ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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|---|---|---|
Q8N5G2 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHYSSKFVETSPSGLDPNASVYQPLKK | Function: Plays a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76178
Sequence Length: 664
Subcellular Location: Nucleus membrane
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Q7TQE6 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKGPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHYSSKFVETSPSGLDPNASVYQPLKK | Function: Plays a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76089
Sequence Length: 664
Subcellular Location: Rough endoplasmic reticulum membrane
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O57342 | MASELAMTAELPTSPLAIEYVNDFDLMKFEVKKEPAEAERLCHRLPAGSLSSTPLSTPCSSVPSSPSFCAPSPGGQPSAGPTAAPLGSKPQLEELYWMSGYQHHLNPEALNLTPEDAVEALIGAPHHHHHHHQSYESFRPQPFGGEELPPAAHHHNAHHHHHHHHLRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRYKRVQQRHILENEKCQLQSQVEQLKQEVSRLAKERDLYKEKYEKLAARGFPRETSPPAAPKTTAADFFM | Function: Transcription factor involved in transcription regulation during lens development, including that of crystallin genes . Binds to CRE-type MARE 5'-TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequences .
PTM: Phosphorylation at Ser-14 and Ser-65 is required for transcription regulation activity and lens differentiation in neuroretina cells . Phosphorylation at Ser-65 may be required for efficient phosphorylation at Thr-53, Thr57 and Ser-61 by GSK3 .
Sequence Mass (Da): 32464
Sequence Length: 286
Subcellular Location: Nucleus
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Q8NHW3 | MAAELAMGAELPSSPLAIEYVNDFDLMKFEVKKEPPEAERFCHRLPPGSLSSTPLSTPCSSVPSSPSFCAPSPGTGGGGGAGGGGGSSQAGGAPGPPSGGPGAVGGTSGKPALEDLYWMSGYQHHLNPEALNLTPEDAVEALIGSGHHGAHHGAHHPAAAAAYEAFRGPGFAGGGGADDMGAGHHHGAHHAAHHHHAAHHHHHHHHHHGGAGHGGGAGHHVRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHILESEKCQLQSQVEQLKLEVGRLAKERDLYKEKYEKLAGRGGPGSAGGAGFPREPSPPQAGPGGAKGTADFFL | Function: Transcription factor that activates insulin gene expression . Acts synergistically with NEUROD1/BETA2 and PDX1 . Binds the insulin enhancer C1/RIPE3b element . Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence .
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 36982
Sequence Length: 353
Subcellular Location: Nucleus
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D3ZNT6 | MAAELAMGAELPSSPLAIEYVNDFDLMKFEVKKEPPEAERFCHRLPPGSLSSTPLSTPCSSVPSSPSFCAPSPGTGSSAGGGGSAAQAGGAPGPPSGGPGTVGGASGKAVLEDLYWMSGYQHHLNPEALNLTPEDAVEALIGSGHHSAHHGAHHPAAAAAYEAFRGQSFAGGGGGGADDMGAGHHHGAHHTAHHHHSAHHHHHHHHHHGGSGHHGGGAGHGGGGAGHHVRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHILESEKCQLQSQVEQLKLEVGRLAKERDLYKEKYEKLAGRGGPGGAGGAGFPREPSPAQAGPGAAKGAPDFFL | Function: Transcription factor that activates insulin gene expression . Acts synergistically with NEUROD1/BETA2 and PDX1 (By similarity). Binds the insulin enhancer C1/RIPE3b element . Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence (By similarity).
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 37780
Sequence Length: 361
Subcellular Location: Nucleus
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Q7ZV50 | MLHKLLIVVFLVVCLHDMRLNGQKKKETLLSEKVSQMMEWVSKRAVVRLNGEKFKRLVRAHPRNYSVIVMFTALQPQRQCGVCRQADEEYQILANSWRYSSAFTNRIFFAMVDFDEGSDVFQMLNMNSAPTFINFPAKGKPKRADTYELQVRGFAAEQLARWVADRTDVHIRVIRPPNYAGPLMLGLLLAFIGSLAYLRRNNLEFLFNKNVWAFSALCFVLIMTSGQMWNHIRGPPYAHKNPNTGQVSYIHGSSQAQFVAETHIVLLFNAAVTIGMVLLHEAATSGLDIVKRKIMCVAGIGLVVLFFSWLLSVFRAKYHGYPYSFLFG | Function: Cell surface magnesium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37422
Sequence Length: 328
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell membrane
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Q9H0U3 | MAARWRFWCVSVTMVVALLIVCDVPSASAQRKKEMVLSEKVSQLMEWTNKRPVIRMNGDKFRRLVKAPPRNYSVIVMFTALQLHRQCVVCKQADEEFQILANSWRYSSAFTNRIFFAMVDFDEGSDVFQMLNMNSAPTFINFPAKGKPKRGDTYELQVRGFSAEQIARWIADRTDVNIRVIRPPNYAGPLMLGLLLAVIGGLVYLRRSNMEFLFNKTGWAFAALCFVLAMTSGQMWNHIRGPPYAHKNPHTGHVNYIHGSSQAQFVAETHIVLLFNGGVTLGMVLLCEAATSDMDIGKRKIMCVAGIGLVVLFFSWMLSIFRSKYHGYPYSFLMS | Function: Accessory component of the STT3B-containing form of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains . Involved in N-glycosylation of STT3B-dependent substrates . Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with TUSC3. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38037
Sequence Length: 335
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell membrane
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P02916 | MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPAWFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLPLLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGGGQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57013
Sequence Length: 514
Subcellular Location: Cell inner membrane
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O51924 | MDNNLTSKLKYREAKLGYLMILPLLTVVLVFIILPVMGTFWISLHRDVTFIPEKPFVGLRNYLRVLSAREFWYSTFVTVSFSFVSVSLETILGLSFALILNERLKGRGVLRAIVLIPWAVPTIISARTWELMYNYSYGLFNWILSILGVSPVNWLGTPISAFFAIVIADVWKTTPFMTLLLLAGLQAIPQDLYEAALIDGASMFERFKSITLPLLKPVLIVALILRTIDALRVFDIIYVLTGGGPGGATTSISLLAFNYYNLGDYGIGSAISILTFVLVLSFTIVYLKVGRFRRD | Function: Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33054
Sequence Length: 295
Subcellular Location: Cell membrane
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Q0DM48 | MTVRPRPAAAAIIIAAVFGAAAAAAGGGMVGVDGTQFVVEGGRTIYFSGFNAYWLMMMASDPARRAAVVAAFAQASSRGLNLARTWAFSDGGDQPLQSSPGVYDEAMFQGLDFVIAEARRHGIYLLLCLTNNFDDFGGKRQYVRWAADAGHNLTAGDDFFTSSVVKSYYKNHVKAVLTRVNTVTGVAYKDDPTIFAWELMNEPRCDADPTGGMVQAWVEEMAPYVKRVDGGRHLVTAGLEGFYGDGEHESKELNPWGIYYGTNYVATHRAAGVDFATIHLYPDVWLWGSTADEQAAFFRNWTRSHVHDTAAFLGKPLLVTEYGKFLWKGGGANKTQRNYFLDVVLDAIYASASRGGPLVGGAFWQLLLDDDVVAGMDDLRDGYEIILAEDSRAASIIGEHSEQLASLNGQDAEALRRRRRRPASSHRKTRLGSGGDSDALRLPRTLLIRFISLSRSISSFIQDNFVLF | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 51217
Sequence Length: 468
Subcellular Location: Secreted
EC: 3.2.1.78
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Q8L5J1 | MNNSIILIFVAILIIFPNEFSKPTRAFSNNNFVYTDGTHFALNGKSLYINGFNAYWLMYIAYDPSTRIKVTNTFQQASKYKMNVARTWAFSHGGSRPLQSAPGVYNEQMFQGLDFVISEAKKYGIHLIMSLVNNWDAFGGKKQYVEWAVQRGQKLTSDDDFFTNPMVKGFYKNNVKVVLTRVNTITKVAYKDDPTILSWELINEPRCPSDLSGKTFQNWVLEMAGYLKSIDSNHLLEIGLEGFYGNDMRQYNPNSYIFGTNFISNNQVQGIDFTTIHMYPNQWLPGLTQEAQDKWASQWIQVHIDDSKMLKKPLLIAEFGKSTKTPGYTVAKRDNYFEKIYGTIFNCAKSGGPCGGGLFWQVLGQGMSSFDDGYQVVLQESPSTSRVILLQSLRLSKLS | Function: Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 45339
Sequence Length: 399
Subcellular Location: Secreted
EC: 3.2.1.78
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B3PF24 | MSLFTPLSETNVRSHTNTSSVFCRRIKTLVAGLTALGLMLAAVSASAGFYVSGKQLREGNGNNFIMRGVNLPHAWFPDRTNQALADISATGANSVRVVLSNGRLWSRTPESQVASIISQAKARQLITVLEVHDTTGYGEQTAATLSEAVDYWIAIRNALIGQEDYVIINIGNEPFGNGQSASTWLNLHRDAINRLRNAGFTHTLMVDAANWGQDWENIMRNNASSLFNSDPRRNVIFSVHMYEVYPNDTAVNNYMSAFNSMNLPLVVGEFAANHFGSYVDAGSIMARAQQYGFGYLGWSWSGNSSNLSALDVVTNFNAGSLTTWGNLLINNTNGIRNTSRKATIFGGSGSSSSSAGSCGTAPNGYPYCCNASSATGNGWGWENNRSCVVATTSTSCNWYGTSYPICVNTSSGWGWENNRSCIAASTCAAQ | Function: Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. It is able to hydrolyze mannosidic linkages that are flanked by mannose or glucose.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 46325
Sequence Length: 430
EC: 3.2.1.78
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G1K3N4 | AGFYVDGNTLYDANGQPFVMRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQNKMVAVVEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMFSIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDDNGGHPEPPT | Function: Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. It is able to hydrolyze mannosidic linkages that are flanked by mannose or glucose.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 34211
Sequence Length: 308
EC: 3.2.1.78
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Q9LZV3 | MKDQLGFRIVLCSAVFIILTQNRALADLDSESHEVNSESVGEEQWEMVQRKGMQFTLNGQPFYVNGFNTYWMMTLAADNSTRGKVTEVFQQASAVGMTVGRTWAFNDGQWRALQKSPSVYDEEVFKALDFVLSEARKYKIRLILSLVNNWDAYGGKAQYVKWGNASGLNLTSDDDFFTNPTLRNFYQSHVRTVLNRVNTFTNITYKNDPTIFAWELMNEPRCPSDPSGDKLQSWIQEMAVFVKSLDAKHLVEIGLEGFYGPSAPARTRFNPNPYAAQVGTDFIRNNQVLGIDFASVHVYPDSWISPAVSNSFLEFTSSWMQAHVEDAEMYLGMPVLFTEFGVSAHDPGFNTSFRDMMLNTVYKMTLNSTRKGGAGAGSLVWQVFPQGAEFMDDGYAVYLTRAHTASKIISLQSKRLAIFNSLCSWRCRWGCKKKNQTALDALLSHDEL | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 50622
Sequence Length: 448
Subcellular Location: Secreted
EC: 3.2.1.78
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Q0DCM5 | MRQERRLYSLLGLLLLLAVVYLTWFPTTHDGGGGGGGGWVKLPVPWLQPRMPFAARRGTHFVDADTGSPLYVNGWNSYWLLPARSPALAAEMLRRGRRMGLSVCRTWAFSDGGPGALQISPGRFSEAVFQVLDYVIYEARRNHIRLILCLVNNLDNLGGKAQYVQWAQAAGANMTNSTDSFYSHPTIKRYYKDYVKAILTRRNSYSRIRYSDEPAIFAWELMNEPRCVSNSSGPYLQAWIAEMAAYVKSLDTNHLVTVGTEGFYGPGIAERLGVNPGEWAASLCSDFIQNSAVEHIDFASVHAYPDSWLPRASLEEKVRYLSNWVDSHLNDSEQILKKPVLFTEVGYLQHSDANSNSTVDRDIILRIVYDKIYDSARKLQAGSGALIWQLMVEGTHMYGDNFSVVARDRPSTYSLITNQSCRLQRLYGEGDPGWQCSIPP | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 49455
Sequence Length: 440
Subcellular Location: Secreted
EC: 3.2.1.78
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Q9FJZ3 | MKLLALFPFLAIVIQLSCWELGTDALPSGGFVRTKGVQFSLNGYPYYANGFNAYWLMYVASDPSQRSKISTAFQDASRHGLTVARTWAFSDGGYRALQYSPGSYNEDMFQGLDFALAEARRHGIKIILSFANNYESFGGRKQYVDWARSRGRPVSSEDDFFTDSLVKDFYKNHIKAVLNRFNTFTKVHYKDDPTIMAWELMNEPRCPSDPSGRAIQAWITEMAAHVKSLDRNHLLEAGLEGFYGQSSPQSKTLNPPGQFGTDFIANNRIPGIDFVTVHSYPDEWFPDSSEQSQMDFLNKWLDAHIQDAQNVLHKPIILAEFGKSMKKPGYTPAQRDIVFNTVYSKIYGSAKRGGAAAGGLFWQLLVNGIDNFQDGYGIILSQSSSTVNVISQQSRKLTLIRKIFARMINVEKWKRARGQGQVGKRGHKINN | Function: Required for both, loosening of the micropylar endosperm, and rupture of the seed coat in germinating seeds. May participate in the hydrolysis of the mannans in the cell wall of germinating seeds.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 48573
Sequence Length: 431
Subcellular Location: Secreted
EC: 3.2.1.78
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P94078 | MAVKCFSLYLILAAIVIGGVTSEYIEYNTKPRIVPEKINVHLVPHSHDDVGWLKTVDQYYVGSNNSIRGACVQNVLDSVIASLLDDENRKFIYVEMAFFQRWWRQQSNAKKVKVKKLVDSGQLEFINGGMCMHDEATPHYIDMIDQTTLGHQFIKTEFGQVPRVGWQIDPFGHSAVQAYLLGAEFGFDSLFFARIDYQDRAKRLREKTLEVIWQGSKSLGSSSQIFTGVFPRHYDPPEGFTFEINDVSAPIQDDPLLFDYNVQERVNDFVAAALAQVNVTRTNHIMWLMGTDFRYQYAYSWFRQIDKFIHYVNKDGRLNVLYSTPSIYTDAKYAANESWPLKTDDFFPYADKPNAYWTGYFTSRPAFKKYVRDLSGYYLAARQLEFLRGRDSSGPTTDMLADALAIAQHHDAVSGTQRQHVAADYALRLSMGYLQAEKLVASSLSFLSAAKSSTEKKNPGTKFQQCPLLNISYCPASEARLLSGKSLVVVVYNSLGWKREEVVRVPVSSENVIVKDASGKEVVFQLLPLSEIALRIRNEYVKAYLGRSPRDTAKHVLAFTASVPPLGFSSYVISDTGRTARGLSASYVTSGSMNQNVEVGQGNLKLRYSEEGVKITRHLSTKNQVTAEQSYAYYIGSNGTDKDPQASGAYVFRPDGVLPIKSKEEAQLTIVQGPLFDEVHQELNSWISQITRVYKGKNHAEIEFTIGPIPADDGISKEIITKLTTTMKTNGTFYTDSNGRDFIKRIRDFRTDWDLQVYQPVAGNYYPLNLGIYMQDKTSELSVLVDRAVGGSSLENGQIELMLHRRMQHDDIRGVGEILNETVCLPEGCKGLTIQGKFYVQIDKPGDGAKWRRTFGQEIYSPLLIAFTEQEGDSWINSHKTTFSAFEPSYSLPKNVALLTLQELENGEVLLRLAHLFEVGEDSEYSVMAKVELKKLFHNKKIREVKETSLSGNQEKAEMEKRRLIWKVEGSAGEEVKRGEAVDAEKLVVELVPMEIRTLLIKFDDQIEMVGDKEQQHRL | Cofactor: Binds 1 zinc ion per subunit.
Function: Liberates mannose from p-nitrophenyl-alpha-D-mannoside in vitro.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 115220
Sequence Length: 1019
EC: 3.2.1.24
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O31646 | MTTEPLFFKPVFKERIWGGTALADFGYTIPSQRTGECWAFAAHQNGQSVVQNGMYKGFTLSELWEHHRHLFGQLEGDRFPLLTKILDADQDLSVQVHPNDEYANIHENGELGKTECWYIIDCQKDAEIIYGHNATTKEELTTMIERGEWDELLRRVKVKPGDFFYVPSGTVHAIGKGILALETQQNSDTTYRLYDYDRKDAEGKLRELHLKKSIEVIEVPSIPERHTVHHEQIEDLLTTTLIECAYFSVGKWNLSGSASLKQQKPFLLISVIEGEGRMISGEYVYPFKKGDHMLLPYGLGEFKLEGYAECIVSHL | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 36003
Sequence Length: 315
EC: 5.3.1.8
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P24174 | MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDMVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLNFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV | Function: Involved in the biosynthesis of the capsular polysaccharide colanic acid.
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 53016
Sequence Length: 478
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
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Q5AZ53 | MIFSTLLSLALLATTATARKGFVTTKGDKFQLDGKDFYFAGSNAYYFPFNNNQTDVELGLSAAKKAGLLVFRTWGFNDKNVTYIEDGLPQYGGEGAGTTEVVFQWWQNGTSTIDLEPFDKVVNAAAKTGIKLIVTLVNNWADYGGMDVYTVNLGGQYHDDFYRLPQIKKAYKRYVKEMVTRYRNSPAIMAWELANEPRCGADGVRNLPASDECTPELLTSWIDEMSTYVKRLDPHHLVTWGGEGGFNYDSDDWAYNGSDGGDFEAELKLKNIDFGVFHSYPDWWSKTVEWTNKWIVDHARAARRVGKPVVHEEYGWLTPQGRLDNLGTVSNITRLEAVGGWQSISLREKMSDMFWQFGYSGYSYGRNHDDGFTIYLDDAEAQELVYKHAKEVNKLNRRR | Function: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar . Also has transglycosylation activity. Produces mainly mannopentaose and mannohexaose out of mannotetraose .
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 45338
Sequence Length: 399
Subcellular Location: Secreted
EC: 3.2.1.78
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Q8FHC7 | MHHDKRCKESNMKIVKAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELSVASYLQDHLCPQLIGRDAHRIEDIWQFFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHSIDEALDDYARHQELGFKAIRVQCGIPGMKTTYGMSKGKGLAYEPATKGQWPEEQLWSTEKYLDFMPKLFDAVRNKFGFDEHLLHDMHHRLTPIEAARFGKSIEDYRMFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSPVCMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHNWTFDNGYMHPGEKPGLGIEFDEKLAAKYPYEPAYLPVARLEDGTLWNW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 47350
Sequence Length: 415
EC: 4.2.1.-
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A4XF23 | MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRGKLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLSPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 45244
Sequence Length: 402
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 4.2.1.8
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P19994 | MIICKTPRELGIMREAGRIVALTHEELKKHIKPGISTKELDQIAERFIKKQGAIPSFKGYNGFRGSICVSVNEELVHGIPGSRVLKDGDIISIDIGAKLNGYHGDSAWTYPVGNISDDDKKLLEVTEESLYKGLQEAKPGERLSNISHAIQTYVENEQFSVVREYVGHGVGQDLHEDPQIPHYGPPNKGPRLKPGMVLAIEPMVNAGSRYVKTLADNWTVVTVDGKKCAHFEHTIAITETGFDILTRV | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 27409
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q4QRK0 | MAAVETRECETEGCHSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKEDKTNDEEKNCVEKEVNTDPWPGYRYTGKLRPYYPLTPMRLVPSNIQRPDYADHPLGMSESEQTMKGTSQIKILNAEEIEGMRVVCKLAREVLDIAAMMVKPGVTTEEIDHAVHLACTARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRHLQEGDILNIDITVYHNGYHGDLNETFFVGEVDEGAKRLVQTTYECLMQAIDSVKPGIRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKPGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTETGCEILTRRLEDNGRAHFLSQM | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 43567
Sequence Length: 386
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q54WU3 | MEGILCASPGCGKPAKLQCPTCVNLKLETPSHFCSQECFKTFWPLHKMYHQKGQPENLPSQFRNYKFTGPLRPTNITPMRKAPEGIELPDYAIGSIPISERVADRKNMANIIHTPEEIEIMRQLGKMSREVLDIAGNAAKVGMTTEELDIIVHNAVIERGAYPSPLNYYKFPKSCCTSLNEVICHGIPDERPLRDGDILNVDVTLYWKGFHSDLNETYLIGNVDERGKNLVKCAYDCLELAVAMCKPGTLYRELGDAIQKHANKQGFSVVKNFCGHGIGRLFHCNPTVPHYSKNKAVGAMKVGHVFTIEPMINEGTWQDEIWPDSWTAVTADGKRSAQFEHTLVITETGCEVLTKRTNGSYIDRHFK | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 41185
Sequence Length: 367
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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P53582 | MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 43215
Sequence Length: 386
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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P9WK20 | MRPLARLRGRRVVPQRSAGELDAMAAAGAVVAAALRAIRAAAAPGTSSLSLDEIAESVIRESGATPSFLGYHGYPASICASINDRVVHGIPSTAEVLAPGDLVSIDCGAVLDGWHGDAAITFGVGALSDADEALSEATRESLQAGIAAMVVGNRLTDVAHAIETGTRAAELRYGRSFGIVAGYGGHGIGRQMHMDPFLPNEGAPGRGPLLAAGSVLAIEPMLTLGTTKTVVLDDKWTVTTADGSRAAHWEHTVAVTDDGPRILTLG | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 27277
Sequence Length: 266
EC: 3.4.11.18
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P53579 | MGDTITLLSRREIEKMRQAGQLAAALLDHLAPMVQPGITTLELNDEAEKWTKAHGAISAPLGYNGFPKSICTSINEVICHGIPHRKRVLQAGDIINVDVTPIVDGYHGDCSRTFFVGTPSPVAEKLVKVTEECLRLGIEAVKPGGKIGDIGAAIQSHAEAQGFSVVRDFVGHGISKIFHTAPQIPHYGKAGKGKRLRPGMVFTIEPMINEGTWEAVLLDDGWTAITKDGKLSAQFEHTIAVTEDGVEILTLGE | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 27235
Sequence Length: 253
EC: 3.4.11.18
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O34484 | MIVTNDQELEGLKKIGRIVALAREEMKRKAEPGMSTKDLDLIGKAVLDEHGAVSAPEKEYDFPGVTCISVNDEVAHGIPSTSKILKAGDLVNIDISAEFGGFYSDTGISFVLGEGEERLHKLCQCAENAFQKGLQQAKAGKRQNQIGRAVYHEARSQGFTVIKTLTGHGIGRSLHEAPNHIMNYYDPFDNALFKNGTVIALEPFISTKAETIVEAGDGWTFKTPDKSMVAQVEHTIVITKDEPIILTKL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 27211
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q4VBS4 | MAAPCAAQCLYRTGGLRLLQRISRLPHCHKDASLAHQCQFHRSFFWRKPKTSHSVVRPAIVRPAYPVPKHIQRPDYVSSSKVPEWPDYIEIKDEEQIQGLRRACQLARHILLLTGNSLKVGMTTDEIDFIVHQEAIRHNGYPSPLHYGGFPKSVCTSVNNVVCHGIPDSRPLQDGDIINIDVTVYLEGYHGDTSETFLIGSVNDQGRKLVDVARQCRDQAIAACGPGQPLCVIGNIISNIANSNGFRVCPYFIGHGIGEYFHGHPEIWHHANDNDLKMEEGMSFTIEPILMEGTSGFRILSDKWTAVSVDDKRSAQFEHTVVITSDGVEILTKLPEED | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 37785
Sequence Length: 338
Subcellular Location: Mitochondrion
EC: 3.4.11.18
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Q54VU7 | MNKILKNIINKSSINNVFKTSFNGGISSSSSSSSSYLNNNNNIIKSYNVQQKQQQRYYSSFEDDLSPKKLKEKILENETEEIRDFVRSQRLTKKTASPLEGMNRKERRKMTTKLYRNPDNLIRGGIVSPQPLIPAHIKKPKYVLGEPVIDFEIDDPIEIHTAESIEHMRVVGKMAKEVLEYAGTLVRPGITTDEIDKLVHQNIIDRGAYPSPLGYKGFPKSICTSINEVLCHGIPDDRPLEFGDIVKIDVTLYYNGYHGDTCATFPVGEIDSSSKRLIEATEKALYAAIGEVKDGALFNKIGKKIQLVANKYSLSVTPEFTGHGIGQLFHTAPFVFQCANEFDSVMKEGMIFTIEPVLVESTSPYAEWKMWDDKWTVSSREGGWSAQFEHTILVTKDGYEILTK | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 45549
Sequence Length: 404
Subcellular Location: Mitochondrion
EC: 3.4.11.18
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Q6UB28 | MAAPSGVHLLVRRGSHRIFSSPLNHIYLHKQSSSQQRRNFFFRRQRDISHSIVLPAAVSSAHPVPKHIKKPDYVTTGIVPDWGDSIEVKNEDQIQGLHQACQLARHVLLLAGKSLKVDMTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLPMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHEA | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 37088
Sequence Length: 335
Subcellular Location: Mitochondrion
EC: 3.4.11.18
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P9WK18 | MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 30891
Sequence Length: 285
EC: 3.4.11.18
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Q96JE9 | MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPPPQQQAQPALAPPSARAVAIETQPAQGELDAVARATGPAPGPTGEREPAAGPGRSGPGPGLGSGSTSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQISAASQASAPILGAPKRRPQSQERWPVQAAAEAREQEAAPGGAGGLAAGKASGADERDTRRKAGPAWIVRRAEGLGHEQTPLPAAQAQVQATGPEAGRGRAAADALNRQIREEVASAVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEASKPTTADNKVIDRRRIRSLYSEPFKEPPKVEKPSVQSSKPKKTSASHKPTRKAKDKQAVSGQAAKKKSAEGPSTTKPDDKEQSKEMNNKLAEAKESLAQPVSDSSKTQGPVATEPDKDQGSVVPGLLKGQGPMVQEPLKKQGSVVPGPPKDLGPMIPLPVKDQDHTVPEPLKNESPVISAPVKDQGPSVPVPPKNQSPMVPAKVKDQGSVVPESLKDQGPRIPEPVKNQAPMVPAPVKDEGPMVSASVKDQGPMVSAPVKDQGPIVPAPVKGEGPIVPAPVKDEGPMVSAPIKDQDPMVPEHPKDESAMATAPIKNQGSMVSEPVKNQGLVVSGPVKDQDVVVPEHAKVHDSAVVAPVKNQGPVVPESVKNQDPILPVLVKDQGPTVLQPPKNQGRIVPEPLKNQVPIVPVPLKDQDPLVPVPAKDQGPAVPEPLKTQGPRDPQLPTVSPLPRVMIPTAPHTEYIESSP | Function: Involved in microtubule stabilization in many cell types, including neuronal cells (By similarity). Specifically has microtubule cold stabilizing activity (By similarity). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B . Regulates KIF5A-mediated axonal cargo transport (By similarity). Regulates axonal growth during neuron polarization (By similarity).
PTM: Palmitoylated. Probably depalmitoylated by ABHD17A, ABHD17B and ABHD17C. During neuronal polarization, palmitoylation and depalmitoylation cycles regulate MAP6 shuttling between secretory vesicles and microtubules, and its polarized distribution in the axon.
Location Topology: Lipid-anchor
Sequence Mass (Da): 86505
Sequence Length: 813
Subcellular Location: Cytoplasm
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Q63560 | MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPAPPQPGLAPPSRAVAIETQPAQGESDAVARATGPAPGPSGDRETAAAPGRSGLGLGAASGSTSGSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQIPATSQPSPPVLGMPKRRPQSQERGPIQLSADARDPEGAGGAGVPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEETPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEETPLPPAQSQTQEGGPAAGKASGADERDTRRKAGPAWMVRRSEGHEQTTAAHAQGTGPEGGKGRAVADALNRQIREEVTSTVSSSYRNEFRAWTDIKPVKPIKAKPQYKPPDDKMVHETSYSAQFKGEASKPTTADNKVVDRRRIRSLYSEPFKESPKVEKPSVQSSKPKKTSTSQKPLRKAKDKQVASGQAAKKKTTESPSATKPDDKEQSKEMNNKLAEAKESRVKPTSDKNQGPVAKEPHKDQGPVAPGLPKGQGPAVQEPLKDQGPMVPGLPKDQAPVVPGSLKGQSPTAPGPPKDQGAVLLGPMKDLGPVAPASVKDQDHMASELLKNKDSVPLAPAKAQSPLLPEPLKNQSPVVPARAKDQSFPAPAPTPLKDPGPVIPEPEKDGAPMVPERRKDQNASIMASLKNEAPVASESVKNQGLGGPEPAKDTGTDLKGHGSVFVAPVKSQGPVVPEPTKGQDPIIPALAKDQGPILPEPPKNQGPPVVLGPIKNQDPVIPVPLKGQDPVVPAPTKDPGPTAPDPLKSQGPRGPQLPTVSPSPPVMIPTVPHAEYIEGSP | Function: Involved in microtubule stabilization in many cell types, including neuronal cells . Specifically has microtubule cold stabilizing activity . Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated axonal cargo transport . Regulates axonal growth during neuron polarization .
PTM: Palmitoylated. Probably depalmitoylated by ABHD17A, ABHD17B and ABHD17C. During neuronal polarization, palmitoylation and depalmitoylation cycles regulate MAP6 shuttling between secretory vesicles and microtubules, and its polarized distribution in the axon.
Location Topology: Lipid-anchor
Sequence Mass (Da): 100485
Sequence Length: 952
Subcellular Location: Cytoplasm
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Q14244 | MAELGAGGDGHRGGDGAVRSETAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPKARQPARSRLWLPSKSLPHLPGTPRPTSSLPPGSVKAAPAQVRPPSPGNIRPVKREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPEVGPAAPAMAPAPASAPAPASAPAPAPVPTPAMVSAPSSTVNASASVKTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQRQAEERALREREEAERAQRQKEEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATDKKTSDQRNGDIAKGALTGGTEVSALPCTTNAPGNGKPVGSPHVVTSHQSKVTVESTPDLEKQPNENGVSVQNENFEEIINLPIGSKPSRLDVTNSESPEIPLNPILAFDDEGTLGPLPQVDGVQTQQTAEVI | Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments.
PTM: The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis.
Sequence Mass (Da): 84052
Sequence Length: 749
Subcellular Location: Cytoplasm
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O88735 | MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNLKARSPAPARLWLPSKSMPHLPGTPRPASSLPPGSVRAASAQAPSSSPGNIRPFKREVKVEPEKKDPLPAVKSRVPLVKVEEVTVEEGTPVKPPEPAAPASAPIATPAPAPATDPAPVPAPSSTVTVGVVPKTSAGTTDPEEATRLLAEKRRLAREQREKEERERKEKEELERQKIEELARRVAEERSRREEEARRLEEEQAREKEELALRLAEEERERWEREEVERVQKQKEEEARAREEAERARQEREKHFQKEEQERLERKKRLEEIMRRTRRTETADKKTTEQRNGDIAKGVLTGEPEVPALPCMASSGNGESAESPHGVALQQSEVTTESSPDLEKQPNENGMSIQNENFEEVINLPVGSKASRLDVTNENPEIPLKPILAFNDEGTLGPLPQVDGVQTQQTAEVI | Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments.
PTM: The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis (By similarity).
Sequence Mass (Da): 82022
Sequence Length: 730
Subcellular Location: Cytoplasm
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Q9FLS8 | MEAEKSKQNPGKKPVEATMEHVLVALRETKEKREIRIQKLFEFFDNSKLGFLDDTQIEKGLSSLSIPPKYRYASDFLKVCDSNRDGRVDYQEFRRYMDAKELELYKIFQAIDIEHNGDICPAELWEALDKAGIKIKDEELASFMEHVDKDNNGIITFEEWRDFLLLNPHEATIENIYHHWERVCLIDIGEQAVIPDGISAHAQRSKLLLAGGIAGAVSRTATAPLDRLKVALQVQRTNLGVVPTIKKIWREDKLLGFFRGNGLNVAKVAPESAIKFAAYEMLKPIIGGADGDIGTSGRLLAGGLAGAVAQTAIYPMDLVKTRLQTFVSEVGTPKLWKLTKDIWIQEGPRAFYRGLCPSLIGIIPYAGIDLAAYETLKDLSRAHFLHDTAEPGPLIQLGCGMTSGALGASCVYPLQVIRTRMQADSSKTSMGQEFLKTLRGEGLKGFYRGIFPNFFKVIPSASISYLVYEAMKKNLALD | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate and, to a lesser extent, other nucleotides . Binds calcium ions Ca(2+) . Mediates also calcium uptake (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53275
Sequence Length: 478
Domain: The N-terminal domain can bind calcium.
Subcellular Location: Mitochondrion inner membrane
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Q9FI43 | MEATKSSKQNCCNPVKKPGPVSIDHVLLALRETREERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMDDKELELYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFLLLYPHEATIENIYHHWERVCLVDIGEQAVIPEGISKHIKRSNYFIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIREAIKLIWKQGGVRGFFRGNGLNIVKVAPESAIKFYAYELFKNAIGENMGEDKADIGTTVRLFAGGMAGAVAQASIYPLDLVKTRLQTYTSQAGVAVPRLGTLTKDILVHEGPRAFYKGLFPSLLGIIPYAGIDLAAYETLKDLSRTYILQDAEPGPLVQLGCGTISGALGATCVYPLQVVRTRMQAERARTSMSGVFRRTISEEGYRALYKGLLPNLLKVVPAASITYMVYEAMKKSLELD | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate, sulfate and thiosulfate, and, to a lesser extent, other nucleotides . Binds calcium ions Ca(2+) . Mediates also calcium uptake .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54506
Sequence Length: 487
Domain: The N-terminal domain can bind calcium.
Subcellular Location: Mitochondrion inner membrane
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Q9LY28 | MESSKPKNRNPMKKPVSITMEHVLLALRETMDEREIRIRSLFDFFDNSNLGFLDYAQIEKGLASLQIPPEYKYARDLFRVCDANRDGRVDYQEFRRYIDAKELELYRIFQAIDVEHNGCILPEELWEALVKAGIEIDDEELARFVEHVDKDNNGTITFEEWRDFLLLYPHEATLENIYHHWERVCLIDIGEQAVIPDGISKHVKRSRLLLAGGLAGAVSRTATAPLDRLKVVLQVQRAHAGVLPTIKKIWREDKLMGFFRGNGLNVMKVAPESAIKFCAYEMLKPMIGGEDGDIGTSGRLMAGGMAGALAQTAIYPMDLVKTRLQTCVSEGGKAPKLWKLTKDIWVREGPRAFYKGLFPSLLGIVPYAGIDLAAYETLKDLSRTYILQDTEPGPLIQLSCGMTSGALGASCVYPLQVVRTRMQADSSKTTMKQEFMNTMKGEGLRGFYRGLLPNLLKVVPAASITYIVYEAMKKNMALD | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate, sulfate and thiosulfate, and, to a lesser extent, other nucleotides . Binds calcium ions Ca(2+) . Mediates also calcium uptake (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53970
Sequence Length: 479
Domain: The N-terminal domain can bind calcium.
Subcellular Location: Mitochondrion inner membrane
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O94737 | MDSKHSVFNVMGQEFVLQKGYEVIKGLGKGSYGVVCSAKNIEVEDNNKVAIKKITNIFSKKMLAKRALREIMLLQHFRNHKNITTLYDMDIVDPSKFNELYLYEELMQANLNSIIRSDQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPSNLLINADCKLKICDFGLSRGISVNQGQGTEYMTEYVTTRWYRAPEVMLSFQSYSKAIDLWSVGCILAELLGRKPFFKGSNYVDQLNQIFCILGTPNENIISKIKSASAQSYIRSLPTLPKMPYSKIFPYANPDALDLLNCLLTFDPYDRISCEEALEHPYLIIWHDPNKEPVCSEQFDFGFEAIDSIEEIRQMIINEVSRFKGLTGNQKLYHSISNT | Function: Serine-threonine protein kinase which may be involved in maintenance of cell integrity. Functionally complements SLT2 null mutant in S.cerevisiae.
PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42396
Sequence Length: 370
Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
EC: 2.7.11.24
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P49071 | MLSLQNQRQPKTTPLTDDYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMECMEGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDLIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPLCTGRMLKEAEETWPEVQEEMTRSLATMRVDYDQMQIKALDKSNNPLLTKRRKKIEEMELYMANATRN | Function: Its physiological substrate seems to be the small heat shock protein (HSP27/HSP25).
PTM: Phosphorylated and activated by MAP kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41401
Sequence Length: 359
EC: 2.7.11.1
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P0C1Q5 | INWKALLDAAKKVL | Function: Potent antimicrobial peptide and potent mast cell degranulating peptide . Is active on both Gram-negative bacteria (E.coli MIC=7.8 ug/ml, and P.aeruginosa MIC=62.5 ug/ml) and Gram-positive bacteria (S.aureus MIC=15.6 ug/ml, and B.cereus MIC=7.8 ug/ml) . Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity). Shows a reduced level of hemolytic activity on rat erythrocytes . Interacts with both zwitterionic and anionic membranes, with 3 to 5 residues embedded into these two types of membrane . Its lytic activity appears to be influenced by the ionic character of the bilayer .
PTM: C-terminal amidation is important for the stabilization of the secondary structure in alpha-helical conformation and for activity . The non-amidated analog Protonectarina-MP-OH has a lower level of alpha helical structure than the amidated peptide, as well as a reduced mast cell degranulation activity, a complete loss of hemolytic activity, and a much more reduced antimicrobial activity compared to the amidated peptide .
Sequence Mass (Da): 1583
Sequence Length: 14
Subcellular Location: Secreted
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P0C022 | INLLKIAKGIIKSL | Function: Antimicrobial and mast cell degranulating peptide. Shows broad-spectrum antimicrobial activity against the Gram-positive bacteria S.aureus ATCC 6538 (MIC=5 ug/ml), S.saprophyticus CS (MIC=5 ug/ml), S.epidermidis CS (MIC=5 ug/ml), B.subtilis CCT 2471 (MIC=40 ug/ml), and the Gram-negative bacteria E.coli CCT 1371 (MIC=20 ug/ml), E.coli ATCC 25922 (MIC=50 ug/ml), and P.aeruginosa ATCC 15442 (MIC=20 ug/ml). Also permeates anionic liposomes. Has little hemolytic activity. Blocks the lobster neuromuscular transmission. Induces the depolarization of the muscle membrane . Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity).
PTM: C-terminal amidation is important for the stabilization of the secondary structure in alpha-helical conformation and for activity . The non-amidated analog eumenin mastoparan AF1 (EMP-AF1) has a lower level of alpha helical structure than the amidated peptide, as well as a reduced antimicrobial potency on both Gram-positive and Gram-negative bacteria . In addition, this non-amidated analog shows a reduced mast cell degranulating activity and is devoid of hemolytic activity .
Sequence Mass (Da): 1524
Sequence Length: 14
Subcellular Location: Secreted
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P0DRA7 | INWLKLGKKMMSAL | Function: Antimicrobial peptide. Has activity against both Gram-positive and -negative bacteria (B.subtilis (MIC=9 uM), E.coli (MIC=65 uM)). Shows mast cell degranulation activity (EC(50)=15-26 uM). Has low hemolytic activity (IC(50)=100 uM) . Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity).
PTM: C-terminal amidation is important for activity, since the deamidated MP-9 analog shows an important decrease in both antimicrobial and hemolytic activities.
Sequence Mass (Da): 1633
Sequence Length: 14
Subcellular Location: Secreted
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A1T9P9 | MTDRVTVGNLRVAPVLYDFINNEALPGTDIDPDTFWSGVDKVVADLTPRNQDLLARRDDLQAQIDRWHRARVIGGFEPEDYKQFLTDIGYLEPEPADFSITTAGVDDEITTTAGPQLVVPILNARFALNAANARWGSLYDALYGTDVISDEGGAEAGSGYNPVRGDKVIAYARRFLDGAVPLASGSWSDITGLKLDEGQLAATLDDGGTVGLGTPEQFVGYLGDAEAPTAVLLVNNGLHIEILIDAEAPIGATDKAGIKDVVLESAITTIMDFEDSVAAVDADDKVLGYRNWLGLNRGDLAEEVSKGGKTFTRVLNSDRTYTAANPGPDGATELTLPGRSLLFVRNVGHLMTNDAIVDAQGNEIPEGIQDALFTSLIGIHGLRTGDGNGPLVNSRTGSIYIVKPKMHGPDEVAFTCELFSRVEDVLGLPQNTLKVGIMDEERRTTLNLKACIKAAADRVVFINTGFLDRTGDEIHTSMDAGPMIRKGAMKSTEWIAAYENQNVDIGLETGFSGRAQIGKGMWAMTDLMADMVEQKIGQPRAGATTAWVPSPTAATLHAMHYHEVDVFAVHNELAGTRRGTVDQLLTIPLAKELAWAPEEIREEVDNNCQSILGYVVRWIDAGVGCSKVPDIHDVALMEDRATLRISSQLLANWLRHGVITEEDVKASLRRMAAVVDEQNAADPDFRPMAPDPDGSIAFQAAQELILSGADQPNGYTEPILHRRRREFKAASNVG | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 79327
Sequence Length: 734
Pathway: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.3.9
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Q50418 | MSIDAKLSRQASGSKAGVACVPDAYSFSEARSPGTRFALMLSAVAAGLAGGAMLHSAMSATSALTGLFIVLALAGGFLSTWSPCGYSSLSLLRPAGRYSFASVLRWSPTFFTHALGYAIGAVVLGGALGMAGWLLFSSLPFSYMVAGMAVLALGYGAHQFGFMKMPYPQRRAQVPHDARFRFRSSVIGLLYGYALGMNYLTYVQTPILYIVTGVALFCGDVKTAIVIIGIFNIGRCLPVAVNFLPVKNVTVQVWLARWQERAVEVDGFLLLSVGSAALMLLVL | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30033
Sequence Length: 283
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q50230 | MSMNIGATAMSRSSQAYAVETCVPDAYHFSKAQSTGTRFIMMLTAVASGVFAGRVMHSTMSVEMALTGLFVVLAFVGGLLSTWSPCGYSSLSLLRPAGRYSLGAVTRWAPTFFTHAVGYAIGAVVLGGALGGISWLLFADVPLQYAVIGLATLAIGYGLHQFGFLKMPYPQRRAQVPHDARFRFRSSVIGLLYGFSLGMNYLTYVQTPMLYIVTGVALLSGGVKAGIAVIAVFNIGRCLPVAVNFLPVKDQSVQAWLARWQESAVEVDGFLLLAIASAALMLVML | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30429
Sequence Length: 285
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q56463 | MASLDNFDMAAGRTDGVADCVAFPGRFSTWTRALILAASAAGGGAAALAMDAAHVALVLGLAAFAGGLLSTWSPCGYSSISLLRPTGKGARAVLDWLPTFATHGLGYALGALILGTLLGAIGGIAGLSGFATSFGLGLLAVIGLAYGAHQLDFLRVPYPQRRAQVPHDARQRFPKWVVGGLYGLSLGLDYLTYVQTPLLYLVTAAAVLSGNVAEAVALIAIFNLGRYLPVAVNLLPVTDYQIQSWLGRNQERAAIADGAILTAVGAAFAMLALA | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28174
Sequence Length: 274
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q49128 | MRAILPIPVLIAWAMVVCGGAYAVTTCSGAATATADASQQDLAALKARFRRPESVPHPKANPLTPEKVALGKALFFDPRLSRSGSVSCATCHNPSLGWSDGLTRAVGFGMVPLPRRTPPVLNLAWGTAFQWDGRADSLEAQARMPITAPDEMNMSMDLVVERLKAVPGYAPLFRNAFGSEEPIGARHVTAALATFQRTLVSGEAPFDRWALGDESAIGADAKRGFALFTGKAGCAACHSTWRFTDDSFHDIGLKAGNDLGRGKFAPPSVTAMRYAFKTPSLRDLRMEGPYMHDGQLGSLEAVLDHYIKGGEKRPSLSFEMKPFEMSERERRDLVAFLETLKAEPAAITLPQLP | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 38146
Sequence Length: 353
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Periplasm
EC: 1.-.-.-
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Q50233 | MLFRHLVLIISTLMVANTAWSANLPPREKFKRPDSIPAPLSNPLTLEKATLGKTLFFDQRLSRSGGMACATCHSPDQRWSDGRTLPLQAESVSNARRTPTVLNSAWLSALMWDGRATTLEEQAVLPITTAHEMNFDLASLVSRLQRIEGYRPLFTQAFGDDSISQQRITQALASFQRTLVSNIAPFDRWVAGDEQAISESAKRGFAVFNDKNKANCVACHSSWRFTDDSFHDIGLPSKDLGRGAKVPSQVTLMQHAFKTPSLRDLSIDGPYMHDGSIRGLKTVIKHYKSEAIQRESLSKDMQKFELSNLEESDLIAFIQSLDGGALKIQAPMMPE | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 37265
Sequence Length: 335
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Periplasm
EC: 1.-.-.-
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Q51658 | MLRLACLAPLAILIPAAGTAEQARPADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSVGDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAGQPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAAAEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITWNCRLCHMQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGIEDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFYNKYTSRRPEAKINPETGAPWGEPEVARNLSLAELQSGLMLDDGRVDALVAFLETLTDRRYEPLLEESRAAQKD | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 42230
Sequence Length: 387
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Periplasm
EC: 1.-.-.-
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P15283 | MSDIETFYDVMRRQGITRRSFMKSVRSPQHVLGLGPSFVPKIGEAMETKPRTPVVWVHGLECTCCSESFIRSAHPLAKDVVLSMISLDYDDTLMAAAGHAAEAAFEETIAKYKGNYILAVEGNPPLNEDGMFCITGGKPFVEKLRHAAEGAKAIISWGACASYGCVQAAAPNPTQATPVHKVITDKPIIKVPGCPPIAEVMTGVITYMLTFDRMPELDRQGRPAMFYSQRIHDKCYRRPHFDAGQFVEHWDDENARKGYCLYKMGCKGPTTYNACSTVPLERRRHFPIQSGHGCIGCSEDGFWDQGSFYDRLTTIKQFGIEATADQIGWTATGLVGAAVAAHAAVSVLKRAQKKNEEA | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39403
Sequence Length: 358
Subcellular Location: Cell membrane
EC: 1.12.99.6
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P31884 | MLEEKGIERRDFMKWAGAMTAMLSLPATFTPLTAKAAELADRLPVIWLHMAECTGCSESLLRTDGPGIDSLIFDYISLEYHETVMAAAGWQAEHNLEHAIEKYKGRYVLMVEGGIPAGSSEFYLTVGPHGTTGAEHARHASANAAAIFAIGSCSSFGGVQAARPNPTNAQPLSKVTNKPVINVPGCPPSEKNIVGNVLHFILFGTLPSVDAFNRPMWAYGLRIHDLCERRGRFDAGEFVQEFGDEGAKKGYCLYKVGCKGPYTFNNCSKLRFNQHTSWPVQAGHGCIGCSEPDFWDTMGPFEEPVANRLYATAFDGLGADKTADKIGITLLAATAVGVAAHAVLSMMVKDKENN | Cofactor: Binds 1 [3Fe-4S] cluster.
Catalytic Activity: a menaquinone + H2 = a menaquinol
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38294
Sequence Length: 354
Subcellular Location: Cell membrane
EC: 1.12.5.1
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P69743 | MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECTGCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGSIPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVLPGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDAGRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGIGFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGVSVMAVRELGRQQKKDNADSRGE | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.
Catalytic Activity: A + H2 = AH2
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39652
Sequence Length: 372
Subcellular Location: Cell membrane
EC: 1.12.99.6
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Q35127 | MRLLKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLACCLIIQIVTGVTLAMHYSPNVLEAFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVILILMMATAFLGYQHSPKWFDISNKGSISNKGNITNSLPPLLQRWGGRINKRLFNKNLVKRGYCTSSSLNSPEMSERLQTIINELGINPVYVYEDLNQPSSWKQILHDTRDLSGVYMIINKTTKDYYIGSASNNRFYTRFCNHVIHFTGSKIVKLAIKKYELKNFAFVILDLYPNVVTKENNKELLDLEDKYLKLLVPNYNILTEAGSSFGYKHTEIDRQKMKDLYSDARREKIGSLNRGKKFSPETIEKIREKALTRPPMSEETKIKCIANTRPVVLYNLNRTIYGKYSTILEAANAINCNEKTIRRALQTEKKLVKRQWIVEDFSDK | Function: Mitochondrial DNA endonuclease involved in intron homing.
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of cob exon 1 plus intron 1, containing the bI1 open reading frame.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51648
Sequence Length: 448
Subcellular Location: Mitochondrion inner membrane
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P03873 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGNMNIASNMFNMMKTIYMMMLMLLIYIFYTIMMRQMMKTKEYTMLIKSMDYINKNKYMINLNMTNKKDMNNNIGPLNMNILSIIYGSMLGDGHAEKRKGGKGTRIVFQQEYCNINYLYYLHSLLANLGYCNTNLPLIKTRLGKKGKIRQYLKFNTWTYDSFNMIYSEWYIKNMSGKGNIKVIPKSLDNYLTPLALAIWIMDDGCKLGKGLKFTTNCFSYKDVQYLTYLLHNKYNIKSTITKGNKENTQFVIYVWKESMPILTKIVSPYIIPSMKYKLGNYL | Function: This protein is responsible for splicing and maturation of cytochrome b mRNA. Specifically, it may be responsible for the splicing specificity of the second intron.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49326
Sequence Length: 423
Subcellular Location: Mitochondrion inner membrane
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A9RAG7 | MTIRKSNPYLSLVNSYLMDSPQPSSMNYWWNVGSLLGLCLVMQMASGMFLAMHYSSSMELAFNSVEHMMRDVNAGWLMRYIHANGASFFFMCLYLHMGKALYYGSYKSPRVLVWSMGVMMFMLTMATAFMGYCLVYGQMSHWGATVITNLLSAMPFMGGDLVPLSIILSLYLLYISLKTFMKMIFNQSYMCPAKGWVKKVLDNTFCIKKYMHMYLSSRTSPXLYINTMSNMQHMKIMSTKSHTKDRDTSFLEKDIKNMDRNLLALMVGFMDGDGYIRMNKKSKDNMNYIYMSLIMNLNKNDLKLLQYFHQQLNMGKVYNMTPKKGNKLARWEMNKLDLFNKMEPLLEYHNMKFLTETRQKQYLLLKYIKHNKLVYYEDIINNNNYINEFIENNTLMDNFIKLDYFNNWLVGFTMAEGSFLIKKNKDICFQLKQKYNLELFNNMTLFFNTTRKLNINKNKYMQFNVSSKNDIQNMINFFSFSNNQPLLGNKLISYNKWLFTIKNSMRYKELKTPYMSWHQKEQ | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61859
Sequence Length: 522
Subcellular Location: Mitochondrion inner membrane
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P0CY43 | MRLLKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLACCLIIQIVTGVTLAMHYSPNVLEAFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVILILMMATAFLGYVLPYGQMSLWGATVITNLISAIPWIGQDIVESKIITLIINLSFIAILFSIVVVYYYILLHVNFSSNLPTIGVIHQNALKKSNKALRLDKQEYISIPSSFLAFLAGLVDGDGYIQVTKTSKGFIAIKLVISLHLEDLSILEYIHSVLKIGKINIYKDLRSPTCKLVINKTDLQEILFPLLMYNKIFFLTNTRADQFNLAMYIFKNDIKMYNQIPDNTPAVFEIPKNPIDYTLLPFFKNWIVGFTCSEGSFFIKSNNDGCFQLKQRIHTNLFEAFKLMFNTNRKIDTTNNFNQFGVSSKSDIQKVINFFSFSGLHPLVGLKYIQYIKWLNNLRESLRYSTLNYPDAK | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (cob) gene, containing its own coding sequence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54555
Sequence Length: 477
Subcellular Location: Mitochondrion inner membrane
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Q9ZZW7 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFNMEDPYYSNMMLNKSVLCWNIFIWMMNYYIIQLIIYNNMIWNKNNMVKMFIMRRKLAVINMYMYMKLIIQRTYSYYMNNTIIYDKNHKLNTDNPIYAYIGGLFEGDGWITISKKGKYLLYELGIEMHIRDIQLLYKIKNILGIGKVTIKKLKMKDGTIKEMCKFNVRNKNHLKNIIIPIFDKYPMLTNKHYDYLYFKDNLLKDIKYYNDLSYYLRPIKPFNTTEDILNKNYFSSWLIGFFEAESCFSIYKPMNKKMKTASFEVSQNNSMEVMLAIKSYLKITQNIYTDKFNNSRMTTKSINGIKNVVMFINNNPIKLLGYKKLQYLLFLKDLRTITKYNNYFKIPPKY | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence. In vivo splicing requires the formation of a ribonucleoprotein complex together with the imported mitochondrial RNA-splicing protein MRS1. The complex seems to stimulate the intrinsic ribozyme activity of intron bI3 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61172
Sequence Length: 517
Subcellular Location: Mitochondrion inner membrane
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P03879 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNIVSDLFNPNRVKYYYKEDNQQVTNMNSSNTHLTSNKKNLLVDTSETTRTTKNKFNYLLNIFNMKKMNQIITKRHYSIYKDSNIRFNQWLAGLIDGDGYFCITKNKYASCEITVELKDEKMLRQIQDKFGGSVKLRSGVKAIRYRLQNKEGMIKLINAVNGNIRNSKRLVQFNKVCILLNIDFKEPIKLTKDNAWFMGFFDADGTINYYYSGKLKIRPQLTISVTNKYLHDVEYYREVFGGNIYFDKAKNGYFKWSINNKELHNIFYTYNKSCPSKSNKGKRLFLIDKFYYLYDLLAFKAPHNTALYKAWLKFNEKWNNN | Function: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exons 1 to 4 plus intron 4, containing the bI4 open reading frame. Cleavage would take place close to the Met-385 resulting in an active maturase of about 30 kDa.
Sequence Mass (Da): 74580
Sequence Length: 638
Subcellular Location: Mitochondrion
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Q8WQL7 | MNTADVPDNLQSWGQQPSSSYSNTQQHSQMTNLPPINHNNLCDTEPMNEDFQLQDVQADELQKQQKQQEQQHIQQQNAQRFIAQSRQPHSNILRFPQPPITSIKTNSHAFYPQQEVTQVRPKKHRVSMTNAEAALTPGMPPEKQAAKKRNIGQFSTDTVPAGIGMIGIPFESTSKPLQIQQFRNPQDAPVRKLTSDLIKTYKAINESFYLRKQVRRDRHKSQDAGKPKGSKDGSGASLTDTFSIHNAIPITSSDNHYQQDAHQNAPPLLDTNAPPTSTMVVPMRTETDLQQQQRQKSSRGGPYNNGYDDQNYDYILKNGEIFDKRYVILSDTPVGKGSFGQVTKAYDTLNKEEVAIKIIKNKKTFFDQAQIEIHLLELTNAHDKDNKYNIVTLKGHFVHRAHLCLVFELLSYNLYDLLKNTSFRGVSLNLARKFAQQLGKTLLFLSSPELSIIHCDLKPENVLLVNAKRSQIRVIDFGSSCQTGHRIYQYIQSRFYRSPEVLLGIAYDTKIDMWSLGCILVEMHTGEPLFAGSSEVDQMMKIVEVLGMPPKEMLDIGPKTHKYFDKTEDGIYYCKKTRDGYRHTYKAPGARKLHEILGVTSGGPGGRRLGEPGHSVEDYSKFKDLIKRMLQFDPKQRISPYYVVRHPFLKQKEERVPSQPPVSHSNLQQQQQLYIQQPSSQMSQVMESPSVGSVYVEDNGMYRQAPGSSANPISVTSSFDEGDAMEVDAGRRRFSAHQQNYHNPNYQYSQPQQQQQQQYQQTQRTQLEQQQKQAQLQQQLQQQQMQQQQQQQQQRQHMPQAQSSSQQHLQSRARPRQQDQNEWRNQFELDDTFQQKQRKVDDSVSNQISRNQFNPQQVSMTHGNVNANNREMEKLDYPNNKL | Function: Possible role in the function of olfactory neurons.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 101244
Sequence Length: 882
Subcellular Location: Nucleus
EC: 2.7.12.1
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Q73ZP8 | MSAATTADIDHYRTVLAGAFDDQVLEWTREAEARQRFPRELIEHLGARGVFSEKWCGGMLPDVGKLVELARALGRLSSAGIGVGVSLHDSAIAVLRRFGKSDYLRDICERAIAGQAVLCIGASEESGGSDLQIVRTEMSSRDGGFDIRGVKKFVSLSPIADHIMVVARSIDHDSASKHGNVALIAVPTSQASVQRPYAKVGAGPLDTAAVHIDTWVPADALVARAGTGLAAISWGLAHERMSIAGQIAASCQRAIGITLARMMTRRQFGRTLFEHQALRLRMADLQARVDLLQHGLNGIAAQGRLDLRAAAGVKVTAARLGEEVMSECMHIFGGAGYLVEETPLGRWWRDMKLARVGGGTDEVLWELVAAGMAADHGGYRSVVGASSA | Function: Catalyzes the dehydrogenation at the alpha-beta position of ACP-bound acyl chains. This results in the introduction of a double bond in the lipidic chain, which is further transferred to the epsilon-amino group of lysine residue in the mycobactin core by MbtK (By similarity).
Sequence Mass (Da): 41370
Sequence Length: 388
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 1.3.99.-
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O43462 | MIPVSLVVVVVGGWTVVYLTDLVLKSSVYFKHSYEDWLENNGLSISPFHIRWQTAVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSYSSSSSSSSSSSSSSSSSSSSSSSLHNEQVLQVVVPGINLPVNQLTYFFTAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLDGSTECCNNHSLTDVCFSYRNNFNKRLHTCLPARKAVEATQVCRTNKDCKKSSSSSFCIIPSLETHTRLIKVKHPPQIDMLYVGHPLHLHYTVSITSFIPRFNFLSIDLPVVVETFVKYLISLSGALAIVNAVPCFALDGQWILNSFLDATLTSVIGDNDVKDLIGFFILLGGSVLLAANVTLGLWMVTAR | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 . Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached . Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription . Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) . Involved in intramembrane proteolysis during bone formation . In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression .
Catalytic Activity: Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57444
Sequence Length: 519
Subcellular Location: Membrane
EC: 3.4.24.85
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O42954 | MDINPPPSTAPSSPRRSIQRISDAKNKALTFNRRRLGLIKKAHELSVLCDAKVVVMIFDSKNACHVYSSEEPEEQRDALLQKFLNKDFVTVDPLRNINPNIPSDESLHNWRPKDKRIASVTTYSAQPSNNCSSATDSENDFQSFTIKSSTTYHTTPTTASENKKIESITIPDHASVYNDLPLSPTVKHSFVSPVSGDYSDSPLEPSSSSSFSVPPESLNPTLSFQHNDVPQTDNFIPFLTPKRQAYGQSSSRADRSSVRRSQSFKNRRNGKPRISRLHTSHASIDGLTDFIQSPSSGYLDPSSTPITPLDSAINQITPPFLPDNLGQENRGELYSHDNPTSMVYEHPKFDELPNGFIDTHELNILSRSFTASPNQILRESNMVNQDSFTDNPVDATWDALIGTTQIDLDLDYERSSIPSSTIPADQLKDGVPTNSVYRNNMVDHNLYPSLNIERNAP | Function: Acts as a transcriptional activator with a role in the regulation of mitosis. Regulates septation and the periodic transcription of cdc15.
PTM: Phosphorylated. Occurs periodically during mitosis.
Sequence Mass (Da): 50907
Sequence Length: 457
Subcellular Location: Nucleus
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P04298 | MDANVVSSSTIATYIDALAKNASELEQRSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNETVPYDELIKELTTLSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGLDLENLYAVTKTDGIPITIRVTSNGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEPVNAINDRLEESKYVESKLVDICDRIVFKSKKYEGPFTTTSEVVDMLSTYLPKQPEGVILFYSKGPKSNIDFKIKKENTIDQTANVVFRYMSSEPIIFGESSIFVEYKKFSNDKGFPKEYGSGKIVLYNGVNYLNNIYCLEYINTHNEVGIKSVVVPIKFIAEFLVNGEILKPRIDKTMKYINSEDYYGNQHNIIVEHLRDQSIKIGDIFNEDKLSDVGHQYANNDKFRLNPEVSYFTNKRTRGPLGILSNYVKTLLISMYCSKTFLDDSNKRKVLAIDFGNGADLEKYFYGEIALLVATDPDADAIARGNERYNKLNSGIKTKYYKFDYIQETIRSDTFVSSVREVFYFGKFNIIDWQFAIHYSFHPRHYATVMNNLSELTASGGKVLITTMDGDKLSKLTDKKTFIIHKNLPSSENYMSVEKIADDRIVVYNPSTMSTPMTEYIIKKNDIVRVFNEYGFVLVDNVDFATIIERSKKFINGASTMEDRPSTRNFFELNRGAIKCEGLDVEDLLSYYVVYVFSKR | Function: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the methyltransferase OPG102 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure). Also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
Sequence Mass (Da): 96734
Sequence Length: 844
Domain: The N-terminus contains the triphosphatase and guanylyltransferase domains, whereas the C-terminus contains the methyltransferase domain. The N-terminus is involved in binding to the termination motif 5'-UUUUUNU-3' in the nascent mRNA.
Subcellular Location: Virion
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Q9LHQ7 | MKRGFSDSPSSSAPPPSSRFKSNPEGDSQFLEDETTKNFARKVADHYSRRTNQTLEEREASPIIHLKKLNNWIKSVLIQLYARPDDAVLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADHHQRRKKFSFPSRLLCGDCFEVELDKILEEDAPFDICSCQFAMHYSWTTEARARRALANVSALLRPGGVFIGTMPDANVIIKKLREAEGLEIGNSVYWIRFGEEYSQKKFKSSSPFGIEYVFHLEDAVDCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKPEFVELMRRLGALGDGSNDQSTLSADEWEAAYLYLSFVLRKRGESDGARRSGRRKNGKMNLSKDDVLYIDS | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42238
Sequence Length: 370
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q6Z9U7 | MNKRPRDEPSSSFASAPKRQYGAGGGGYGGHGYSEERSSARRVADHYSARSNQTLEERENSPIIHLKKLNNWIKSVLIQLYAHPGDCVLDLACGKGGDLIKWDKAKVGYYVGVDIAEGSIKDCMTRYNGDTDQQRRKKFSFPARLICADCYEARLDEHLYEDAPFDICSCQFALHYSWSTEARARQALANVSALLRPGGVFIGTMPDANVIIKRLRETDGMEFGNGVYWISFGEEYAEKKFPASRPFGIKYKFHLEDAVDCPEWVVPFHLFKLLAEEYDLELVLTKNFHEFVHEYLQKPEFAELMRRLGALGDGRQDQSTLSQDEWEVAYLYLAFVLRKRGQPPSQRRANNANRGKMFLTENDIDFLGV | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42040
Sequence Length: 369
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q5HZ60 | MSGFVVSKPEQSHHRLFDFAKTAIINIFAHPYATVCELYCGGAPETDKWEAAPIGHYIGIDTSSGISSVREAWESQRKNYDVEFFEADPSKDDFEIQLQKKLEQADLVSCWRHLQLCFETEESARRLLTNVACLLKPGGYFFGITPDSSTIWAKYQKNVEAYHNRSGAKPNVFPNYIRSESYMITFELEEEKFPLFGKRYQLKFSGDNASEDHCLVHFPSLIRLAREAGLEFVEIQSLTDFYDDNRAQFASLLMNAGPNFVDPRGKLLPRAFDLLGLYATFIFQKPDPDIEPPLTTPIPFESSNNHDERELPVITVITDASAPAEDPSQGLGKIVEQKGILGPGPADLRFSEAI | Function: mRNA capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39889
Sequence Length: 354
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q6K833 | MAVTPHHRLYEFAKTALIKIFAFPYATVCDLYCDGGVDTDKWGDAQIGHYIGIDASASGVNDARELWESRKKLFTSEFIELDPSADDFEAQMQEKGIQADIVCCMQHLQLCFESEEHAQKLLNNVSSLLKPGGYFVGIIPDSSTIWTKYQKNVEASHNKGLKTVPNSIRSENYVITFEVEEEKFPFFGKKYQLKFANESMFENHCLVHFPSFMRLAREAGLEYVEIQNLTEFYDDNRTQFAPLLGGYGSSLVDPRGKLVARSFDILGLYSTFVFQKPDPDAMPPIVTPELHDPENDQEEEWLWTQQASMDDGRVSRTDILPPADNEKGILGPGPADMRL | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38388
Sequence Length: 339
Subcellular Location: Nucleus
EC: 2.1.1.56
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A1CT57 | MENRSSSGTPRPSAGSPDAAKRPSETSPAAGRIPAGQNGSSGDKKRKVTEEGEASEKSEPPADRPMSKRKRMEERHQKLRKRGRTPPSAYSRRDAEAAPVPNRNRDDPANRSLSPLPHRSPTPEEQPRQRKRPGGGARMGLVDRETLRRRQEERERALVEEAMRTSQGRGVTDVVRQHYNAVPQRGREWRKTESKIKGLRSFNNWIKSTLIQKFSPDEEFLARLNDGRDWADDSGPPPAEEKRLLVVDLGCGKGGDLGKWQLAPQPVELYVGLDPAEVSIVQARERYNSMKSGRGNRGRRNPLFHGEFAPKDCFGEWLGDIGIVQQVGIDPNAGPGGSVMSSRWGGGGFDVVASMFAIHYAFESEEKARQMLRNVAGCLKKGGRFLGVCPNSDIISARVVELNAKRKAREEQEKKEKSDEAPEDGEVEEDTKLEWGNSIYRVQFPGKTPEDGIFRPPFGWKYSYFMEEAVEEVPEYVVPWEAFRALTEDYNLELQYRKPFLGIWGDEKDDRELGPLSERMGVRDRNTGELLMTEEEKEAANFYHAFCFYKV | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 62163
Sequence Length: 551
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q4WN42 | MYDPARDSWEERDGDEARSCRGRLASDQPHAVFSPPEQIHGASGENNNTTDLQQHPDPSSKTTASAEVLYAESQPAQPTTQTPPSVSTRIQSPVDPAAQKASNPQSLTSTAQNQLNKSNTTMENTSGSATPKPRADPSDKPNRPVQVASPTDQNGSQGDKKRKLPAEENASEKSQPAPDRPVSKRKRMEERHQKLRKRGRTPPSAYSRRDAEETSSAADRNGPTYRSTSPLPPPRSPTPEDQPRQRKRPGGGARMGLVDRETLRRRQEERERAQVEEAMRASQSRGVADVVRQHYNAVPQRGREWRKTESKIKGLRSFNNWVKSTLIQKFSPDEEFLARFNGTKEWAEDGGVPPVEEKRLLVVDLGCGKGGDLGKWQLAPQPVDLYVGLDPAEVSIVQARERYNGMKSGRGNRGRRNPIFHAEFRPKDCFGEWLGDVDIVQQVGIDPNVGPGGSVMSSRWGGGGFDVVASMFTIHYAFESEEKARQMLRNVAGCLKKGGRFLGVCPNSDVISARVSEINAKKKARQAQAKKEKSDEAPEDGEVEEDDGKVEWGNQIYRVRFPITPPEDGVFRPPFGWKYSYFMEEAVEEVPEYVVPWEAFRALTEDYNLELQYRKPFLDIWRDEKDDPELGPLSERMGVRDRVTGKLLMTEEEKEAASFYHAFCFYKV | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 74939
Sequence Length: 668
Subcellular Location: Nucleus
EC: 2.1.1.56
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Q9RPW2 | SLSHGKYYALGSGPARAMATKVKDGAVEPVEELYKELEYRDSHDKTVLVIENDAVPPVEIVEKVAAACGVSPADLTIIVTPTSSLAGGVQVVGRVLEVAMHKAHALHFPLENIVDGTGSAPVCPPHPNFVKA | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 13863
Sequence Length: 132
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Subcellular Location: Cytoplasm
EC: 3.5.4.27
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P51616 | MVSVNIEAKKIVDRMIEGADDLKISVDKLENGSTVIDCGVNVDGSIKAGELYTAVCLGGLADVGISIPGDLSERFALPSVKIKTDFPAISTLGAQKAGWSVSVGDFFALGSGPARALALKPAETYEEIGYQDEADIAVLTLEADKLPGEDVTDKIAEECDVSPENVYVLVAPTSSLVGSIQISGRVVENGTYKMLEALHFDVNKVKYAAGIAPIAPVDPDSLKAMGKTNDAVLFGGRTYYYIESEEGDDIKSLAENLPSSASEGYGKPFYDVFKEADYDFYKIDKGMFAPAEVVINDLRTGEVFRAGFVNEELLMKSFGL | Function: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+).
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 34230
Sequence Length: 320
Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 3/3.
Subcellular Location: Cytoplasm
EC: 3.5.4.27
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Q9RPD4 | ICLGGLGKVTLAPAPGQTNWPFWLTVTSNDPVVACLASQYAGWSLSHEKFFALGSGPGRSLARKEPLFQELPYEDSASRATIVLEAGAPPPEPVVAKVAESCGVSPDKLAFIYAPTQSLAGSVQVVGRVLEVALHKAHELKFPLEHIVDGIATAPLSPPHPDFVTAMGRTNDAIIYSGRAHLFVRGSAEAAKALAEKLPSSNSRDYGRPFAEIFKAYKGEFYKIDPSLFSPAEAIVTAVETGETFRAGAIDEKLLDASFG | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 27622
Sequence Length: 260
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Subcellular Location: Cytoplasm
EC: 3.5.4.27
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P14200 | MAKMSLSSYMLMLAFSLFSHGILLSASKSIRNVEDDIVFNTFRMGKAFQKEDTAERSVVAPSLEGYKNDESGFMKDDDDKTTKNTGSKQNLVTHGLPLSLAVKPYLALKGPAVFPAENGVQNTESTQEKREIGDEENSAKFPIGRRDFDMLRCMLGRVYRPCWQV | Function: MCH inhibits ACTH secretion at the end of the light on period which corresponds to the peak of the circadian rhythm in ACTH. Inhibits also stress induced ACTH release during the light off period of the cycle. Involved as a neurotransmitter or neuromodulator in a broad array of neuronal functions. Stimulates sexual behavior when injected into the ventromedial nucleus, this effect is antagonized by NEI. In the medial preoptic area, stimulates anxiety and sexual behavior. Antagonizes inhibitory effect of melanotropin alpha on exploration behavior.
PTM: Pro-MCH is processed differentially in the brain and in peripheral organs producing two neuropeptides; NEI and MCH. A third peptide, NGE, may also be produced. Preferential processing in neurons by prohormone convertase 2 (PC2) generates NEI. MCH is generated in neurons of the lateral hypothalmic area by several prohormone convertases including PC1/3, PC2 and PC5/6.
Sequence Mass (Da): 18482
Sequence Length: 165
Subcellular Location: Secreted
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Q7UPS1 | MKSATPDDLPRTGVEPDLSRSASECFESLWNGAIGMRSLPLTIAGARVLDAGVTCSGSLEAGLGLARLCLGDLANVRYVPATADDLVGLSVTIQTDHPVLSCLGGQYAGWPVSVADYFAMASGPMRCLRGKEAMLEQLHLSRQATDDDFAVGVLESDTLPGEDVIEAMADECGVDPSRLCLAVAPSTSIAGSAQVVSRSVETALHKLHALEFDVTRVVSAHGDAPLPPPAKKGDTIGGIGRTNDAMLYGARVTLWVDAEDDAIDSVASKVPSQSSDDHGRPFAEIFKQYEYDFYQVDPMLFSPAVVTIHSLQSGRTWRHGQISIDVMRKSFGL | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 35408
Sequence Length: 333
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Subcellular Location: Cytoplasm
EC: 3.5.4.27
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Q9RQ01 | MTSQATSQATSPALTTPVDAAPQISLATCVAPLVEALIRDADALRLKVSRGPRDALIVDAGITAAGGLEAGRRIAEICLGGLGRVALVPTGRFSPWDTLASVSTSGPVLACLGSQYAGWSLAAGDFFALGSGPGRAIAAVETLYGELGYRDRGEKVVLVLETAVVPPAEVVDEIAARCAVAPSDITLILTPTSSLAGTVQIVARVLEVALHKAHALHFPLEHIADGVGSAPICPPSPDFLTAMGRTNDAVLYGGDVHLFVHGPAEAAKDLATRLPSLASRDYGRPFGEIFAGYDCDFYKVDPLLFSPARVTVTAIDHGESFTAGGFDPILIARSFGG | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 34783
Sequence Length: 337
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Subcellular Location: Cytoplasm
EC: 3.5.4.27
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P29458 | MSSSQQSGRANELRTPGRANSSSREAVDSSPLFFPASSPGSTRLTTPRTTARTPLASSPLLFESSSPGPNIPQSSRSHLLSQRNDLFLDSSSQRTPRSTRRGDIHSSVQMSTPSRRREVDPQRPGVSTPSSLLFSGSDALTFSQAHPSSEVADDTVRVIWGTNVSIQESIASFRGFLRGFKKKYRPEYRNELMPPPDAEQLVYIEALRNMRIMGLEILNLDVQDLKHYPPTKKLYHQLYSYPQEIIPIMDQTIKDVMLDLLGTNPPEDVLNDIELKIYKIRPFNLEKCINMRDLNPGDIDKLISIKGLVLRCTPVIPDMKQAFFRCSVCGHCVTVEIDRGRIAEPIKCPREVCGATNAMQLIHNRSEFADKQVIKLQETPDVVPDGQTPHSVSLCVYDELVDSARAGDRIEVTGIFRCVPVRLNPRMRTVKSLFKTYVDVVHIKKQDKRRLGTDPSTLESDIAEDAALQIDEVRKISDEEVEKIQQVSKRDDIYDILSRSLAPSIYEMDDVKKGLLLQLFGGTNKSFHKGASPRYRGDINILMCGDPSTSKSQILKYVHKIAPRGVYTSGKGSSAVGLTAYITRDQDTKQLVLESGALVLSDGGICCIDEFDKMSDATRSILHEVMEQQTVTVAKAGIITTLNARTSILASANPIGSKYNPDLPVTKNIDLPPTLLSRFDLVYLILDRVDETLDRKLANHIVSMYMEDTPEHATDMEVFSVEFLTSYITYARNNINPVISEEAAKELVNAYVGMRKLGEDVRASEKRITATTRQLESMIRLSEAHAKMHLRNVVEVGDVLEAARLIKTAIKDYATDPATGKISLDLIYVNERETLVPEDMVKELANLISNLTVGGKTMLVSQLLTRFREQSSTRLDASDFEACLGAFREQSSTRLDASDFEACLGALERRGRIKVITSAGHRIVRSIAQTD | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Required for S phase execution.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 103728
Sequence Length: 931
Subcellular Location: Nucleus
EC: 3.6.4.12
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P30665 | MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEGNIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSSSSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRIIWGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSNLNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKFYKVRPYNVGSCKGMRELNPNDIDKLINLKGLVLRSTPVIPDMKVAFFKCNVCDHTMAVEIDRGVIQEPARCERIDCNEPNSMSLIHNRCSFADKQVIKLQETPDFVPDGQTPHSISLCVYDELVDSCRAGDRIEVTGTFRSIPIRANSRQRVLKSLYKTYVDVVHVKKVSDKRLDVDTSTIEQELMQNKVDHNEVEEVRQITDQDLAKIREVAAREDLYSLLARSIAPSIYELEDVKKGILLQLFGGTNKTFTKGGRYRGDINILLCGDPSTSKSQILQYVHKITPRGVYTSGKGSSAVGLTAYITRDVDTKQLVLESGALVLSDGGVCCIDEFDKMSDSTRSVLHEVMEQQTISIAKAGIITTLNARSSILASANPIGSRYNPNLPVTENIDLPPPLLSRFDLVYLVLDKVDEKNDRELAKHLTNLYLEDKPEHISQDDVLPVEFLTMYISYAKEHIHPIITEAAKTELVRAYVGMRKMGDDSRSDEKRITATTRQLESMIRLAEAHAKMKLKNVVELEDVQEAVRLIRSAIKDYATDPKTGKIDMNLVQTGKSVIQRKLQEDLSREIMNVLKDQASDSMSFNELIKQINEHSQDRVESSDIQEALSRLQQEDKVIVLGEGVRRSVRLNNRV | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for S phase execution.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 105003
Sequence Length: 933
Subcellular Location: Nucleus
EC: 3.6.4.12
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P55862 | MSGFDDLGVYYSDSFGGEQQVGDDGQAKKSQLKKRFREFLRQYRIGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPTEHLQLLEEAAQEVADEVTRPRPAGEETIQEIQVMLRSDANPANIRSLKSEQMSHLVKIPGIIIAATAVRAKATKISIQCRSCRNTIGNIAVRPGLEGYAMPRKCNTEQAGRPNCPLDPYFIIPDKCKCVDFQTLKLQESPDAVPHGELPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIRKSGKTSTKGRDRVGVGIRSSYIRVVGIQVDTEGTGRSAAGAITPQEEEEFRRLAAKPDIYETVAKSIAPSIYGSSDIKKAIACLLFGGSRKRLPDGLTRRGDVNLLMLGDPGTAKSQLLKFVERCSPIGVYTSGKGSSAAGLTASVMRDPVSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVYGRWDDTKGEENIDFMPTILSRFDMIFIVKDEHNEQRDMTLAKHVMNVHLSARTQSSSVEGEVDLNTLKKYIAYCRAKCGPRLSAEAAEKLKNRYILMRSGAREHERETEKRSSIPITVRQLEAIVRISESLGKMKLQPFATETDVEEALRLFQVSTLDAAMSGSLSGVEGFTTQEDQEMLSRIEKQMKKRFAIGSQVSEHSIIQDFLKQKYPEHAIHKVLSLMMRRGEIQHRLQRKVLYRIK | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82435
Sequence Length: 735
Subcellular Location: Nucleus
EC: 3.6.4.12
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O80786 | MSGWDEGAVYYSDQPQFPEAGDAATISPHAVLTKFKEFIRNFEIEQNCFPYREALLDNPKRLVVHLEDLLSFDSDLPSLIRSAPADYLPVFEKAAGEVLTGLKMREANEGGVMEEPLTRDVQILLTSREDPVSMRLLGAQYISKLVKISGISIAASRVKAKATYVFLVCKNCKKTREVPCRPGLGGAIVPRSCDNIPQPGEEPCPLDPWMVVPDRSQYVDQQTLKLQENPEDVPTGELPRNMLLSVDRHLVQTIVPGTRLTVMGIYSIFQASSSSNSHKGAVAIRQPYIRVVGLEDTNEASSRGPANFTPDEEEEFKKFADSQDVYKNICTKIAPSIFGHEDVKRAAACLLFGGSRKSLPDGVKLRGDINVLLLGDPSTAKSQFLKFVEKTAPIAVYTSGKGSSAAGLTASVIRDSSTREFYLEGGAMVLADGGVVCIDEFDKMRPEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPPSGRYDDLKTAQDNIDLQTTILSRFDLIFIVKDIRKYSQDKEIASHIIRVHASANKFSDENTDSKEDNWLKRYIQYCRARCHPRLSKDAAENLQRKYVTIRMDMKRRAHETGEAAPIPITVRQLEAIVRLSESLAKMRLSHEATPDDVDKAFKLFDTSTMDAARSGINQQINITGEMANEIKQAETQIKRRMGIGARLSERRLIEDLARMGMNDSMVRRALLIMHQRGEVEYQRERRSIVRKA | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81015
Sequence Length: 727
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q0V8B7 | MSGFDDPGIFYSDSFGGDNAADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEELADYLYKQPAEHLQLLEEAAKEVADEVTRPRPAGDEVLQDIQVMLKSDASPSSIRSLKSDTMSHLVKIPGIVIAASGVRAKATRISIQCRSCHSTLTNIAMRPGLDGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTSNRGRDRVGVGIRSAYIRVLGIQVDTDGSGRTFAGAMTPQEEEEFRRLAALPNIYELISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQAQAVEGEIDLAKLKKFIAYCRAKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQELLSRIEKQLKRRFAIGSQVSEHSIIQDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82146
Sequence Length: 734
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q21902 | MSNLDNPGIYYQERFFANDGVPDTGRELIAEYRQLITQFRNFIRDFSTGGFGMIYRDQLKRNYFSHEYRLEINLNHLKNFDEDIEMKLRKFPGKVLPALEEAAKIVADEITTPRPKGEEKLHDIQVTLTLDEYPTSLRQVKSAQVSQVVKISGIIVAAAQVRSKATKVTLQCRQCKHTIPDVSIKPGLEGFALPRTCAAPQQGQMQRCPIDPYIMLPDKCECVDYQTLKLQENPEDVPHGEMPRHLQLFTERYLTDKVVPGNRVTIVGVYSIKKLIQKKGGDKSLQGIRTPYLRVLGIHMETSGPGRTNFTTFTPEEERMFKTLAQRKDAYELIAKSIAPSIYGSADIKKSIACLLFGGARKKLPDGITRRGDINVLLLGDPGTAKSQLLKFVEQVSPIGVYTSGKGSSAAGLTASVIRDPQSRSFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVYGRWDESRGDDNIDFMPTILSRFDMIYIVKDTHDVLKDATLAKHVIEVHVNASAAKERDIAGVPKTATTDSDGVMTMFDTDGFLTIEFLKKFVTYARLNCGPRLTPQASEKLVNHYVKMRNPVVNADAFKSGKKAHNSAIPITVRQLEAIVRIAESIAKMELQQFATDKHVEEALRLFRVSTIEAAATGNLAGVEGFTSTADQEALNRIEVQMKKRFAIGTHVSEHLIVQDFVARQHYRESLVKKVIDNLVRRGDLQQKMQRKMLYRVR | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84936
Sequence Length: 759
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q54CP4 | MSGFDEGNVTVSGGGGKGGFKKNNGFVEDTSVRDLFKRFINEWKDQDNVFIYKEQLRQHYNLGWHYIEVSIDHLTDFNQELSGRFISSPNELMPSFEDAIKDIIKEMNYNKEQVDEDIQILFKSSANPEPIRYLRAGLISKLVKVQGIVISASRTQPKPSTMVVKCKNCQHTQTLHIRPGIVSSVLPQQCERGSNDAGKPCPNNPYVVLSDQSTFVNQQILKLQESPETIPTGEMPRHIILSLDKSLADKITPGTRIKVLGVLGIFEGGGKRREIAGGTIRTNYLRVLGITSDNAGRDSMHFTPSEEQSFKVFSRRQDLRNIIASSIAPSIYGHEDIKRAISCQLFGGSSKKLPDKMRLRGDINLLLLGDPGTAKSQLLKFVEKVAPISVYTSGKGSSAAGLTASVIREPSTGEYYLEGGAMVVADGGVVCIDEFDKMNVDDRVAIHEAMEQQTISIAKAGITTILNSRTSVLAAANPVYGRYNDAADDNINFQSTILSRFDLIFIVKDPKNEKRDFIISKHVINIHEKSSRSGGSGSVGNNTYDLSNTVVDDSHIGENEVTIQYLKKYIAYARSRISPRLSEDAVTTLKNHYVSVRAKSKEQEMINNGSYGGGGSKNSVETERKKRKNAIPITVRQLEAIIRISESLAKMSLSPIATNEHAKEAIRLFDISTFDAITTNNTVNETLTPERLENIRTAEKYLKDRVPIGSSIRIKDVRFQLSRSGLDHFTILKAVDILVGRDEFEFRNQKRTLFRKQ | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84221
Sequence Length: 757
Subcellular Location: Nucleus
EC: 3.6.4.12
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P33992 | MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built . The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82286
Sequence Length: 734
Subcellular Location: Nucleus
EC: 3.6.4.12
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P49718 | MSGFDDPGIFYSDSFGGDPGAEEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEELADHLHKQPAEHLQLLEEAAKEVADEVTRPRPAGDELLQDIQVMLKSDASPSSIRILKSDMMSHLVKIPGIIISASAVRAKATRISIQCRSCHNTLTNIAMRPGLEGYALPRKCNMDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLNPSKGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGSVSPQEEEEFRRLAALPNIYELISKSISPSIFGGMDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVIRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDMMLAKHVMTLHVSALTQTQAVEGEIDLAKMKKFIAYCRARCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGNLSGVEGFTTQEDQEMLSRIEKQLKRRFAIGSQVSEHSIVQDFTKQKYPEHAIRKVLQLMLRRGEIQHRMQRKVLYRLK | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82407
Sequence Length: 734
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q6KAJ4 | MSGWDEGAVFYSDQAQFPRGGPGGDPSADLTRHSALRKFKEFLRGFTGPTGDFPYRESLVHNRDHVTVAIEDLDAFDAELSDKIRKSPADYLPLFETAASEVLASLRSKVAGETGEMEEPATGDVQIFLSSKENCLSMRSIGADYMSKLVKIAGITIAASRVKAKATHVTLLCKNCRSVKTVPCRPGLGGAIVPRSCDHVPQPGEEPCPLDPWIAVPDKSKYVDLQTLKLQENPEDVPTGELPRNMLLSVDRHLVQTIVPGTRLTVIGIYSVYQASANQKGAVGVKQPYIRVVGLEQSRDANSNGPSNFTLDEEMEFKEFAQRPDAYVKICSMIGPSIYGHSDVKKAIACLLFGGSKKRLPDGVRLRGDIHVLLLGDPSTAKSQFLKFVEKTAPIAVYTSGKGSSAAGLTASVIRDGSSREFYLEGGAMVLADGGVVCIDEFDKMRPEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIAGRYDDLKTAQDNIDLQTTILSRFDLIFIVKDVRMYDQDKRIASHIIKVHASGAAASSKNTDASEGENWLKRYIEYCRVTCKPRLSEKAAEMLQNKYVEIRQKMRQQAHETGRAAAIPITVRQLEAIIRLSESLAKMRLTSVATPEHVEEAFRLFNVSTVDAARSGINEHLNLSPDIANEIKQAEAQIKRRMGIGSHISERRLIDELNRMGMNESIVRRALLIMHQRDEVEYKRERHVIVRKA | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80376
Sequence Length: 729
Subcellular Location: Nucleus
EC: 3.6.4.12
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P41389 | MAAATGWERSAVYYTPVLPGEQELDSNVSHEKNFIQFIEEFVIDNDFIYRTQLRDNLVVKQYMLNIDLRHLISYNEDLAHLLLSQPTDILPLFESAVTTVAKRLLYRSQENASTNIPTCQVTLRYDANILPIRNLTASHISKLVRVPGIIIGASTLSCRATALHLVCRNCRATRILQISGGFSGVQLPRVCEAPVLDGEKKDCPMDPFIIDHSKSTFIDQQVLKLQEAPDMVPVGELPRHILLNADRYLTNQITPGTRCVITGIFSIFQNKSVKASGAVAIRNPYIRVVGIQMDSNDGSKSTPLFSEEEEEEFLEISRTPNLYDIISNSISPAIYGNVDIKKAIACLLFSGSKKILPDGMRLRGDINVLLLGDPGTAKSQFLKFVERLAPIAVYTSGKGSSAAGLTASIQRDSVTREFYLEGGAMVLADGGIVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTILNSRTSVLAAANPIFGRYDDMKTPGENIDFQSTILSRFDMIFIVKDEHDETKDRNIARHVINLHTNLQESSETLAIGEIPFDKFRRYINYCRHKCAPNLDAEAAEKLSSQFVAIRKLVHQSEQDSNSRSTIPITVRQLEAIIRITESLAKMSLSPIASEAHATEAIRLFLTSTLAAATQSSPEVTEEVKKIEASLRKRLPIGFQASYRMLIREYVNGHGYSQHALEMALQIRSSKETIQLRNGGQTVYRSGV | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Role in DNA replication and essential for viability.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80100
Sequence Length: 720
Subcellular Location: Nucleus
EC: 3.6.4.12
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P29496 | MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQLSRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGTAKSQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNIDFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMKRYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRITESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKRRLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86411
Sequence Length: 775
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q5FWY4 | MELGGPAAAGDTDIAGQQLFKDELSDKCQKLFLEFLEECKGKDGSNLYVSAAEELIRPERNTLAVNFTDIEYYNQQLATTIQEEYYRVYPHLCRAVRSFARQMGNIPANKEFYIAFSDFPARQKIRELSSAKIGTLLRISGQVVRTHPVHPELVSGTFLCMDCQSIVKDVEQQFRYTQPTICKNPVCANRRRFTLDTNKSRFVDFQKVRIQETQAELPRGAIPRSVEIILRAEAVESAMAGDRCDFTGTLIVVPDVSALAAGDARMETGAKVTGGEGFNSEGVQGLKALGVRDLSYRLAFLACYVGATNPRFGGKDLREEDQTAESIKNQMTVQEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEIKRGVLLMLFGGVPKTTMEGTSLRGDINVCIVGDPSTSKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVKDEESHEFVIEAGALMLADNGVCCIDEFDKMDLKDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVGGRYERSKSLKHNVNLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHARNEESIERVYSIEDIQRYLLFARQFQPKITKEAEEFIVEQYRRLRQRDGSGVAKSSWRITVRQLESLIRLSESMARMHCSDEVQPKHVKEAFRLLSKSIIRVDTPDVSFDQGEDEKNIEGENNGNLNNGEEAMETNQDEPINEKPSSNAGLKMSFAEYKQISNLLVLYMQKMEETEEECHLTTTDLVNWYLKEMEAEIETETELILKKRLIEKVIHRLIYYDHILIELNKSELKTMDDTKETGEDAAEDRILVVNPNYMLED | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 92639
Sequence Length: 821
Subcellular Location: Nucleus
EC: 3.6.4.12
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P15529 | MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL | Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
PTM: N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43747
Sequence Length: 392
Domain: Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b.
Subcellular Location: Cytoplasmic vesicle
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O88174 | MTAAPLMPDSTHPCRRRKSYTFFWCSLGVYAEALLFLLSHLSDACELPRPFEAMELKGTPKLFYAVGEKIEYKCKKGYLYLSPYLMIATCEPNHTWVPISDAGCIKVQCTMLQDPSFGKVYYIDGSFSWGARAKFTCMEGYYVVGMSVLHCVLKGDDEAYWNGYPPHCEKIYCLPPPKIKNGTHTLTDINVFKYHEAVSYSCDPTPGPDKFSLVGTSMIFCAGHNTWSNSPPECKVVKCPNPVLQNGRLISGAGEIFSYQSTVMFECLQGFYMEGSSMVICSANNSWEPSIPKCLKGPRPTHPTKPPVYNYTGYPSPREGIFSQELDAWIIALIVITSIVGVFILCLIVLRCFEHRKKTNVSAAR | Function: May be involved in the fusion of the spermatozoa with the oocyte during fertilization.
PTM: May be O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40881
Sequence Length: 365
Subcellular Location: Cytoplasmic vesicle
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O02839 | MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASPPKDAESLDGGIIAAIVVGVLAAIAVIAGGVYFFHHKYNKKRSK | Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39692
Sequence Length: 363
Subcellular Location: Cytoplasmic vesicle
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Q96AQ8 | MDCGSVGGQRTQRLPGRQRLLFLPVGLSGRPGGSETSARRCLSALSDGLGALRPRAPAARGGVSRASPLLLLLLVPSPRLAAAAPRRQLGDWERSRLGYAAPPAGRSSAWRCSPGVAAAAGALPQYHGPAPALVSCRRELSLSAGSLQLERKRRDFTSSGSRKLYFDTHALVCLLEDNGFATQQAEIIVSALVKILEANMDIVYKDMVTKMQQEITFQQVMSQIANVKKDMIILEKSEFSALRAENEKIKLELHQLKQQVMDEVIKVRTDTKLDFNLEKSRVKELYSLNEKKLLELRTEIVALHAQQDRALTQTDRKIETEVAGLKTMLESHKLDNIKYLAGSIFTCLTVALGFYRLWI | Function: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion . Plays a direct role in uniporter-mediated calcium uptake via a direct interaction with MCU . Probably involved in the assembly of the membrane components of the uniporter complex (uniplex) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39694
Sequence Length: 359
Subcellular Location: Mitochondrion inner membrane
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Q9CXD6 | MDSGSVAAERPRRTPSRQRLPSSGCGVPARPGVSTLPGGRSWLRPRGRAARASPLLFLLLVPSPRLAATATATAPRRTLAERSRPGLVLPAAALGAGRNALGRLRLGARRVAALASSRRELSLSAKCHQLEHRKENLPLSVSRQLYFDTHALVCLLEANGFTIQQAEIIVSALVKITETNMNIIYKDMVSKMQQEIALQQVLSKIANVKKDMVILEKSEFSALRAENEKIKLELHQLKQQVMDEVTKVRTDTKLNFNLEKSRVKELYSLNEKKMLELRTEIVSLHAQQDRALTQTDRKIETEVAGLKTMLEAHKLDTIKYLAGSVFTCLTVALGFYRLWI | Function: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. Plays a direct role in uniporter-mediated calcium uptake via a direct interaction with MCU. Probably involved in the assembly of the membrane components of the uniporter complex (uniplex).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37849
Sequence Length: 340
Subcellular Location: Mitochondrion inner membrane
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Q0P4J6 | MSRLQLRFLLRRALSGSGCPRYSMPGSGCPGCFLPRVTCFRDFNIITSTMQYNLDKRNIYTSVGKHYFFDTHAVVQLLEANGFSAEQSEIVVSALVKILNVNMNLIHKDMVTKEQQEISLQQVMSLIASVKKDMIILEKSEFSALRTQNEKVKIELQQLKKQLNDSIVKVRASNKLDFNLEKSRVKEMHADNERKLLELRTSIVELHSQQDRGLTQTKRKIDTEVSGVKTMQESHKLDTIKYLAGSVFTCLTIALGFYRLWI | Function: Key regulator of mitochondrial calcium uniporter (mcu) required for calcium entry into mitochondrion.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30024
Sequence Length: 262
Subcellular Location: Mitochondrion inner membrane
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Q21121 | MRNGRCLVTPFVTAQRLANLRNTLWNRQQIAFSTTTASSSTSPIQESSSPLSIRFEYGLPLLDVPLPSRNEPCQFTMRPLSDTIGSLCEFLRQEDRGIDYVAVYGTNGVKLATCTSIEHLLQFGSFRLRLNDKFFDVTVPKTGTMPYDSDKLRQLDDLRATVASLHAALCVDEYKLSREKKLLLQLENAETLLAPLHDAKRKIEQECEAHTDRVMWAGFAAMGVQTGLFARLTWWEYSWDIMEPVTYFATYSTVCATFGYYLYTQQSFEYPSARERVYTKQFYRRAQKQNFDIEKYNRLVTEVDELRNQLKRMRDPLFQHLPVSYLSNLEAEK | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Required for rapid mitochondrial calcium uptake and mitochondrial reactive oxygen species (mtROS) production after wounding . In addition, together with mitochondrial calcium regulator micu-1, required for mitochondrial calcium uptake following axon injury in PLM touch receptor neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38554
Sequence Length: 333
Domain: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region (residues 293-316): while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core, which may contribute to stabilizing the transmembrane pore structure. The transmembrane pore is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH), which contains a kink around Glu-204 and interacts with the IJMH.
Subcellular Location: Mitochondrion inner membrane
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Q08BI9 | MAAKVCRSVLLLSRSSGAVASSAYPAFGVSSQRHQGTKTEALSMSLGGHQTVRRAHGLRTGGRCALFCHPSATLTAQGWKGSPSWQVQRLLCSPAAEDVSVVYQNGLPVISVRLPSRRERCQFTLKPLSDTVGVFLQQLQAEDRGIDRVTIYSADGARIASSTGIDILLMDNFKLVINDTSYLVQPPRRDLLPHEDGERLNDVKILVQQLYTTLRIEEHQLNKERELIGRLEDLNSQLQPLEKVKEELSKKAERRTTWVLWGGMAYMATQFGILARLTWWEYSWDIMEPVTYFITYGTAMAMYAYFVLTRQEYLYPDARDRQYLLFFHRGAKRTRFDIEKYNKLKDAIAEAELDLKRLRDPLQLNLPIQQIDTSKD | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes the pore-forming and calcium-conducting subunit of the uniporter complex (uniplex). Activity is regulated by micu1 and micu2. At low Ca(2+) levels mcu activity is down-regulated by micu1 and micu2; at higher Ca(2+) levels micu1 increases mcu activity. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes. While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42864
Sequence Length: 376
Domain: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region: while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core. The inner core is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH).
Subcellular Location: Mitochondrion inner membrane
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Q54LT0 | MNSFVIRNGFGLVRTFNTRLFTTSTQNLEGELKTILGQAKVSKLQEKLKLDPRSKITFNDFKGIAKEVGIEEKEINSVSNALAQSGSIIYLPNSLNENLKTSVFTKPAHIYQSLEHILDIENKGVGLNKLIESKKSEINSLRQKIQPLEEKKQVIDRKAHRRATAIIWTGLGYCFAQAAILARLTWWDLSWDIIEPVSYFLTFGSVLIGYTYFTMTKTEFTYEALNHRLFSKRQDKLFKRNNFPKEDYENLVQAIDKKEKELKELELATKYDHTH | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit . Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31756
Sequence Length: 275
Domain: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region: while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core. The inner core is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH).
Subcellular Location: Mitochondrion inner membrane
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