ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P06015 | MVTKERNAALKIVMLVASALTLHPQQALAQTAGRPLADVVGKTLCTYSKTAKRQAANLAQTLQRASSAAKQSRQAQQLAALALAKLPDYKEAAATLLIYATHKIQDAQASIENWTGENTKLVGQAMYSSGRIDELMLLLEGHREDGANGQDKTCLGAAAGGNTVNEFVKTECDTESGHNIEADNSNIGQAATTLSQESTDPEASGGASCKITANLATDYDSHANELPLLGGLLTIHNAGGFKTGQSLQTAAPTNKLISALKNKGAGVAAKLATVTSAAPTSKQELKTLLASKGERAKLQAANDEYNNWKPGAKPEDFDAH... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 52814
Sequence Length: 503
Subcellular Location: Cell membrane
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P06017 | DQKGKSPESECNKISEEPKCNEDKICSWHKEVKAGEKHCKFNSTKAKEKGVAVTQTQTAGGTEATTDKCKGKLEDTCKKESNCKWEGETCKDSSILVNKQLALSVVSAAFAALLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12530
Sequence Length: 115
Subcellular Location: Cell membrane
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P26335 | KNTGRRPNYRECEMRDGECNAKVAKTAEPDSKTNTTGNNSFAIKTSTLLLAVLLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6077
Sequence Length: 55
Subcellular Location: Cell membrane
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P20950 | MFTQAVIALIGLVSIRTGKTEDVTPCTTNCGCWARLEKQITVYRGDYSAAEENLKENKKNFGKIIAATVLGSEKLKATVAPVLLSAAQIIHECEEALTTARPAILDAEKKVAELRALYDVQQKLKEGNGELQLHIQDDTNINTAKEVPKANLGNINKKGCADDLNTPDAATIDKTNIETEGPTPKVITHVHVEARCQRDGTPTNGCHDGQLGQNGKLEFSLTYDSKDTNDLATWLADTATKKQISATEVDFIGNLNTEANTAIKGLKSSNPAPACSKKIRDYKTIADNSKFNLMVTKALIGKTDAEAGQESKEPELAAAI... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 49416
Sequence Length: 457
Subcellular Location: Cell membrane
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P02897 | MPTAGAVLLLATAAVLSRPAAAANEKKPLTISAAGAVCGFSNELKEVASFAATKVNAYLTETEQLGTLAVDFCAAIFNGNGKPTAGEVYAALLAAKTQTDRQAQQQKLVTGALLASSLCSQQAGHIESFIHVFYQAHRDATTTCIYKSDEHQRKAADVPCVNNGGGLNKITITTRATKPQLNSKYKAIVAGTTPNGAAAEKNCKLVNGEQSQNVFLASQTTNIALKWGDGLLTVPIGDTAISASNWEPNNKDSIASGNYKECAAALEQVPPRQSTATAAASKLLKLEAEDDPKLEEELISKNSFYGDFPISNVKITATDF... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 50723
Sequence Length: 476
Subcellular Location: Cell membrane
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P02898 | SEPTMSTRVQQATSCVLLIIGCTNYAASKQQTENNAVCDTPCKCLGRLAVQKAYLEGALEHARQSIKAFASSSRQHTIAAGATNTKLSGHHPNQGRRGRRRSSSARPNNSKGNSPSKRAGGAVRGETPASGRLKAAKLLKSSNYETATFTPTEMTIQNRRACEQVDESKEYRFDELNFDKEQGIPTPALTLEISMGCQKNPGDTGGACDGTNADDGVVTKLTFTTAAPVAETSPLVAGAYKKTSKASLSISNRTEEGRVANSKAAHEAAKRLMAIKQPSDLSTYTDDSSFALLVGQLAMKPPLGAELTPALRDQVNKFIT... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 49963
Sequence Length: 467
Subcellular Location: Cell membrane
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P0DJF0 | VVGGDCIPQVPFLAFLYSEYFC | Function: Thrombin-like serine protease which cleaves specifically the Aalpha chain of human fibrinogen (FGA) to release fibrinopeptide A. Also cleaves rapidly the Bbeta chain of human fibrinogen (FGB). Is selective for Arg over Lys at position 1 of the tripeptide substrates.
PTM: Glycosylated; required for activity. H... |
Q7LZF4 | VIGGAEENINEHRSL | Function: Snake venom serine protease that potently induces platelet aggregation. Its aggregatory activity is partially inhibited by monoclonal antibodies against GPIb and the thrombin receptor. Its ability to induce intracellular Ca(2+) release is blocked by pretreating platelets with thrombin. Hydrolyzes thrombin chr... |
C0HK18 | GGDECNINEHRSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATSRTLCAGILEGGKDTCHR | Function: Thrombin-like snake venom serine protease.
Sequence Mass (Da): 7072
Sequence Length: 64
Subcellular Location: Secreted
EC: 3.4.21.-
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C0HLA3 | VFGGDECNINEHRSLVVLFDSDGFLCAGTLINKEWVLTAAHCDSENFQMQLGV | Function: Snake venom serine protease that has fibrinogenolytic activity. Hydrolyzes the alpha-chain of fibrinogen (FGA), without affecting the beta- and the gamma-chains. Also displays hydrolytic activity towards S-2302 (plasma kallikrein substrate) and S-2251 (substrate for plasmin), but has no hydrolytic activity wi... |
Q9AST6 | MADVPGYLRTCLDMGKIAFLAILVSTGIVLQILACALFNNWWPMLSVIMYVLLPMPLLFFGGSDSTSLFNESDNSWINAAKFLTGASAVGSVAIPSILKHAGLIGWGALALDLSSYVVFLVAILGYICIGDASDNYYSYI | Function: Involved in endosomal protein transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15025
Sequence Length: 140
Subcellular Location: Endosome membrane
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P20948 | MKRVLSNVLKAWIFTIVAFHNFSTSVTADAPVNAAEYNALCRLYNIARAGEGLKEEDWLPCAGKAACEKTAASIEDVFMKLNFSEPSAVVTTLDGTRVELQNSASTRIKRAKLAKVLAAAETIKAQQLKYHESSKSLLESAKANFTKAIVGGWGNPTTPDESGLPTTFKTNRADDCKLAGGNGGKSLVFDIACLCTTSDSASGSKYTCGPKSGDNGSGWLDNNGDNQGKPAAKEAWKNLRADCRRQSAGVRVTPELISQSLVIFEGLIGTRAASGHDNARYIFGTVATAQSCGHSTATNKGSIDYKASNAQQRGDIEWEK... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44767
Sequence Length: 419
Subcellular Location: Cell membrane
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P20949 | MLDNSRARSIVHLLILLKAHVITQIIKNTQEFTSLCTFVKVTLKATDGLTSAASKSQTDWALGENPTSRIKKLITELETSSDRIRLGEEPNLTIQLPQGDPKQRLRRKLEVFLARAKYTEELVRQAQGDVGGRCNEAKAELEEAVTGRKGPDLETQATAAAAALHNKARGTACKVAGATTDTNFAGTSLVADLMCLCAAETNSREKHICGFESHASGVWANAGTNSNAGEIWGKILDACKNREIQVEVTPQFLRIAITKFEGLLGAQAHKLTSNGNAGAWLLGYSMNAGSVTCDGQSSTNGICVDYKGSSDARGPIAWLG... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44324
Sequence Length: 413
Subcellular Location: Cell membrane
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A6QLN9 | MLPWTVIGLALSLRLARSGAERGLPASALQGDLLFLLDSSASVSHYEFNRVREFLGRLAALLPVGPGALRASLVHVGSRPHTEFPFGQHSSGSAVQDAIRAAAQRMGDTNTGLALAYAKKQLFAKAAGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNLLELSAAASAPAEKHLHFVDVDDLHIITQALRGSILDAMWPQQLHASEVTSSGFRLAWPSLLTADSGYYVLELAPSTDPGAARRQQLPGNATGWAWTGLDSDTDYDVALVPESNVRLLRSQHLRVRTLPEETGPELIVVSHTRPRSLR... | Function: Promotes matrix assembly (By similarity). Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (By similarity).
PTM: N-glycosylated.
Sequence Mass (Da): 43738
Sequence Length: 413
Subcellular Location: Secreted
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Q6PCB0 | MLPWTALGLALSLRLALARSGAERGPPASAPRGDLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHTGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFVDVDDLHIIVQELRGSILDAMRPQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDVALVPESNVRLLRPQILRVRTRPGEAGPGASGPESGAGPA... | Function: Promotes matrix assembly (By similarity). Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (Probable).
PTM: N-glycosylated.
Sequence Mass (Da): 46804
Sequence Length: 445
Subcellular Location: Secreted
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Q8R2Z5 | MLFWTAFSMALSLRLALARSSIERGSTASDPQGDLLFLLDSSASVSHYEFSRVREFVGQLVATMSFGPGALRASLVHVGSQPHTEFTFDQYSSGQAIQDAIRVAPQRMGDTNTGLALAYAKEQLFAEEAGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTIFIVSTGRGNLLELLAAASAPAEKHLHFVDVDDLPIIARELRGSITDAMQPQQLHASEVLSSGFRLSWPPLLTADSGYYVLELVPSGKLATTRRQQLPGNATSWTWTDLDPDTDYEVSLLPESNVHLLRPQHVRVRTLQEEAGPERIVISHARPRS... | Function: Promotes matrix assembly . Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (By similarity).
PTM: N-glycosylated.
Sequence Mass (Da): 44709
Sequence Length: 415
Subcellular Location: Secreted
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Q92558 | MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFV... | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation . The WAVE complex regulates actin filament reorganization via ... |
Q9Y6W5 | MPLVTRNIEPRHLCRQTLPSVRSELECVTNITLANVIRQLGSLSKYAEDIFGELFTQANTFASRVSSLAERVDRLQVKVTQLDPKEEEVSLQGINTRKAFRSSTIQDQKLFDRNSLPVPVLETYNTCDTPPPLNNLTPYRDDGKEALKFYTDPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKEKLGTSGYPPTLVYQNGSIGCVENVDASSYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPVDNQRGSGLAGPKRSSVVSPSHPPPAPPLGSPPGPKPGFAPPP... | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via i... |
Q8BH43 | MPLVTRNIEPRHLCRQTLPSDTSELECRTNITLANVIRQLGSLSKYAEDIFGEICTQASAFASRVNSLAERVDRVQVKVTQLDPKEEEVSLQGINTRKAFRSSTTQDQKLFDRNSLPVPVLETYNSCDAPPPLNNLSPYRDDGKEALKFYTNPSYFFDLWKEKMLQDTKDIMKEKRKHRKEKKDNPNRGNVNPRKIKTRKEEWEKMKMGQEFVESKERLGPSGYSSTLVYQNGSIGSVENVDAASYPPPPQSDSASSPSPSFSEDNLPPPPAEFSYPADNQRGSVLAGPKRTSMVSPSHPPPAPPLSSPPGPKPGFAPPP... | Function: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via i... |
Q9UPY6 | MPLVKRNIEPRHLCRGALPEGITSELECVTNSTLAAIIRQLSSLSKHAEDIFGELFNEANNFYIRANSLQDRIDRLAVKVTQLDSTVEEVSLQDINMKKAFKSSTVQDQQVVSKNSIPNPVADIYNQSDKPPPLNILTPYRDDKKDGLKFYTDPSYFFDLWKEKMLQDTEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQPVTPSYAAGDVPPHGPASQAAEHEYRPPSASARHMALNRPQQPPPPPPPQAPEGSQASA... | Function: Downstream effector molecules involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape.
PTM: Phosphorylation by ABL1 promotes lamell... |
A7Z063 | MTPTGTQHSLAGQTYAVPLIQPDLRREEAIQQVADALQYLQKVSGDIFSRISQRVELSRSQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFMGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKFFPVCVNTKPEPEDEAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISRREQLERQVPENYFYVPDLGQVPDIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPTFHTEVAQPFKPDLEDGVLTARPPPPPPPPPPPAPAVL... | Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome ... |
Q8TAF3 | MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKST... | Function: Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46 . Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself . Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating... |
A7E3S5 | MASSAGLALCGHALVVRGGSRLLATSTSSSDGDSLFIYDCSAAEKKSQENKGEDGQPVDQGSDTVLASTFSKSGSYFVLTDDSKRLILFRTNPWQCLSVRTVVRRCTALTFTASEEKILVADKSGDVYSFSVLEPHGGGRLELGHLSMLLDVAVSPDDRFVLTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRIFVVPNHPELLLSSSGDCTLRLWEYRSGRELHCCPLTSLQEPTEPWSDKRFAVSRITYWSQEDCVALSCDGLPVVYIFQLDAAQRQLVPRQLLTFQHRVWDAAFEEGHGLWVLQDCREDPLVLYRP... | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding. Required for the formation of N... |
Q23232 | MSFITAFRERVFIASGDLIRTFRISEETELKNFISWSKINPERIQKPSFDIEKELKAVEKRVILCLAHSNVLTTHGRRLVAVGTNEKQIHVFEYFVNDKGDIVTAEHIVTSVVPKAPTAIVFDKEDAYVVVGDRAGDVHRFSVLNGSAIEMAGAISMILDVAFSPDGKRLLMADRDEKVRALRYPATSVIDSFFLGHTEYVKTLAVQDNDSLWSSGGDKNLYNWSIAKCSAPRRTLDLSQFDAPIRKISINLQHKKIAVIFEKIETVVIVDLNQESLQTTSVSIVGESQCLDIASTKDYFAVLGRSTVHLIDLNNMEQKF... | Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Sequence Mass (Da): 43639
Sequence Length: 388
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular ... |
A4IGH4 | MAVVCSKADWFVTSCSTTLVAVNLKQSREPFVFDCSKAEKKPKEADVDNKSAGEGSEEKDSDSILAFAISASGKHVALTDDHKRLVLFCTEPSWKCISTRWVVRRCTSLAFTQAEDELYVADKSGDVYSFSILEPHKAGELKLGHLSMLLDVALSPDDKYIITADRDEKIRVSFRRSPYNIQAFCLGHTEFVSSLLVPAGHPDWLLSGSGDGTVNVWHYETGRRLHSVDMRKFGLDSENTEKRFAVSRIISSPDGQHVAVQCEGFPSVQLFTVDCGTEGLLKPADTLTLPLSPWDVTFDSENQLWVLLESEDMKVLLYRH... | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, wdr4 acts as a scaffold for tRNA-binding. Required for the formation of N... |
Q54UI3 | MSTTAVFIPPQIMVTSNVEKVPISIITHSSDSNFIAYRLNNKLNIFDNKLNKLGELESGSQHTGIIRSIEFTKNNQSLITSSSDKFLKIWDTTNNFKNIKSINTNKKIICSILNKDDSEILVSDKCGDVFKYSLIDDSKNKIEVSGDKSAKHDEKESDKNLVFGHYSSIVDIKFSPCFNYLLSADRDEKIRVSHYPNCFDIESFCLGHTKYVTEILLVPGRDDLLISGSGDGTIKLWNWKQGKCLQTVDFNSKHENAITIPQVVFKVDATTTTNQLIFSIENSNNIYILPMNVEKGEFNQSELKTIPLTQSSPISIDLID... | Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Sequence Mass (Da): 52703
Sequence Length: 467
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular ... |
P57081 | MAGSVGLALCGQTLVVRGGSRFLATSIASSDDDSLFIYDCSAAEKKSQENKGEDAPLDQGSGAILASTFSKSGSYFALTDDSKRLILFRTKPWQCLSVRTVARRCTALTFIASEEKVLVADKSGDVYSFSVLEPHGCGRLELGHLSMLLDVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRISVVPTQPGLLLSSSGDGTLRLWEYRSGRQLHCCHLASLQELVDPQAPQKFAASRIAFWCQENCVALLCDGTPVVYIFQLDARRQQLVYRQQLAFQHQVWDVAFEETQGLWVLQDCQEAPLVLYRPV... | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs) . In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding . Required for the formation of... |
Q9EP82 | MASSAGLALCAQTLVVRGGSRFLAFSTTGSDDDCVFTYDCSTAEKKATPEDKGEDGQPADTGSDSILASTFSKSGRYFALTDDSKRLILFRTKPWQCLSVRMVVRRCTALTFTASEDRVLVADKSGDVYSFSVLEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRILVVPSHPELLLSSSGDGTLRLWEYRSGRQLQCCDLAGLQEPGEQPGHKGLAASRIAFWGQESYVVLLCECVPVVFVFQLDASRQQLVFRQRLTFPHRVWDVVFEEARGLWVLQDCRDAPLVLWR... | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs) . In the METTL1-WDR4 methyltransferase complex, WDR4 acts as a scaffold for tRNA-binding (By similarity). Required for t... |
Q7ZY78 | MLRVGPGSLAITGGSRLLGHRVGSECCPFHLDCSLLEKQSAAPGQEGSADSHGSDKILAAAFSPSGEYFALTDDNKRLVLFRTKPAWEKISVRWVSRRCTALTFSPCGNHILVADKSGDVFSFSVPRALEQGRLELGHLSMLLDVTVSLDGKHIITCDRDEKIRVSCWGAPHVIMSFCLGHTEFVSQLLPLPGQEKLLLSGSGDGTLRLWEYESGKEVHSVTLRSLAHELEDQENKRFAVSRISCCSCNGIQLAVLCEGVPGIFLFSVSPEPRLTFTQYIALTHTPIDLDFDGSAFLWVLSGVREEPLLKYKELDDQWQS... | Function: Non-catalytic component of the METTL1-WDR4 methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the METTL1-WDR4 methyltransferase complex, wdr4 acts as a scaffold for tRNA-binding. Required for the formation of N... |
P27833 | MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALINFLKEAEIMAVFH... | Function: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate.
Catalytic Activity: 2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate
Sequence Mass (Da): 41901
Seque... |
Q84LH3 | MSSSNWIDDAFTEEELLAIDAIEASYNFSRSSSSSSSAAPTVQATTSVHGHEEDPNQIPNNIRRQLPRSITSSTSYKRFPLSRCRARNFPAMRFGGRILYSKTATEVDKRAMQLIKVLDTKRDESGIAFVGLDIEWRPSFRKGVLPGKVATVQICVDSNYCDVMHIFHSGIPQSLQHLIEDSTLVKVGIGIDGDSVKLFHDYGVSIKDVEDLSDLANQKIGGDKKWGLASLTETLVCKELLKPNRIRLGNWEFYPLSKQQLQYAATDAYASWHLYKVLKDLPDAVSGS | Function: Exonuclease that digests recessed strands of DNA duplexes in the 3' to 5' direction but hardly single-stranded DNA or blunt-ended duplexes. Also able to digest 3'-protruding strands and 3'-recessed strand termini of duplexes containing mismatched bases.
Sequence Mass (Da): 32090
Sequence Length: 288
Subcellul... |
Q077R2 | MELVSIIIAAYNCKDTIYATVESALSQTYKNIEIIICDDSSTDDTWDIINKIKDSRIICIKNNYCKGAAGARNCALKIAKGRYIAFLDSDDYWVTTKISNQIHFMETEKVFFSYSNYYIEKDFVITGVFSSPPEINYGAMLKYCNIACSTVILDRTGVKNISFPYIDKEDYALWLNILSKGIKARNTNLVDTYYRVHAGSVSANKFKELIRQSNVLKSIGIKAHHRIICLFYYAINGLIKHCFSYRDKRNA | Function: Catalyzes the addition of Glc, the second sugar moiety of the O56-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = beta-D-Glc-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl d... |
Q5R9R3 | MAGAIIENMGTKKLCIVGGILLVFQIIAFLVGGLIAPGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVSMDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCG... | Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Also plays an important role in establishment of the anterior-posteri... |
P43446 | MSSHDISWHSPASVYFSSDLDVKRIAGKLRGCWTDLLLRQESCCERVLQKSSSSMDYFLFRLFCSLALASLLVQRADSNEILGLKIPFDPILNANTVCLTLPGLTKKQLDVCMRNPDVTASAIQGIQIAIHECQHQFRGHRWNCSSLETRNKIPYESVVFSRGFRESAFAYAIAAAGVVHAVSNACAMGKLKACGCDEKRRGDEEALRIKLNRLQLEAINRGKGMVHGVMEHFPAEALGPQDSWEWGGCSPNVEYGERFSKDFLDSRETYRDIHSRMRLHNNRVGRQVVVDHMRRKCKCHGTSGSCQLKTCWQVTPEFRT... | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Required for normal tooth development . Regulates the expression of genes involved in tooth development .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt sign... |
Q9GZT5 | MGSAHPRPWLRLRPQPQPRPALWVLLFFLLLLAAAMPRSAPNDILDLRLPPEPVLNANTVCLTLPGLSRRQMEVCVRHPDVAASAIQGIQIAIHECQHQFRDQRWNCSSLETRNKIPYESPIFSRGFRESAFAYAIAAAGVVHAVSNACALGKLKACGCDASRRGDEEAFRRKLHRLQLDALQRGKGLSHGVPEHPALPTASPGLQDSWEWGGCSPDMGFGERFSKDFLDSREPHRDIHARMRLHNNRVGRQAVMENMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGALLRSRFHRATLIRPHNRNGGQLEPGPAGAPSP... | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays a role in normal ectoderm development . Required for normal tooth development . Required for normal postnatal development and maintenance ... |
P70701 | MGSAHPRPWLRLPQGPQPRPEFWALLFFLLLLAAAVPRSAPNDILGLRLPPEPVLNANTVCLTLPGLSRRQMEVCVRHPDVAASAIQGIQIAIHECQHQFRDQRWNCSSLETRNKVPYESPIFSRGFRESAFAYAIAAAGVVHAVSNACALGKLKACGCDASRRGDEEAFRRKLHRLQLDALQRGKGLSHGVPEHPAILPASPGLQDSWEWGGCSPDVGFGERFSKDFLDSREPHRDIHARMRLHNNRVGRQAVMENMRRKCKCHGTSGSCQLKTCWQVTPEFRTVGALLRNRFHRATLIRPHNRNGGQLEPGPAGAPSP... | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a role in normal ectoderm development. Required for normal tooth development. Required for normal postnatal development and maintenance of tongue papillae... |
P28131 | SGSCQLKTCWQVTPEFRVVGNLLKERFYGATLIKPHNRNTGQLDHSHIPHRRRTSINSLVYFEKSPDFCEREPQLDSTGTQGRICNKTSPGMDNCESLCCGRGHNILRQTPSERCNCKF | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Required for normal tooth development. Regulates the expression of genes involved in tooth development.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway... |
Q801F7 | MELPHRQCLGRVLIVTAALLSPAFTVLGNDILGLKVAGEPVLTPNAVCLRLAGLTKKQMRLCVRSPDVTASALQGIQVAIHECQHQLRDQRWNCSSLENHGKLPHQSAILNRGFRESAFSLSLLAAGVVHSVASACSLGKLRGCGCEAKRRLDDDKIRLKLTQLQLQTFQRSGVSLAGAGENTPELSSLHGSLPANLHSSHPMSLLKPLPDEVTMLQDTWEWGGCSHDIRFGVRFSRDWLDSRGSPRDIHARTRIHNNRVGRQVVTDNMRRKCKCHGTSGSCQFKTCWYVSPEFRLVGSLLREKFLTAIFINSQNKNNGV... | Function: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Involved in neurogenesis. Performs a partially redundant function with wnt1 in the formation of the midbrain-hindbrain boundary (MHB) organizer.
PTM: Palmitoleoylation is required for efficient b... |
P48614 | MLEEPRSRPPPLGLAGLLFLALFSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRSPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKTFPISQPSPVPGSVPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAIGAALRERLSRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCER... | Function: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripot... |
P49893 | MAPTRHWVTPLLLLCCSGICGAIQWLGLTVNGSRVAWNESEHCRLLDGLVPDQSQLCKRNLELMQSVVNAAKQTKLTCQMTLSDMRWNCSSVENAPSFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSAGTQATKIMNLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCCGRGYNAY... | Function: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signa... |
P31283 | QECKCHVSGSCTLRTCWRALSDFRRTGDYLRRRMNGAVQVMATQDGANFTSARQGYRRATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCC | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 14312
Se... |
A0A7J6K7Y0 | MPEQDLASGFLLRFQNARPVCLSVGSFVSFRTVQPRKMRDRGWRCVWHRMAGVGALFGIFGVLCTVEAGATVAAPQVETGPLLSVRAPRSPLHLRDVDAPEVTHASSEGSPQFESSLSQQRLRRPADRGEAHNGEEPRKDAATQTVRGYGGQSTEPPPASIVPVSSEAPQDGAEQRQASSAAESLAGLDPDAGDTGLRSQEMDEEGSGAAQDMERAHAAQPTVSTWDDAHLVQVSTSHPDMFPVDGSFSKKQEGRRERRLAVRGDDSFARGHNRDRDASNGRSILRRAPGWAKIAALATGLLVSAFGYSSYKHGGPRVAL... | Function: Serine/threonine-protein kinase which, at the tachyzoite stage, phosphorylates several parasitophorous vacuole (PV)-resident proteins such as GRA2, GRA6 and GRA7 . By phosphorylating GRA2 and GRA6, regulates the formation of a functional intravacuolar network (IVN); IVN is composed of membranous tubules that ... |
A0A7J6K7I9 | MMFPAVAAPPRRLPGERLQRSQNPVETSWLSFRILATRGPCVTSTFLFLTVAFLGLSWVSVAVAAHAEHPEDSATNFLFSFAENSLANREPPEDSAARPSSRSGGAERRRLDSLIPGFLKRRRIFKQLRPVDEFQLREFQEASSKVKAQFFSAGHSKVTFVDRPSAALLSFLHLEEEDVPYGVVIKAIPYDAFDFYESVAEPYIHRMFDDPRKFPYVVPVLAALRSTSKRVLYLVLPLYRELPETVDEEARSLDFVLLLAEMAMAVCQLHERNLAHRDLKEDNFLVSPEGHIVVSDLATLDITDNKSFLIGTSGYMPPET... | Function: Probable serine/threonine-protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61601
Sequence Length: 553
Domain: The protein kinase domain has an atypical kinase fold which lacks the glycine-rich loop that is critical for ATP binding in ca... |
Q8RXE5 | MEEADFVQKDPTGRYIRYNDVLGRGAFKTVYKAFDEVEGIEVAWNLMSIEDVLQMPGQLDRLYSEVHLLNSLKHDNIIKLFYSWVDDHNKSINMITELFTSGSLTLYRKKHRKVDPKAIMNWARQILKGLHYLHSQTPPVIHRDLKCDNIFVNGNTGKVKIGDLGLAAVMQQPTARSVIGTPEFMAPELYEEEYNELVDIYSFGMCMLEMVTCEYPYRECRNQAQIYKKVTSGIKPQSLSKVDDPQVKQFIEKCLLPAPSRPTALELLKDQLLAVDGAKDSTLTASSNTTFKPAMPPQCEYRPMDVEYKKNTSVSICSSA... | Function: May regulate flowering time by modulating the photoperiod pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59246
Sequence Length: 524
EC: 2.7.11.1
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Q6ICW6 | MMTCASSDDNESEKDKDSESFVEVDPTGRYGRYGELLGSGAVKKVYRAFDQEEGIEVAWNQVKLRCFSDDPAMTERLYSEVRLLKNLKNSNIITLYKVWRDERNNTLNFITEICTSGNLREYRKKHRHVSMRALKKWSKQILKGLDYLHTHDPCIIHRDLNCSNIFVNGNIGQVKIGDLGLAAIVGKNHLAHSILGTPEFMAPELYEENYTEMVDIYSYGMCVLELVSLEIPYSECDSVAKIYKRVSKGLKPEALNKVNDPEAKAFIEKCIAQPRARPSAAELLCDPFFDGILDDDDEDGENNDNNGAGRIVVS | Function: May regulate flowering time by modulating the photoperiod pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35531
Sequence Length: 314
EC: 2.7.11.1
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Q9CAV6 | MNNLSYLEPDYSEFVEVDPTGRYGRYNEVLGKGASKTVYRAFDEYEGIEVAWNQVKLYDFLQSPEDLERLYCEIHLLKTLKHKNIMKFYTSWVDTANRNINFVTELFTSGTLRQYRLRHKRVNIRAMKHWCRQILRGLHYLHSHDPPVIHRDLKCDNIFVNGNQGEVKIGDLGLAAILRKSHAAHCVGTPEFMAPEVYEEAYNELVDIYSFGMCILEMVTFDYPYSECTHPAQIYKKVMSGKKPDALYKVKDPEVKCFIEKCLATVSLRVSARELLDDPFLRIDDGEFDLRSVDMEDSVGPLYRQPHHLPDYYNYPSNSS... | Function: Regulates flowering time by modulating the photoperiod pathway. Phosphorylates APRR3.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80208
Sequence Length: 700
EC: 2.7.11.1
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Q9FMH6 | MAETETESITTSSPPPISETENSTTLPTTETEKNPNPVTISLRIWPPTQKTRDAVINRLIETLSTESILSKRFGSLESEEASSVAKSIEDEAYAIASATVFGDDDGIEILKAYSKEISKRMLESVKAKSNVASPPPKDGDGIESAVDSKIDSSEA | Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting.
Sequence Mass (Da): 16634
Sequence Length: 155
Domain: The WPP domain is required for the nuclear envelope localization.
Subcellular Location: Nucleus envelope
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Q9C500 | MAETAETINTTISSPPPESESSTTISAMTDPTSQEAASKDTDLTKEAESEKKPGGISLRIWPPTQKTRDAVLNRLIETLSTESILSKRYGTLKSDDATTVAKLIEEEAYGVASNAVSSDDDGIKILELYSKEISKRMLESVKARSNASVGNGSVEDANTDASEVSKDDAGPASEEEKSEA | Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting.
Sequence Mass (Da): 19134
Sequence Length: 180
Domain: The WPP domain is required for the nuclear envelope localization.
Subcellular Location: Nucleus envelope
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P54423 | MKRRKFSSVVAAVLIFALIFSLFSPGTKAAAAGAIDQAAALENGKEQTGAMKEPEQVKWYKVTPGATDIQKNSHMALTVKSDSVLNVSVYPSKEKALKDETFEMYRSFTAEDGKSEVIFPYAWSGPYYVKVEYLGEEEPEDGGTAEAAAEAKYTIGYKGTKKQPSDLEEEEACPVEMSVDQKKSGKGILDKLRSIRDEQLSQTAEGKELTSLYYKAAPFIVAKLALNKTARNEIYQDLVTLKPLFDDVSENGASSSYKVTEKDQKAINRLYDKALQSVPSFLKEEIKKQADRLNMKQLQGKTAGAILTENNIAAKSEVQT... | Function: CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges.
PTM: Proteolytically cleaved to yield CWBP23 and CWBP52.
Sequence Mass (Da): 96488
Sequence Length: 894
Subcellular Location: Secreted
EC: 3.4.21.-
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P50902 | QGYSTVAFDGPPSYGHAPSHHAAQFSNHSFKHEDPIAQQTSLGDQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYNSDNLYQMTSQLECMTWNQMNLGSTLKGHATGYENENHTAPMLYSCGAQYRIHTHGVFRGIQDVRRVPGVAPTIVRSASETNEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL | Function: Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as a... |
P19544 | MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAQWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYGPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTPTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGSSSSVKWTEGQSNHSTGYESDNHTTPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEK... | Function: Transcription factor that plays an important role in cellular development and cell survival . Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' . Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppre... |
O62651 | MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAEWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYEPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTSTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGTSSSMKWTEGQSNHGAGYESDSHATPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEK... | Function: Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppress... |
Q96WS1 | MNSNYVPLTSSVDVEEKMESENGVDLGNDIDLEKGLPLKYNSENESGLPSNSASSYLINPDPTMDLEAQTFNHNESTTSVGHDNSNSPPKCRKTCSSNKVYSNEVPLLFVFVISISIVCIFDLVIFGCLQYNMVSMDDLHVMQRLSWFCASLALLFILMRYYDFWTKACKDGIKHIFKKWKNTPLAFLQVLIFNIIGFFVRKGLKDSFGEQWGLKTSLFAHVSFATMSIFIFIFETLKPGSCSVDWIARILKAVVYFLEDSDEL | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29937
Sequence Length: 264
Subcellular Location: Membrane
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O74512 | MENNHHLAKDSLDELNPKRGKGEHETQVSQYTVVEEATIPQSLVKTSRPADHKVMEASKVADTRTAWSTKIPAVLLPVFVINIALFKYLVFANFSTKDRVLFGLGNGGINIFSMWLLLATYETWFRSIKEVIVACGAGIRSFPQKRGVNMLYAILKLTFVNAFAIPLLMFFRSHFEQWRLGCPLVERVIGVMLNVAYFIIEIENPGLFTRVFNKYCDCLFAIRDILNRN | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26109
Sequence Length: 229
Subcellular Location: Endoplasmic reticulum membrane
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G2TRU7 | MSNNYTSLSSSLDEEMGLKAGHEIDLEGSPPSEHNSEEKSTLPSNSDILTSANPVSQASETPDHSIESNTGSTQSPTSHSLLLKFSFCIVYYSYFAIVVLGCVLPFEHTHTFLIAFLVIFGIISVILFSGSIYYYETWTKTVKHFLKKVISPFKKEYIVCAFLKTFVFYGLLKTIEHFLVLLSGDKWGWKCSTLSSILTPVSCISFCLNESVQLRSCSTHLFINTVAWIKSLGGGKNAFENNYNQLNETSPEDLV | Function: May act in meiotic drive.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28404
Sequence Length: 255
Subcellular Location: Spore membrane
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Q94CT7 | MGHGLSCSRDTDEYDLFRAAQLGDIHALSALLAADPALARRATVYDRFTALHIAAANGRLQVLSMLLDRDGDVDVLSRKKQTPLMVAAMRGNTECVVRLLRGGANVLTFDSPRARTCLHHAAYYGHAECLQAILGAAAQAQGPVAASWGFARFVNVRDERGATPLHLAARHARASCVRLLLDKGAIVSAPTAVYGFPGSTALHLAARAGSMECIRELLAWGADRLQRDSAGRIAYAVAMRRGHRACAALLNPAAAEPIVWPSPLKFIGELEADAKALLEAALMEANREREKRILHGSDINIKGGDEEEESEDEEEACNIC... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 47701
Sequence Length: 446
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q6NLQ8 | MRFLSLVGNSFGCSASGERLVSAARDGDLQEAKALLDYNPRLARYSTFGVRNSPLHYSAAQGHHEIVSLLVESGVDINLRNYRGQTALMQACQHGHWEVVLILILFGANIHRSDYLNGGTALHLAALNGHPRCIRILLSEYIPSVPNCWSLLKNKKTSVAGFDSSVLHEVINRAADGGITPLHVAALNGHIETVQLLLDLGASVTQVTVEDGTTIDLIGAGSTALHYASCGGNTQCCQLLISKGACLAAVNSNGWTPMMVARSWHRNWLEEILNPTTEQPQLHLPNVPSPFLCLPLMSIVNIAQECGWRENDCLTPCRDP... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of ACC synthases (ACS). Negatively regulates ethylene biosynthesis probably via ubiquitin-dependent degradation of ACS4 and ACS7 enzymes. Regulates lateral root formation and development by controlling ethylene production which inhibits lateral root for... |
Q6KAE5 | MGFLSLVGNSFGCSASGERLVSAARDGDLQEARALLEYNPRLARYSTFGGRNSPLHYAAAQGHHEIVSLLLESGVEINLRNYRGQTALMQACQYGHWEVVQTLMLFNANVHRTDYLNGGSALHFAALHGHARCLRLVLADYVPSMPNFWNSMKDSLSEEGPSADLDEDGLFKMVNQKADGGLTPLHMAALNGHVECVQLLLDLGASVIEATIEDGTTIDLIGAGSTPLHYAACGGNAVCCQLLIARGASLSAQNASGWTPLMVARSWHRNSLEEILSKEPESRIRTVPSPYLCLPLMSIMSIAREFGWRYLNQSPVCIDP... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53617
Sequence Length: 496
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4FE45 | MGNSFGCSASGERLVSAARDGDFVEAKMLLDCNPCLAKYSTFGGLNSPLHFAAAKGHNEIVGLLLENGADVNSRNYCGQTALMQACRYGHWEVVQTLLLFRCNVTRADYLAGRTALHFAAVNGHARCIRLVLADFLPSDKLNSLPETGVVTAKNKSEQSALSKFVNKAADGGITALHMAALNGLFDCVQLLLDLEANVSAVTFHYGTSMDMIGAGSTPLHYAACGGNLKCCQILLARGARKMTLNCNGWLPIDIARMWSRHWLEPLLSPNSDVVIPAFPHSNYLSLPLLSILNIAREFGLQSATIGDEVDICAVCLERTC... | Function: Possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence ... |
Q9FPH0 | MGQQQSQSKDEMLFQEVSNNNVEGIKSLHHEGAGLEGVDKLGRTPLILACTNDDLYDVAKTLLELGSNVNAYRSGCNGGTPLHHAAKRGLVHTVKLLLSHGANPLVLDDDVKTALEVARDEGYSNVVRAIESHICLFSGCMREYSGSSLLNLFAPQLLSRKVWVVVVPTGSRNPTKPLKLELVLYDSIQDAQPRMVIPLWKANLEEPKSFRCDDSVMIIDDSRSPKSMRQRRESGFISQARRWAQVDRQIRLKLAAEIKGDMKQMNWFSEACKGVPQPMNPPRFMKTSQATTTTTNVPALSDDALTRVAMSLPSPKTANK... | Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequenc... |
Q7XI08 | MGLQQSKEELVYQQVNYGNADGIRALRAQGAGLEWIDKEGKTPLMVASMRPDLINVVQVLIELGANVNAYRPGSYCGTALHHAAKKGLEQTVHLLLSHGANPFITNDDCHTALDLAREKGHVNVVRAIEGRISLFCGWMRENYGPGFLEAFAPQFLTRKIWAVILPREARNQTRPLKLELTIYPELQASKPQAVIKLWKCQLEEPKFNQANPSVTIFDKGTRTRYKLLPVCEGDKQQLQWFYSACCGIPQVASMVPAQPANAPLPNPSSASSLPSVISTPSKEDAELAMAINASILSAIAEGVPDVQPITTTTATNDWGN... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54729
Sequence Length: 513
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4FE47 | MGQQQSKGELLYQQVSYGNSEGIRALHRDGGDLEWMDREGKTPLILACMNSELFDVAKTLIELGSNVNAYRPGRHAGTPLHHAAKRGLENTVKLLLSHGANPLVLNDDCQTPLEVARVKGFSNVVRAIEKHICLFSGWMREFYGPTFLDLFAPQLLSRRVWVVIVPTGSRNPTKPFKLELVVYASLQDAQPRTVMPLWKANLEEPKAKQSDTSVMIVDNSTIPSRRMKKRRVCASHGRRRPQVVRQTRLKFAPSTEGDSQQLKWFCDACKGIPQPMHPPVFLQAPPSAPPPPSEDGLAMGMNASLHTTMSDPSNLNHHSI... | Function: No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequenc... |
Q7EZ44 | MGLLGMVGDSFGCSATGERLVSAARDGDIQEAMALLELNPRLARYSTFGIRNSPLHYSAAKGHHEIVSLLIESGVDINLRNCRGQTALMQACLYGHWKVVQILVLFKANIHKKDCFSGATAIHFAALKGHTRCLRLLVADYVPSLPEFWSVMHAKCTDETNKEAFDAVALRRLINNKSDGGVTPLHLAALHGHAECVQLLLDLGASVSEVTINDGSTIDLIGSGSTPLHYAACGGSAVCCQLLVAAGANMRAQNTNGLTPLMVARSWHKSSVEGILTKRSEVPVRILPSSYLSLPLMSIVKIARECGWRKTSVSSVCHDP... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53082
Sequence Length: 495
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q4JHE0 | MGNSLGCVGLGERLAAAAKDGDAAEAQRLLAANPGLARCTTFGNLNSPLHVAAAKGHHEIAALLLENGADVNARNIYGQTPLMQACRFGHWEVVQTLLVFRCNVWRVENLSGRTALHMAAAGGHVKCVRLLVADAAGDRDGYVNKAANGGVTALHLAALHGHVECVHLLIDERASLAAQTLPCAAPPMASIGAGSTPLHYAACGGEVKCCQILVSRGADRTAINCNGWLPIDAARIWGCNWLEHVLSPKSHLPIPKFPPSGYLSQPLPSLIAIAREQGLNLSSEVSDGFDEGADACAVCLERPCTVAAEGCDHELCVKCA... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 43457
Sequence Length: 420
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q65XV2 | MGHGVSCARTGDEHDFFRAAQLGDLDALAALLAADPSLARRATLYDRLSVLHIAAANGRIEVLSMFLDRGAPPDAVNRHKQTPLMLAAMHGKIDCVLKLLQADANILMFDSVHARTCLHHAAYYGHVDCLQAILAAAQTTPVADSWGFARFVNVRDDHGATPLHLAARQGRPGCVQVLLENGAIVSALTGSYGFPGSTSLHLAARSGNLDCIRKLLAWGADRLQRDSAGRIPYSVALKRNHGACAALLNPTSAEPMVWPSPLKFISELEPEAKALLEAALMEANREREKKILNGTKYSLPSPSPGDDSADDDACSEVSDT... | Function: E3 ubiquitin-protein ligase required for full accumulation of the LRR receptor kinase XA21 and XA21-mediated disease resistance. Binding to XA21 may stabilize the receptor kinase and maintain its protein level. Autoubiquitinated in vitro.
PTM: Phosphorylated by XA21.
Catalytic Activity: S-ubiquitinyl-[E2 ubiq... |
G5EE07 | MSNYPKRIYVLPARHVAAPQPQRMAPKRALPTEQVVAQLLGDDMGPSGPRKRERLNHLSQEEKMDRRKLKNRVAAQNARDKKKERSAKIEDVMRDLVEENRRLRAENERLRRQNKNLMNQQNESVMYMEENNENLMNSNDACIYQNVVYEEEVVGEVAPVVVVGGEDRRAFESAAFINEPQQWEQARSTSINNNISNQLRRMDSKKNNTISVDMYLTIISILCNHMDRNKKMDTSNKSSNISRAQAESSIDSLLATLRKEQTVMQRLVQADPCTHLQKRVKHFRRIP | Function: Required for transcriptional regulation of the unfolded protein response (UPR) in the endoplasmic reticulum (ER) under stressed conditions, acting downstream of ire-1, and also maintaining ER homeostasis via a negative feedback loop, in parallel with ER kinase pek-1 . May also regulate Golgi protein trafficki... |
P17861 | MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAFWTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQWGRHQPSWKPLMN | Function: Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity).... |
Q5BG78 | MKLLALSLASLASAATITRRADFCGQWDTATAGNFIVYNNLWGQDNADSGSQCTGVDSANGNSVSWHTTWSWSGGSSSVKSYANAAYQFTATQLSSLSSIPSTWEWQYSTTDVVANVAYDLFTSSSIGGDSEYEIMIWLAALGGAGPISSTGSSIATVTLGGVTWNLYSGPNGSMQVYSFVASSTTESFSADLMDFINYLVENQGLSNSQYLTHVQAGTEPFTGSDATLTVSSYSVSVS | Function: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components. Active against tamarind xyloglucan.
Catalytic Activity: xyloglucan + H2O = xyloglucan oligosacc... |
Q4WBT4 | MLYPRNLALFSLLSLSSAAPSQVERSPDAVLKPRAVCTPTAGGSPSIDDVPAIRKAIASCGNGGTIVFPAGSTYYLNSVLDLAGCSNCDIQVEGVLKFSGSTEYWGGKTAMLNIDMINGLRLRSLTGSGVIDGNGQNAYDRFASDKNYKRPTLLYITGGSNIEVSGLRQKNPPNVFNSVKGDTQHVTFKNLRMDATSNSQNPPKNTDGFDIGASTHVTISSVSVTNDDDCVAFKPGSNYVTVEDVTCTGSHGISVGSLGKSGPDVVQNILAHRITMIESTKAAGIKTYPSGNGHGLSTVKNVTFSDFNVRGCDYAFQIES... | Function: Pectinolytic enzyme involved in the degradation of xylogalacturonan (xga), a galacturonan backbone heavily substituted with xylose, and which is one important component of the hairy regions of pectin. Activity requires a galacturonic acid backbone substituted with xylose (By similarity).
Sequence Mass (Da): 4... |
A0KNR2 | MPKKFYVSWDNLQREARRLARRQLPVSQWKGIIAVSRGGLVPAALMARELGIRNVETLCISSYDHNNQRDLVVVKAATTAGDGEGWLVVEDLVDTGTTAKAIRELYPKAKFIAIFAKPMGEQLLDDFEVAIPQDTWIEQPWDMALEFATPICDEE | Function: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosph... |
P55808 | MESWWGLPCLAFLCFLMHARGQRDFDLADALDDPEPTKKPNSDIYPKPKPPYYPQPENPDSGGNIYPRPKPRPQPQPGNSGNSGGYFNDVDRDDGRYPPRPRPRPPAGGGGGGYSSYGNSDNTHGGDHHSTYGNPEGNMVAKIVSPIVSVVVVTLLGAAASYFKLNNRRNCFRTHEPENV | PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 19723
Sequence Length: 180
Subcellular Location: Cell membrane
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P39798 | MQQEADVNVFQQDLADMKGEHKALEQRVSALERVSDRQDQQIMTLNEKLNKIEENTTWIKRTITGAIITAVSTGIIGGAIAIMYSLLQH | Function: Associated with cell lysis upon induction of PbsX.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9997
Sequence Length: 89
Subcellular Location: Cell membrane
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Q99163 | MNTFDKGTVIRTVLLLIALINQTMLMLGKSPLDIQEEQVNQLADALYSAGSIAFTIGTTLAAWFKNNYVTEKGKKQRDLLRDNNLTK | Function: Involved in cell lysis upon induction of PbsX.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9731
Sequence Length: 87
Subcellular Location: Membrane
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P98170 | MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQH... | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis . Acts as a direct caspase inhibitor . Directly bind to the active site ... |
Q60989 | MTFNSFEGTRTFVLADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAIDRWQYGDSAVGRHRRISPNCRFINGFYFENGAAQSTNPGIQNGQYKSENCVGNRNPFAPDRPPETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKSFQNWPDYAHLTPRELASAGLYYTGADDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYEARIVTFGTWTSSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHA... | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis (By similarity). Acts as a direct caspase inhibitor (By similarity). Dir... |
A5D8Q0 | MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAK... | Function: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that... |
D0U690 | MPSTALSPPSRPPAQSYDSYSSSLSPSSPRFHAAAGSHGRRSPSPSRLESLLDGPHVPPRSPSRKIRSALSRHIRPHITPRTLTPVFLWTLALWLIHHFLFPLSSPFAKLAKPKAEEHFLSTTFPPPAQRLGDDRLDSVDPRWRAYHPLPAPEPPFPRLRPTRFLPPQCLEQWFAEGETLCGAKEMGEEETLDATWLWVNGSDHRWRDSMVEWREKENVNSPERHYREQNELVHSMRSVLDALPGHLRTFHLILADYPFNYPEDLELVPSSIIPDLEVAASKSKGRRHPRELPGAPASLANLTERVTPESISPTLASHLQ... | Function: Xylosylphosphotransferase that is specific for UDP-xylose as a donor and mannose as an acceptor to form a xylose-alpha-1-phosphate-6-mannose linkage. Functions in the O-glycosylation of proteins en route through the secretory pathway.
Catalytic Activity: 3-alpha-D-mannopyranosyl-alpha-D-mannopyranose + UDP-al... |
A7GCI1 | MKLLEDKILKEGILLEGNILKVDSFLNHQMDVKLFNEIGKEFKRRFEGCNINKILTIEASGIGIATIVSQYFDFCPVVFAKKVDAANMDKDTYESKVHSFTKNKTYNVRVSKKYINKGDKILLIDDFLANGCAALGLIDIIKQGGAELAGVGIAIEKGFQKGRKELEKVGAKVESLAILDKIENDKVYFK | Function: Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Catalytic Activity: diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
Sequence Mass (Da): 21225
Sequence Length: 190
Pathway: Purin... |
Q5AY46 | MLKHSSAATKENDSPKLKVLDIVSKLEPSLDHSHTHWWKLTSPQLALMLEAADYSIEKQFETLLFHYHWVVPYLGPKPDADGNFKWRSLVSDVGIPLEYSWKWDTATSGPDVRLTIEPINELSGTRVDPLNQAPSLELLHRLAEILPRLDVSWASHFLSTFYDHDKLKYIKESESETGMPLRSTMLVCFEFGRNGITTKTYMSPRKLGQQGFAPLSDYHSAIAALGPSCALDAVTEFLNNSPEGPHLSPFMLAVDNIIPCSSRLKLYFATPRTSYNSIREVLTLGGRLSTVTLESKLRAIHELVKAIMPFPPDLPDDADI... | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the ... |
P0DP82 | MATDGMVLHKRSLSEGGTSTQAWKVLSQTLPSRGPDVDAWWQLTGRHLAVLLDAAAYPIEKQYECLLYHYHYAAPYLGPAPREGASPPTWKSMLQLDGTPFEFSWKWNNPGGEPDVRFGLEPIGPMAGTSLDPLNHLAMREILYKLSSAVPGSDLTWTHHFLATLFDHDYAKYTQKAATMGSSIGTSLVYSLEFQRKSTGLKTYFHPRKLDQQAFLDIPSWEASFRGLHPNSPSRTAVHEFLSTNPEGKLLKPFCLSVDNCSPAKARIKWYFNSPHTNFRAIREIMTLGGRIADTETRTKQFSELFNLLKTVTEEHADFP... | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the ... |
Q5AUN2 | MAKLSVILLFRSLLLCGALTVSRHATLVTEREVQSSKYDFIVVGGGVSGLTVADRLTEIPDVSVLVIEAGPVDRGEDFVYVPGSYERDPYIWPGLTNEPSAELNNRVFDSVVARVAGGGSIVNAMIFLRGTALDFDGWESLGNHGWGWEGMLPYFIKSENFTRPTPELAHEGNITWDDSVRGHDGPVRYSYPNYIYPGLGRLYEAALHIGIQPRLDPNGGQNTGVFNQPFAIDAATWTRSSARRNHYDPAVSRPNYHFLSDTTVARVIFDGTRAVGVEYLPSRGGGISTAFAAKEVLVAAGALHTPQVLQLSGVGPRDLL... | Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone . Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the ... |
Q5BGA7 | MSPPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYEAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKRSDLFIVSKLWNSFHDGERVEPIARKQLSDWGIDYFDLYIVHFPVSLKYVDPEVRYPPGWENAEGKVELGKATIQETWTAMESLVDKGLARSIGISNFSAQLLLDLLRYARIRPATLQIEHHPYLTQERLVTFAQREGIAVTAYSSFGPLSFLELSVKQAEGAPPLFEHPVIKDIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPARLLQNLDVVGFDLEDGELKAISDLDKGLRFNDPPNYGLPITIF | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-p... |
Q876L8 | MASPTLKLNSGYDMPQVGFGLWKVDNAVCADTVYNAIKAGYRLFDGACDYGNEKECGEGVARAIKDGLVKREDLFIVSKLWQTFHDEDKVEPITRRQLADWQIDYFDLFLVHFPAALEYVDPSVRYPPGWFYDGKSEVRWSKTTTLQQTWGAMERLVDKGLARSIGVSNYQAQSVYDALIYARIKPATLQIEHHPYLQQPDLVSLAQTEGIVVTAYSSFGPTGFMELDMPRAKSVAPLMDSPVIKALADKHRRTPAQVLLRWATQRGIAVIPKTSRPEVMAQNLDNTSFDLDSEDLAKIADMDLNIRFNKPTNYFSANKL... | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-p... |
P86450 | GVQRYTFDAVVSQQDTILSGLDLDCGSYLGYTSPLQGLTAFVPTS | Function: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity).
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence ... |
A5JTQ2 | ANTKNREPKVSSVFLCFSIFYVTVLLNCNHVYGQTSTVFACDVAKNTNVSSYGFCDNSLSVEDRVSDLVKRLTLQEKIGNLGNSAVEVSRLGIPKYEWWSEALHGVSNIGPGTHFSSLVPGATNFPMPILTAASFNTSLFQAIGSVVSNEARAMYNVGLAGLTYWSPNINIFRDPRWGRGQETPGEDPLLSSKYAAGYVKGLQQTDDGDSDKLKVAACCKHYTAYDVDNWKGVQRYTFDAVVSQQDLDDTFQPPFKSCVIDGNVASVMCSYNKVNGKPTCADPDLLKGVIRGKWKLNGYIVSDCDSVEVLYKDQHYTKTP... | Function: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls. Does not cleave xylan from oat spelts although xylan from oat spelts was degraded to xylose when this enzyme was used in combination with xylanase. Als... |
A1CFY8 | MATSSTTPQNLSFVLEGIHQVKFEDRPIPELRDPHDVIVNVKYTGICGSDVHYWEHGAIGHFVVKDPMVLGHESSGVVAKVGSAVTSLKVGDRVAMEPGVPCRRCEPCKAGKYNLCEKMAFAATPPYDGTLAKYYPLPEDFCYKLPENISLQEGALMEPLGVAVHITRQASIKPGESVVVFGAGPVGLLCCAVARAFGASKIIAVDIQKTRLDFAKKYAATAIFEPAKVSAVANADQMREENDLGPGADVVIDASGAEPSVHTGIHVLRPGGTYVQGGMGRNEINFPIMAACTKELTIKGSFRYGSGDYKLAVDLVASGK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Xylitol dehydrogenase which catalyzes the conversion of xylitol to D-xylulose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, t... |
P27156 | MSAAEGPLVVGVDTSTQSTKALVVDVATGRVVASGQAPHTVTSGAGRESDPRQWWDALCEALRQCGEAAHEAAAVSIGGQQHGLVTLDGHGEPVRPALLWNDVRSAPQGHRLIEELGGAKFWAERTGSVPAASFTVTKWAWLAEHEPEAVRATRAVRLPHDYLTERLTGQGTTDRGDASGTGWWASGTEAYDEEILGHVGLDPALLPRVVRPGEVAGTVRDSHELPFSKGTLVACGTGDNAAAALGLGVRPGTPVMSLGTSGTVYAVTQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVAALLGLDREAVEPGH... | Function: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Catalytic Activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+)
Sequence Mass (Da): 49822
Sequence Length: 481
EC: 2.7.1.17
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Q9A9Z1 | MTAQVTCVWDLKATLGEGPIWHGDTLWFVDIKQRKIHNYHPATGERFSFDAPDQVTFLAPIVGATGFVVGLKTGIHRFHPATGFSLLLEVEDAALNNRPNDATVDAQGRLWFGTMHDGEENNSGSLYRMDLTGVARMDRDICITNGPCVSPDGKTFYHTDTLEKTIYAFDLAEDGLLSNKRVFVQFALGDDVYPDGSVVDSEGYLWTALWGGFGAVRFSPQGDAVTRIELPAPNVTKPCFGGPDLKTLYFTTARKGLSDETLAQYPLAGGVFAVPVDVAGQPQHEVRLV | Cofactor: Binds 1 Fe(2+) per subunit.
Function: Involved in the degradation of D-xylose . Catalyzes the hydrolysis of D-xylonolactone to D-xylonate .
Catalytic Activity: D-xylono-1,5-lactone + H2O = D-xylonate + H(+)
Sequence Mass (Da): 31586
Sequence Length: 289
EC: 3.1.1.110
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Q8U7Y1 | MKALVLEEKGKLSLRDFDIPGGAGSGELGPKDVRIRTHTVGICGSDVHYYTHGKIGHFVVNAPMVLGHEASGTVIETGSDVTHLKIGDRVCMEPGIPDPTSRASKLGIYNVDPAVRFWATPPIHGCLTPEVIHPAAFTYKLPDNVSFAEGAMVEPFAIGMQAALRARIQPGDIAVVTGAGPIGMMVALAALAGGCAKVIVADLAQPKLDIIAAYDGIETINIRERNLAEAVSAATDGWGCDIVFECSGAAPAILGMAKLARPGGAIVLVGMPVDPVPVDIVGLQAKELRVETVFRYANVYDRAVALIASGKVDLKPLISA... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: NAD(+) + xylitol = D-xylulose + H(+) + NADH
Sequence Mass (Da): 36776
Sequence Length: 350
EC: 1.1.1.9
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Q9A9Z2 | MRSALSNRTPRRFRSRDWFDNPDHIDMTALYLERFMNYGITPEELRSGKPIIGIAQTGSDISPCNRIHLDLVQRVRDGIRDAGGIPMEFPVHPIFENCRRPTAALDRNLSYLGLVETLHGYPIDAVVLTTGCDKTTPAGIMAATTVNIPAIVLSGGPMLDGWHENELVGSGTVIWRSRRKLAAGEITEEEFIDRAASSAPSAGHCNTMGTASTMNAVAEALGLSLTGCAAIPAPYRERGQMAYKTGQRIVDLAYDDVKPLDILTKQAFENAIALVAAAGGSTNAQPHIVAMARHAGVEITADDWRAAYDIPLIVNMQPAG... | Function: Catalyzes the dehydration of D-xylonate to 2-dehydro-3-deoxy-D-arabinonate during D-xylose degradation. Can also dehydrate D-gluconate, with similar catalytic efficiency. Has weak activity with D-galactonate, D-fuconate and L-arabinonate.
Catalytic Activity: D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
... |
Q59545 | MIMKALVLEKAGKIAIQDWQSNEVLGDDDVEIKIHTVGICGSDVHYYQHGRIGPFVVDEPMVLGHEASGVITAAGKNVKHLKVGDRVCMEPGIPDLQSPQSRAGIYNLDPAVRFWATPPIDGCLRESVIHPAAFTFKLPDNVSFAQGAMVEPLAIGMQSATKAGIKPGDIGLVIGAGTIGIITQSALAGGCSDVIICDVFDEKLKVAEKYQGLHAVNSKDQQALADKVRELTGGEGVNVLFECSGAKPVIASISDHIAPGGTAVLVGMPIDPAPLDIVAAQAKEVTFKTILRYANMYPRTIRLLSSGKLNVAPLLSATYK... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: NAD(+) + xylitol = D-xylulose + H(+) + NADH
Sequence Mass (Da): 35952
Sequence Length: 338
EC: 1.1.1.9
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P06622 | MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNERFMTVLT | Catalytic Activity: catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H(+)
Sequence Mass (Da): 35156
Sequence Length: 307
Pathway: Xenobiotic degradation; toluene degradation.
EC: 1.13.11.2
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P0AGF5 | MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTII... | Function: Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Catalytic Activity: D-xylose(in) + H(+)(in) = D-xylose(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53608
Sequence Length: 491
Subcellular Location: ... |
P23106 | MNAPQQSPEIGREILAAGYRTNLHDQGEGFPALLIHGSGPASPPGPTGAGSFRSSQTRRVIAPDMLGFGYSERPADGKYSQARWVEHAIGVLDALGIQQGDIVGNSFGGGLALALAIRHPERVRRLVLMGSVGVSFPITAGLETAWGYTPSLANMRRLLDLFAHDRTLVNDELAELRYQASIRPGFQESFAAMFPPPRQNGVDDLASNETDIRALPNETLVIHGREDRIIPLQASLTLAQWIPNAQLHVFGQCGHWTQIEHAERFARLVENFLAEADALHS | Function: Catalyzes the conversion of 2-hydroxymuconate semialdehyde to 2-hydroxypent-2,4-dienoate.
Catalytic Activity: (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = 2-oxopent-4-enoate + formate + H(+)
Sequence Mass (Da): 30598
Sequence Length: 281
Pathway: Aromatic compound metabolism; benzoate degradation via hydr... |
Q4J710 | MAKSKDEIKEEIAKAIINQVSKTDLSRRRALSTLAKGGIIAGVLAAFGAGFGSGYVTAPKGSSSSGVAPPQPGFMYGQVPEHPTWKIVFINHVTTNPFFVPTQYGIQDACLLLDCNYQWTGSETSDTTTMVNDMEAAISQGANGIAVSVISPNAFDKPTQDALNAGIPVFAYNAYIPTDDPSYSQYHNPPYLGYIGQSLYASGQLFGQRILNLVPSGSRVALFIATPGTANIQPRIDGIQSVIEGHYTIDVVATGALVSDEQSAIESYFNSHPDVKGMFAVDAGSTQGVGNVLREHGIKTVSNGGTIAAGGYDLLPATIQ... | Function: Part of the ABC transporter complex XylFGH involved in the uptake of xylose and arabinose.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42695
Sequence Length: 402
Subcellular Location: Cell membrane
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Q2YJE7 | MSEYLLEMRNIGKEFNGVKALDGIYLKVRAGECVGLCGENGAGKSTLMKVLSGVYPHGTWTGEIFWEGKELKASGIRDTEAAGIVIIHQELMMVPHLSVAENIFLGCEPTTGGFIDYDQMNARAAELLARLKINDINVALPVYHYSGGKQQLIEIAKAINKNAKLLILDEPTSALTASETRVLIDLIKDFKKQGMACVYISHKLDEVAEISDTVTVIRDGAHIATRPMSELTTPDIITMMVGREMKNLFPREPHDIGEVMFEARNISCWDVTNPGRKVVDDVSFALRRGEILGIAGLVGAGRTELVSSLFGVWPGACQGQ... | Function: Part of the ABC transporter complex XylFGH involved in xylose import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-xylose(out) + H2O = ADP + D-xylose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55814
Sequence Length: 511
Sub... |
D7EZJ3 | MHDAPAQRKRRRPGRIGPLPRSSRFARLKLLIASACAALLATLALPPGAAHAQTVTSNQTGNHNGYFYSFWTDAPGTVSATMGSGGNYSTSWRNTGNFVIGKGWSTGGRRTVTYSGSFNPSGNAYLTLYGWSRNPLVEYYIVDNWGTYRPTGTFKGTVTTDGGTYDIYQTTRYNAPSIEGNKTFNQYWSVRQQKRTGGTITTGNHFDAWARAGMQLGSHDYMIMATEGYQSSGSSNITVGGTSGGGGGGGGGGGCTATLSAGERWDDRYNLNVSVSGSSNWTVTMNVPSPATILSTWNITATWPSSQVLVARPNGSGNNF... | Function: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and birchwood xylan, releasing xylobiose and xylotriose as the major products.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in... |
Q8J0K5 | MGISSILLSALIAGGALALPAAEPVSFDIRDENITLARRAEAINYNQDYIASGANVQYSPNMAAGSFSINYNTQGDFVVGLGWQPGDANPITYSGSFSASGVGILAVYGWSTNPLVEYYVMEVHDGYQTAGTHKGTVTTDGGTYDIWEHQQVNQPSILGTSTFNQYISIRQSPRTSGTVTVQNHFNAWAQAGMNLGTLNYQVMAVESWSGSGSGQISLSKGTGGGSTTTTPTGPTSTSTAPSSGGTGAAQWGQCGGIGWTGPTTCVAPYTCKYENAYYSQCQ | Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence ... |
P36906 | MIKVRVPDFSDKKFSDRWRYCVGTGRLGLALQKEYIETLKYVKENIDFKYIRGHGLLCDDVGIYREDVVGDEVKPFYNFTYIDRIFDSFLEIGIRPFVEIGFMPKKLASGTQTVFYWEGNVTPPKDYEKWSDLVKAVLHHFISRYGIEEVLKWPFEIWNEPNLKEFWKDADEKEYFKLYKVTAKAIKEVNENLKVGGPAICGGADYWIEDFLNFCYEENVPVDFVSRHATTSKQGEYTPHLIYQEIMPSEYMLNEFKTVREIIKNSHFPNLPFHITEYNTSYSPQNPVHDTPFNAAYIARILSEGGDYVDSFSYWTFSDV... | Function: Has hydrolytic activity towards xylopentaose, xylotriose, xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity toward xylan.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence Mass (Da): 58606
Sequence Length... |
Q45070 | MIPRIKKTICVLLVCFTMLSVMLGPGATEVLAASDVTVNVSAEKQVIRGFGGMNHPAWAGDLTAAQRETAFGNGQNQLGFSILRIHVDENRNNWYKEVETAKSAVKHGAIVFASPWNPPSDMVETFNRNGDTSAKRLKYNKYAAYAQHLNDFVTFMKNNGVNLYAISVQNEPDYAHEWTWWTPQEILRFMRENAGSINARVIAPESFQYLKNLSDPILNDPQALANMDILGTHLYGTQVSQFPYPLFKQKGAGKDLWMTEVYYPNSDTNSADRWPEALDVSQHIHNAMVEGDFQAYVWWYIRRSYGPMKEDGTISKRGYN... | Function: Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xyl... |
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