQGVQLAKLGQERLQQAEQRIQILLQKTEDAPLNDYKGNDYEGNA | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9512... |
Q9K968 | MIKNEQPPLSFEEAMEQLEEVVEQLEQGDVPLEEAISMFQKGMNLSKVCHEKLATVEKQMDQILKEDGNFEETVLQEEQE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9268... |
A1WYI6 | MSETDSQETAPQGDLPDFERSVAELEALIERMERGEQTLEEALRDFERGIHLTRHCQKALSAAEQKVAILLENSEDGDVGPFRPDDS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9757... |
B0TEJ2 | MAKGKANLNLTYEAAIGRLEEVVRSLETGEASLDESLKLFQEGIGLVRHCHSQLDAYEAKVQRLIETPDGAAVVEERRTEEGE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9170... |
B6JNY0 | MQDELFETEKAPPKNAKNAPKKSFEEHVHSLEQAIDRLNDPNLSLKDGMDLYKTAMQELFLAQKLLENAYLEYEKLQTTDKKA | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9626... |
A3CLQ8 | MSKEKKFEENLADLEVIVQKLENGDVALEEAIAEFQKGMKLSKELQASLDKAEKTLVKVMQADGTETEME | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 7859... |
Q67NB3 | MTQELSFEEAIQRLEQVVRELESGDLPLERGLELFQEGVALARHCTALLDRAEARIEQLLERDGGVETLPFEPE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8421... |
Q2LUA0 | MAKEKFEEAMAKLEALVRKMETGDMTLEESLKAFEEGIRLSRLCASRLDDAERRVEMLIAENSNVTVQPLRENGEKNES | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9017... |
Q31R15 | MAKAKPAWSYETAIAEVEQIVQQLESGELPLAEVVEQFQQASQRLQQCDRFLRDKQAELDLLIESLDEPPVPPQ | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8421... |
A0LI55 | MAKKKSDQFEEALKKLQDIVEKLERGDMPLEEAMEAFSEGIRLARVCHGKLEEAERKVRILLKEQEGDWTTSPFEPASGEPPGG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9471... |
Q0AZF3 | MEKLSFELALKKLEESVEQLESGELELEESIKVFEQGIELSLFCRKELSQAEGKIQRLVKNLGGEFELLDFEV | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8405... |
Q2TZQ9 | MKVTRLAVLNTLATLTVAWLPTTDKTITSSNGTDLFKASHGKIRGVNLGSQFVFEPWIATKAWSELGCEGQESEFDCVMKLGQDAANKAFAKHWDSWITKEDIKEIRSYGLNTIRIPVGYWMNEDLIYHDSEYFPHGGFAYLEKLCGWASDAGLYIIIDLHGAPGAQVAKNAFTGQFADTPGFYVDFQYQRALEFLEWMTIKVHTLHNFRNVGMLEVVNEPVQNPQVTTTLRSNYYPNAFHSIRKVEGALSIDRKDYLHIQMMDGAWGAGDPHEHLTDDYYAAYDNHRYLKWDPRVEVSKDSYIKTSCNDNVATNWPAII... | Function: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides (By similarity).
Catalytic Activity: Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.
Sequence Mass (Da): 46614
Sequence Length: ... |
Q5B6Q3 | MKFILPLFTSLPVALAWLPGIDKDIYSAAGTNIFNVTSASSKRWLPASKKIRGVNLGSHFVIEPWMASMAWSNMGCSGQRSEFDCVMALGQETADQAFADHWGSWITQDDINQMVQYGLNTIRIPVGYWLKEDLVYADSEHFPKGGIGYLEDVCGWASDAGMYIIIDLHGAPGAQQPKQPFTGQYAPNPGFYQDYQYDRALEFLEWMTTSIHQNNKFRNVGMLEIVNEPVQNADQASSMINSYYPSAFTRIRNTESSLGITSNNYLHIQMMNEKWGSGDPTQSLTDNYFAAYDDHRYVKWDSSVAVDKESYISASCVDDR... | Function: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
Catalytic Activity: Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.
Sequence Mass (Da): 46267
Sequence Length: 409
Subcellular ... |
A2QX52 | MPGHSRSRDRLSPSSELDDADPVYSPSVYQREHYYNNDSLFDSADDDYTRTPRNVYSYETHDEYHDDDDDDDDVHEHDHDHEYDDKFEEPWVPLRAQVEGDQWREGFETAIPKEEDVTQAKEYQYQMSGALGDDGPPPLPSDALGRGKGKKRLDRETRRQRRKERLAAFFKHKNGSASAGLVSGDALAKLLGSQDGDEDCLSHLGTERADSMSQKNLEGGRQRKLPVLSEEPMMLRPFPAVAPTGQTQGRVVSGAQLEEGGPGMEMRHRGGGGPPAEGLLQKEGDWDGSTKGSSTSARPSFWKRYHKTFIFFAILIVLAA... | Function: Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (By similarity).
Catalytic Activity: Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.
Location Topology: Single-pass type II membrane protein
Sequence Ma... |
Q5AVZ7 | MPSQSRSRDRYGRDSDRDRSRVQPRRRYHVSEDDDDDDDFDDNPRDRRYRRDGYRRAPVDSRAYDSHDDYEVVDVEEEPRRYRSDTERRRERARASPGTSPRKRERTRDSGGGHRRRRTEESDGSQAPQAHRDRRSRTRRDRGLDDEDLEDAARRLRRRERERERERRAETSKHKSTDSSNSSAGLLNANALAKLRAQHEELDRQEQRRAEKEAKAERKRRRKRPAVEGQMRTLDPFPDEVPRGQSKGRIVSGAYLEEGRAPDMEVRLRGGGRGPPRERRWEKDSDGSAPLTPFWKRKKWWWIGAIVLVIVVIIIVVAVV... | Function: Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan.
Catalytic Activity: Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 95363
S... |
Q96V64 | MLYPRALLPAAVALASLVLAVPLEERQLAFDFNNQKVRGVNLGGWFVLEPWITPSIFQQWANGGDVIDEYSYTAALGKDEAFTRLNNHWATWITEEDFAEIASMGLNHVRIPIGYWALVAIPNDPYVQGQLSYVDRAIDWARKNGLKVMLDLHGAPGSQNGFDNSGRTGTIAWQSGDNVPNTLRAIQALAERYAPQTDVVTAIELLNEPANWGNDLSQIKKFYYDGWGNVRTQGQTAVTIHDAFLDPRSWNGFMNSEAGVNNVILDTHIYQVFSQNEVAMKPCAHVQTACSSIDKIKPTDKWTIVGEWTGAQTDCAKWLN... | Function: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).
Catalytic Activity: Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, re... |
Q558Z9 | MSAPPRLSARLSVLDQKKSNAPSPTSPTGLKTSLGMPPNSGSSGGGGGLKSSVGISSLPTIPSTKSTSPTLPKRNSANLSLLQQQQQQHTNKSTSPSSNTPTATSTTSPFSYLGKQASAQNLNTMMSMMMLNKNPLSPVVPQPGASLFYATPTEADDEEFEHIRNLLNSEYSVTTVQSTGALKSSNLVVMSWKNNATSELTEQDDQLENDKRDLQFIKEQLEKNNSMSKQMIYILDRFNEGLSQLEMDVAPINASMNEWSSIFNNINSTMEQVKSVLDKFDVDKIDSKINDGAKGDYVSYMLALEHVGNAIDYIAEKSHF... | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94447
Sequence Length: 840
Subcellular Location: Cytoplasm
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Q9UPT5 | MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTKNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKEALESEFRSLMTRHSKVVSPVLILDLISGDDDLEAQEDVTLEHLPESVLQDVIRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFHKSSSSSGVPYSPAIPNKRKDTPTKKPVKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGLLPCTPRGGLPGPWINAAC... | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). It... |
O54922 | MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTKNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKESLESEFRSLMTRHSKVISPVLVLDLISADDELEVQEDVVLEHLPESVLQDVIRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFRKSSSSSGVPYSPAIPNKRKDTPTKKPIKRPGRDDMLDVETDAYIHCVSAFVRLAQSEYQLLMGIIPEHHQKKTFDSLIQDA... | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). It... |
P45632 | MSEAHTFHPTVLREYDIRGIVGSTLTAADARAVGRLRHRGRPAAVRKTVCVGYDGRLSSPELEAAMVDGLVACGLHVLRIGLGPTPMLYFATRDREAAAGIMITGSHNPPDYNGIKMMLGKGPVYGRQILDIGAIASKADYVSGEGSSEQLDIKDAYVERLLRDDDGTRDLTIAWDAGNGASGEDPAPPDREVPGKHVLLFDEIDGNFPNHHPDPTVEKNLVDLKAAVAEHGCDIGIGFDGDGDRIGAIDHLGRVVWGDQLVAIYAADVLKSHPGATIIADVKASQTLFDEIARLGGNPLMWKTGHSLLKAKMAETGSPL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Sequence Mass (Da): 51130
Sequence Length: 469
EC: 5.4.2.8
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P04536 | MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIAPSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTRIEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR | Function: 3'-5' exonuclease that preferentially uses ssDNA as substrate. Plays a role in group I intron homing. May play a role in the final step of host DNA degradation, by scavenging DNA into mononucleotides.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Seq... |
Q52923 | MVCQARFGVKNASRGHRMERPQTVKGKIMAVEFGDSQRSLSDTLTGMIASIRGNTITLRELMIEIGEQGFLLLCALLTLPFLIPVSIPGVSTVFGAAIILISLAITLNRMPWLPKRILDREIATEKLVPTLRKGAALVSKLDRYVRPRLNFLTEGALMNRFNGLMIMAGGVLLMFPLGLIPLSNTLPGIAILLLSLGIIQRDGLMVAGGYFFLVATTVYFAVLGYAAFAAGQGLSHFFVS | Function: Required for nodule invasion. Mutations in this gene lead to sensitivity to alkaline conditions which prevents nodule invasion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26040
Sequence Length: 240
Subcellular Location: Cell membrane
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O01705 | MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQ... | Function: Glycosyltransferase required for the biosynthesis of heparan sulfate . Initiates heparan sulfate synthesis by transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core linker (GlcNAcT-I activity) . In association with rib-1, is also responsible for the alternating addition of beta-1-4-linked glucuronic acid (Glc... |
Q9Y169 | MTKIKNLLSFVTQSRAISHTNPREHILNCLTYGLLVIVALCAGFLLWDLSSSPRDGFFHGKRDSHTLILDLEHIQELAVNPEAEQRARNVNCTFWDCLNIYKCEHDRLKVYIYPLQEFVDEQSDKTATTLSSEYFQILEAVLKSRYYTSNPNEACLFLPSLDLLNQNVFDKHLAGAALASLDFWDRGANHIIFNMLPGGAPSYNTVLDVNTDNAIIFGGGFDSWSYRPGFDVAIPVWSPRLVRQHAHATAQRKFLLVVAQLNILPRFVRTLRELSLAHSEQLLLLGACENLDLTMRCPLSQHHKSLEYPRLLSRGKFCLL... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. Plays a central role in diffusion of morphogens hedgehog (hh), ... |
Q93063 | MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEKRSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGVSVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRWDRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEVDLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRCHKHQVFDYPQVLQEATFCVV... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan .
Catalytic Activity: 3-O-{[(1->4)-be... |
Q9XZ08 | MPPAYDLGHSGEAYQPLDTGSGGGNEACAPNSSSAQIRHSMGFRTSWMRQFRRYKLPMVLLMLLFLVSCLAYRILSVEQDAPPLDLHRSSPLLDAYEDFSAMRAGDLKMRIEEMVRIKSTVSVELRELESRRQKLQSDISQYNQKIEELKQELLREQTELERLKISVEQAQVAQREAVQRNTPDLALPRSLLPNTLPRKSNPITGGMAASCEMHNCFNHSRCSLTSGFPVYLYDPDEHSVQRKGYDIDGFLKTTLKQTLGYNAHIVKDPKHACIYLVLVGEALLEQDLLRNNRYAAQEAEHQQPSTPTLENDCPVDMEKL... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. Plays a central role in diffusion of morphogens hedgehog (hh), ... |
Q92935 | MQSWRRRKSLWLALSASWLLLVLLGGFSLLRLALPPRPRPGASQGWPRWLDAELLQSFSQPGELPEDAVSPPQAPHGGSCNWESCFDTSKCRGDGLKVFVYPAVGTISETHRRILASIEGSRFYTFSPAGACLLLLLSLDAQTGECSSMPLQWNRGRNHLVLRLHPAPCPRTFQLGQAMVAEASPTVDSFRPGFDVALPFLPEAHPLRGGAPGQLRQHSPQPGVALLALEEERGGWRTADTGSSACPWDGRCEQDPGPGQTQRQETLPNATFCLISGHRPEAASRFLQALQAGCIPVLLSPRWELPFSEVIDWTKAAIVA... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate (HS) . Transfers N-acetyl-alpha-D-glucosamine to the nascent HS chain (GlcNAcT-II activity) . Appears to lack GlcNAcT I and GlcAT-II activities .
Catalytic Activity: 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3... |
Q9JKV7 | MLWRRKSFWLALSAFWLLLVLLGVFPLRLAVLPGPLPGRSQGWPRWLDAAFLQSFSQSETNPEDVAQLPRVSRGSSCTWGACFDTSKCRGKVLKIFVHSPAGPTSEAQRRILDSLEGSRYSALSPADACLLLFLPSQDRRGACGPLPPNWNGGRNHLVLSLYPAPCTRLGQAMVAEASPSSDIFRPGFDLALPYLPEAHPLRGGAPGKLQQHSPQPGATLLAVAEEKGRWRITSTHASACLWDRHCEQDPGPQQTYPGETLPNATFCLIPGHRSATSCFLQALQAGCIPVLLSPRWELPFSEVIDWTKAAIIADERLPLQ... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate (HS). Transfers N-acetyl-alpha-D-glucosamine to the nascent HS chain (GlcNAcT-II activity). Appears to lack GlcNAcT I and GlcAT-II activities.
Catalytic Activity: 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-b... |
Q9UBQ6 | MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGKSTMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIPVIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPRKHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDTQNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKLVNIYDSMPLRYSNIMISQFG... | Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains.
PTM: The soluble form derives from the membrane form by proteol... |
O43909 | MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEAGKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLHNCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVILVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQSTFYTVQYRPGFDLVVSPLV... | Function: Glycosyltransferase which regulates the biosynthesis of heparan sulfate (HS) . Initiates HS synthesis by transferring the first N-acetyl-alpha-D-glucosamine (alpha-GlcNAc) residue (GlcNAcT-I activity) to the tetrasaccharide linker (GlcA-Gal-Gal-Xyl-)Ser core linker . May also transfer alpha-GlcNAc residues du... |
Q38913 | MASFLVLAFSLAFVSQTTANYFYSSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYH... | Function: Structural component which strengthens the primary cell wall.
PTM: Extensins contain a characteristic repeat of the pentapeptide Ser-Pro(4). For this particular extensin, a typical repeat of Ser-Pro(3) is found. In both cases, the proline residues are hydroxylated and then O-glycosylated (arabinosylation).
Se... |
Q9M1G9 | MGPSAHLISALGVIIMATMVAAYEPETYASPPPLYSSPLPEVEYKTPPLPYVDSSPPPTYTPAPEVEYKSPPPPYVYSSPPPPTYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVDYKSPPPPYVYNSPPPPYYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVEYKSPPPPYVYSSPPPPYYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVEYKSPPPPYVYSSPPPPYYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVDYKSPPPPYVYSSPPPPYYSPSPKVDYKS... | Function: Structural component which strengthens the primary cell wall.
PTM: Extensins contain a characteristic repeat of the pentapeptide Ser-Pro(4). The proline residues are hydroxylated and then O-glycosylated (arabinosylation).
Sequence Mass (Da): 83015
Sequence Length: 743
Subcellular Location: Secreted
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P06599 | MGRIARGSKMSSLIVSLLVVLVSLNLASETTAKYTYSSPPPPEHSPPPPEHSPPPPYHYESPPPPKHSPPPPTPVYKYKSPPPPMHSPPPPYHFESPPPPKHSPPPPTPVYKYKSPPPPKHSPAPVHHYKYKSPPPPTPVYKYKSPPPPKHSPAPEHHYKYKSPPPPKHFPAPEHHYKYKYKSPPPPTPVYKYKSPPPPTPVYKYKSPPPPKHSPAPVHHYKYKSPPPPTPVYKSPPPPEHSPPPPTPVYKYKSPPPPMHSPPPPTPVYKYKSPPPPMHSPPPPVYSPPPPKHHYSYTSPPPPHHY | Function: Structural component in primary cell wall.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 34225
Sequence Length: 306
Subcellular Location: Secreted
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P14918 | MCPAFSIFFNSRRYSLTPPTYTPSPKPPTPKPTPPTYTPSPKPPASKPPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPATKPPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPATKPPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPTHPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPTPKPTPPTYTPSPKPPATKPPTPKPTPPTYTPTPKPPATKPPTYTPTPPVSHTPSPPPPYY | Function: Structural component in primary cell wall.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 28349
Sequence Length: 267
Subcellular Location: Secreted
|
P24152 | MMGGKAALLLALVAVTLAVVEIQADAGYGYGGGYPTPTPKPPAKGPKPEKPPTKGHGHKPEKPPKEHKPTPPTYTPSPKPTPPPATPKPTPPTYTPSPKPKSPVYPPPPKASTPPTYTPSPKPPATKPPTYPTPKPPATKPPTPPVYTPSPKPPVTKPPTPKPTPPVYTPNPKPPVTKPPTHTPSPKPPTSKPTPPVYTPSPKPPKPSPPTYTPTPKPPATKPPTSTPTHPKPTPHTPYPQAHPPTYKPAPKPSPPAPTPPTYTPPVSHTPSSPPPPPPPPYY | Function: Structural component in primary cell wall.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 29593
Sequence Length: 283
Subcellular Location: Secreted
|
P13983 | MKLSTLFALVLLLQSTAILSLVAAEATTQYGGYLPPPVTSQPPPSSIGLSPPSAPTTTPPSRGHVPSPRHAPPRHAYPPPSHGHLPPSVGGPPPHRGHLPPSRGFNPPPSPVISPSHPPPSYGAPPPSHGPGHLPSHGQRPPSPSHGHAPPSGGHTPPRGQHPPSHRRPSPPSRHGHPPPPTYAQPPPTPIYSPSPQVQPPPTYSPPPPTHVQPTPSPPSRGHQPQPPTHRHAPPTHRHAPPTHQPSPLRHLPPSPRRQPQPPTYSPPPPAYAQSPQPSPTYSPPPPTYSPPPPSPIYSPPPPAYSPSPPPTPTPTFSPP... | Function: Has a specialized structural function, possibly in the mechanical penetration of the cortex and epidermis of the main root.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 65407
Sequence Length: 620
Subcellular Location: Secreted
|
P12260 | MSESSGTAFGGRRAIPPNTSNAAENDPPTVELQGLVPRGFNPQDYLNVTNVHLFKERWDSNKVDHHTDKYSNDKLIVRRGQSFYIQIDFNRPYDPTRDLFRVEYVIGLYPQENKGTYIPVPLVSELQSGKWGAKVVMREDRSVRLSVQSSADCIVGKFRMYVAVWTPYGVIRTSRNPETDTYILFNPWCEEDAVYLEN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to ... |
Q5V311 | MNTLDEIERAVKDTAHYVSGNLANYANRAAGENPSGEQQVGGDVWADDLFFDALAYIDGIGAYASEERSDVVDCGEGYSIAIDPLDGSSNLASNNSVGTIIGVYDAELPAAGREMVASLMVLYGPYTTLTIARSDRDVVQEHLLRDGHSERWGQFELPAEATVVGLAGKTGERSDAFNDIAQSFERDLKLRYGGATVADLAQVLEYGGLFGYPVTSGYPNGKLRVHFESAPLAYLVEAAGGASSDGSQSLLDVEPDGIHDRTPTFLGNAELVDELEAALSET | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 29980
Sequence Length: 282
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
|
B2JVN8 | MECAQPALSDFLADHLAPRRAQGPGVVHAADAEGLCAVIDEIAGTVKRIAARIAQGAIGGARPAMPGDTALGIAVQDLLIAMCERSAGIAGLVLPGMAAARPTSAGRYVLFADSLDGAANAESNVALGTVFSIRHAGAASADGGCVIAGSRQLAAGYALYGPATIFVITVGRGTHGFTLCRERGGFVLTHRSMRVPEQGAELAVNGGNERFWEPPVQRYVSECRDGSAGVRQRDFETRWIASLVADTHRTLMRGGLCLLPRESRCAPRAARQPLLYHAQALAWLVEQAGGLASTGRARLLDAAAGQDTHARTPMFLGTRC... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 37985
Sequence Length: 357
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
|
Q2S1G3 | MTGSHRTSHAGDGAPEDDLGTFQTLEQFILDRQDSFPHSTGAFSRLLRDISLAAKIVNRDMRRAGLLDVYGSTGERNVQGEVQQKMDALAHREFVQALRRGGECCLIGSEEHAEAIPLSTVSKEGDGKYIVLLDPLDGSSNIDVNVSVGTIFSIYRLPDGYEEEEPDPAAALQPGTEQVAAGYVVYGSSTMLVYTTGNGVNGFTLDPSIGEFLLSHPDIQTPSRGRLSSINSGYYHSFEEGLRDYLDWLQQKDPETNRPAKTRYIGSFVSDFHRNLLKGGIYMYPATESSPAGKLRLMYEANPMGFIAEQAGGAASDGHR... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 39652
Sequence Length: 361
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
|
A2SJK3 | MPTGGKSTLTQFLIEERRKHPAATGELNALITDVSLACKAISRKVAFGGLAGVLGSAGSGNVQGEEQKTLDVLSNTMFLRATEWGGHVAGMVSEELEAPYTLPPQYARGKYLLMFDPLDGSSNIDVNVTVGSIFAIHRAPQPRQDPQPQDYLQPGTTMVCGGYAIYGPSTMLVLTLGDGTHAFTLDPQLGEWVLSHPNLRIPEKTREFAINASNSRFWEPAVKRYVDECLAGSTGPRGTDFNMRWIASLVAETHRILMRGGVFLYPRDSKDPNKAGRLRLLYEANPISFLIEQAGGMASTGRKRLLEVQPEDIHQRIGFV... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 39078
Sequence Length: 357
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
|
P25851 | MAATAATTTSSHLLLSSSRHVASSSQPSILSPRSLFSNNGKRAPTGVRNHQYASGVRCMAVAADAAETKTAARKKSGYELQTLTGWLLRQEMKGEIDAELTIVMSSISLACKQIASLVQRAGISNLTGVQGAVNIQGEDQKKLDVISNEVFSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYVVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECIVDDSDDISALGSEEQRCIVNVCQPGNNLLAAGYCMYSSSVIFVLTLGKGVFSFTLDPMYGEFVLTQENIEIPKAGRIYSFNEGNYQMWDDKLKKYIDDLKDPGP... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the irreversible reaction from fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate, to regenerate the primary CO(2) acceptor molecule, ribulose-1,5-bisphosphate (Probable). Involved in the regulation of photosynthetic electron flow and... |
A6GWD9 | MEERNKTLGEFIIENQQSFQYSSGELSRIINSIRLAAKVVNYKVNKAGLVDIVGAAGEQNIQGEDQQKLDVYANEIFIQTLINREIVCGIASEENDDFITVAGSDNSHNNKYVVLMDPLDGSSNIDVNVSVGTIFSVFRRITPVGTPVTIEDFLQPGINQVAAGYVIYGTSTMLVYTTGDGVNGFTLNPAIGTFYLSHPNMKYSKDGHIYSMNEGNYVHFPQGVKNYIKYCQSEEGDRPYTSRYIGSLVSDFHRNMIKGGIYIYPTSSKAPKGKLRLLYECSPMAFIAEQAGGKASDGYNRIMEIQPTELHQRVPFFCGS... | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 37321
Sequence Length: 335
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
|
Q18B55 | MKNLCKISDDYLNSKLKYLKLLSKQYPSISKASTEIINLEAILNLPKGTEHFITDVHGEYEPFVHVLKNGSGVIKRKIEELFSNTIRDSEKKMLATLVYYPEQKLDLIIKQEENIDDFYRINIYRLIELCKYASSKYTRSKVRKLLPENFKYIIEELLHEHVKSEHKEEYYKSIVETIVDIGIAKEFIIAISTVIQKLVVDRLHVIGDIYDRGPRPDIIVDKLIEHHCVDIQWGNHDILWMGAASGEKTCIANALRISARYANLDIVEDIYGINLLPLATFAIEMYKDDPCKEFIPKVNDQSVTTTEKSLMAKMHKAISI... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 76452
Sequence Length: 661
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
|
Q6AMN0 | MAEKICITEIDKLSQKLLRIETELNANIPTTLWISDLHGEGDRFKSILRGRFGMLYQTCKEGLPATFTPEKIQYLAKIVRKKNYFADSQQQMDRQDVILCFVQILKYKLTNSTNRNREIFLPEFRETIGRLLAGLPVPDPIFEESIISDRLIFHLSYAIRQVLLDRIQVLGDVFDRGSQPDKIIRILSSPAYKEMVDYVFGNHDILWMGAAAGTPSLVAETLRITCRYDHFRLLNRLRFDTSRLAEFAERTYEIKKATGKFKAKTDRGRAMEKALTVIQFKLEEKLINDFPHYGMEKRLWLERLAEMLKTGATEELNDSD... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 70302
Sequence Length: 605
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
|
B0S0K3 | MNNLKYLKLLAKEFPTIEQAANKIISLTSLSVLPKGTEYFLSDLHGQYDSFNRIIKSASGNTRIKIDLEFKDKLSESRKNQLANLIYDPKTIINITKENDEYTETWIRDTIFYLIRIAKRVASKYSRQKVRNQTPFYYRDLIDEMLNIQYESLNKKEYFNQLLDSIIKIEVSENFIITLCELIQDLNIDWLHIVGDIFDRGKRPDIIMDTLIAKKDVDIQYGNHDVTWIGAYLGSYVNACNVVRNAISYNNFQSLEDGYGINLRLLSTLADESYYDDPCERFKVRILDDNKHSETDLLHAARMHKAISIIQFKLENQLFK... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 75232
Sequence Length: 650
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
|
Q036S2 | MDLYSELTAKYQTVPAIATEIINLEAILNLPKPTEAFMSDIHGEYNAFQHVLRNGSGNVKSKIRSCFRDEMTEATLQRFAFLVYYPSERMAAIHREMAGDDLQQWYLTTFRRLIRLLAFTATKYTRSKVRKAMAPEFVYITEELLYNDADTPDKLAYYWQIIRNLIVLEQADQWIAATCQTIQRLTVDHFHVVGDIYDRGPAPDQVVESLIRRDRRHSVDIQWGNHDILWIGGAAGSALCIANLVRISARYNNLSILEDVYGINLRHLARLAEQYYQDNPAFSPKMERSDRPITEAERLQITQIHQAIAMIQFKLEGPVI... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 73866
Sequence Length: 643
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
|
Q8Y8R5 | MKTIDMKYLRLLAKEYPTIAKTATEIINLEAIMNLPKGTEHFLSDVHGEYSAFEQVLRNGSGVVKRKIRDIFGAELDDAEINSLSTLIYYPEEKMDLIASETEDLHAWYRTTLFRLIELCQYVASKYTRSKVRKAMPEDFAYILEELLHENYNEDDKKLYYEEILQHIISLGRAEEFISALSLLIQQLVVDHLHIVGDVYDRGPYPDKIMDTLMNYHSLDFQWGNHDILWMGAASGSRVCAANVIRISARYLNLDILEDSYGISLRPLALFADEVYKDDPCTYFQPKNEENINYSNAEITQIARMHKAISIIQFKLEGEI... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 75645
Sequence Length: 653
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
|
Q5JX71 | MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVQYGEHFRIRQNLPEHTQGWLGSKWLWLLFVVVPFVILQCQRDSEKNKEQSPPGLRGGQLHSPLKKKRNASPNKDCAFNTLMELEVELMKFVSKVRNLKRAMATGSGSNLRLRKSEMPADPYHVTICEIWGEESSS | Function: May play a role in sperm acrosome biogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 19603
Sequence Length: 171
Subcellular Location: Nucleus inner membrane
|
S5DWK8 | MPSSSGVDSTQELLDAQAHIWNHIFNHINSMTLKWAVQLGIPDIIHKHDKPMTLSQLADAIPINRAKSDALHRIMRILVHSKFFDRVRTLPNEEEAYCLTRASRLLLRDEPLSLTPFALAVLDEDLMGTFHCVPEWFGNECPSPLEFKHEKSIREFAENNQRWSLLFNEGMANDARLVGSILAKESRKVFEGLETMVDVGGGTGMVSKAIVDAFPGMKGIVLDLPYVVSGLKGSGNLRYVGGDMFHSVPPADAVFLKWILHNWSDDECIKILEKCKEAITTSKNMKGGKVIIVDMILGYEKQQDEAVETQLFFDMMMMTT... | Function: Cation-independent flavonoid 8-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibact... |
P00740 | MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLE... | Function: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
PTM: Activated by factor XIa, which excises the activation peptide . The propeptide can a... |
P16292 | GVSVSHASKKITRATTIFSNTEYENFTEAETIRGNVTQRSQSSDDFTRIVGGENAKPGQFPWQVLLNGKVEAFCGGSIINEKWVVTAAHCIKPDDNITVVAGEYNIQETENTEQKRNVIRIIPYHKYNATINKYNHDIALLELDKPLTLNSYVTPICIANREYTNIFLNFGSGYVSGWGRVFNRGRQASILQYLRVPFVDRATCLRSTKFTIYNNMFCAGFDVGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAIKGKYGVYTRVSWYVNW | Function: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can al... |
Q7TXK7 | MRNGNLAGLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLP... | Function: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the ... |
Q81JF6 | MNSKSRITAIGTHVPNQILSNNDLEKMIDTNDEWIVQRTGMKERRIASEDEYSSNLAIKAVENLCTTYKKNLEDVDCIIVATTTADYVFPSVACQIQQYFNIPHTMAFDLNATCAGFTYGLHVGNSLITSGSHKKVLVVATETLSKVTDYTDRTTCILFGDGAGAILLERDENKPSFIAYHMGTNGHGGIHLYRTNLSTTMNDTPLQTNEKIVQNGREVYKWATRTVPVGIKELLHTANMKMDDIDWFIPHSANLRMIESICEKSQIPIHKTLTSVEYMGNTSSVSIPLALDLARKKGKLNNGDTLLLYGFGGGLTHLGL... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q81F42 | MHSKSRITAIGTYVPDQILSNNDLEKMVHTNDEWIVQRTGMRERRIASEEEYSSNLAIKAIENLCTTYKKNLEDVDCIIVATTTADYVFPSVACQIQQYFNIPHTLAFDLNATCAGFTYGLHVGNSLITSESHEKVLVVATETLSKVTDYTDRTTCILFGDGAGAILLERDENTPSFIAAHMGTNGDGGIHLYRTNLSTTMNGTPLQTNEKIVQNGREVYKWATRTVPKGIKNLLHTVNMQVDDIDWFIPHSANLRMIESICEKSQIPIQKTLTSVEYMGNTSSVTIPLALNLAIKEGKLNNGDTLLLYGFGGGLTHLGL... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
O07600 | MSKAKITAIGTYAPSRRLTNADLEKIVDTSDEWIVQRTGMRERRIADEHQFTSDLCIEAVKNLKSRYKGTLDDVDMILVATTTSDYAFPSTACRVQEYFGWESTGALDINATCAGLTYGLHLANGLITSGLHQKILVIAGETLSKVTDYTDRTTCVLFGDAAGALLVERDEETPGFLASVQGTSGNGGDILYRAGLRNEINGVQLVGSGKMVQNGREVYKWAARTVPGEFERLLHKAGLSSDDLDWFVPHSANLRMIESICEKTPFPIEKTLTSVEHYGNTSSVSIVLALDLAVKAGKLKKDQIVLLFGFGGGLTYTGLL... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9RT22 | MTASLSAPAIGILAVGAYAPAAVITNAHYATRLDTSDDWITSRTGIRERRHAAPDESSSVLGIRATQDLAGRFPGALDGVNLVICATSSPDAMFPSTAALIAGGTGLRGAAAFDVSVACSGFLYALSVGYGMIRAGLAKKALIVGSEVMSGAVDQNDRNTAILFGDGAGCVVIGEVPQGYGFQSFVLGADSAGGPHLYLRGAALRLPEGTEMGPHLTQNGREVFKFAVRTLGDSAEQAMRQAGKTTADIDWLVPHQANIRIIEAACERFGLPIERAVTNLDRYGNTSAASIPLALAEAQAQGRFKDGDQLLLAGFGGGLS... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q88WG8 | MTTNFSILASAKALPTTKVTNQELTQLMATSDDWIKQRTGIRSRHVATDETTTSLAVSVAQQLLQQSRLAATAIDLIIVATMSPDYLTPATAPQVQAAIGAEKAIAFDINVACAGFVYGMQLVHQYLQPGQTALLIGSETLSRLVDWHDRSTAVLFGDGAGGLLITAKPNTTTGHWLGGHYATFGADGHYLTAGQQPQVNPWSTRTDGADSNRWAFQMNGRRVYDFATKQVPHSIEQALMQARLESSDIKAFVLHQANARIVKSVGQKLNLATEQLPMNIAQYGNTAAASEPILFAEMVAQKQVQRGDKLVFTGFGGGLS... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9Z4Y5 | MSAARGGRAGAVVTGVGTCLPETVVDNDEVSRHLDTDHAWIHSRTGIERRRRVSPGTTTGDLAVTAGAAALKSAGRDDCDLVLLATTTPDRRCPATAPRVASRLGLRAAAAFDLSAVCSGFVYGLSVASAMITAGTCDRALVIGADVYSSIVDPDDRGTAVVFGDGAGAVLLERGDTGDPGAVLHTELGSDGTGDELITIPPDGAYLTMRGSDVYTRAVTTMAESARSTAAHAGWDLADVDAFVGHQANLRILTSVAKRLRLPPERVVSNIADVANTAAASIPLALADAAAQGRIGSGDRLLLTAFGGGLTWGSAAVVWS... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9KLJ3 | MTQCYAEITGWGKCLPPATLSNHDLSTFLDTSDEWIQSRTGIEQRRISHVNTSDLATVAAQHAIACAGVSVEEIDLIIVATCSPDSLIPNIASRVQQNLGIPSAAAFDLNAACTGFLYGLETATRLMQASHYRHALVIGAERLSFYLDWTKRDTAVLFGDGAGAVVLSKTEQKVGLQDAQIGCDAQGRDILAVPKFGTAMDRFDADNGYWAFDFVGKEIFKRAVRGMGAAAQQVLARSGLSTEEIDVVIPHQANIRIIQTLCDLAGIAQDKAFVNIHRYGNTSAATVPIALCEALEQGKIKPHDDLLVAAFGAGLTWGAG... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9ZBV4 | MHQGSRITAVGHYQPARILTNEDLAGMVDTSDEWIRSRVGIRTRRIAGPDEPVDELAGHAAAKALASAGLTPADVDLVVVATSTAIDRSPNTAARVAARLGIPGPAALDLNVVCAGFTHALATADHAVRAGSASRALVVGADKMSEVVDWTDRTTCVLVGDGAGAAVVEACAPGEEPGIGPVLWGSVPEMGNAVRIEGTPPRFAQEGQSVYRWATTRLPAIARQACERSGLEPADLAAVVLHQANLRIVEPLAAKIGAVNAVVARDVVESGNTSAASIPLALSKLAERGEITTGDPALLFGFGGNLSYAGQVVRCP | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9JN82 | MSGAGVLAGLGTALPARLVTNEELSRHLDTDDEWIRSRTGIGQRYWSDGASTGDLAVEAGQRALKAAGTDTVDLVVLATTTPDHPCPATAPDVADRLGLSGVAAYDIAAVCSGFIYGLASAVAHITAGLVGSALVIGAETYSTILDPLDRTTSVIFGDGAGAVVLRSGSVDERGAFLGFDLGSDGALKDLIVIPGGGSRERAAAERPQPAGAYFTMQGKPVFRHAVTRMTSSAGALLDRTGWSPASVDRFVGHQANARILHAVADQLRIDGARTVIDLDRVGNTSAASIPLALSRACGEGLLSPGDRVLLSAFGGGLTWG... | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both ace... |
Q9PMZ6 | MKTRFDKAKISGICVSVPEHKICIDDELESVFSNDIKTLKRMKKVIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVTQSPDFFMPSTACYLHQLLNLSSKTVAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICGDTLSKFIHPKNMNLAPIFGDGVSATLIEKTDFNEAFFELGSDGKYFDKLIIPKGAMRIPKADIFNDDSLMQTEEFRQLENLYMDGANIFNMALECEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPNFIMEKYANLSACSLPTLLCELDTPKEFKA... | Function: May catalyze the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 39480
Sequence Length: 353
Pathway: Lipid metabolism; fatty acid biosy... |
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