ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P42293 | MFNRLFRVCFLAALIMAFTLPNSVYAQKPIFKEVSVHDPSIIETNGTFYVFGSHLASAKSNDLMQWQQLTTSVSNDNPLIPNVYEELKETFEWAQSDTLWAADVTQLADGKYYMYYNACRGDSPRSAMGVAVADNIEGPYKNKGIFLKSGMEGTSSDGTPYDATKHPNVVDPHTFFDKDGKLWMVYGSYSGGIFILEMNPKTGFPLPGQGYGKKLLGGNHSRIEGPYVLYNPDTQYYYLYLSYGGLDATGGYNIRVARSKKPDGPYYDAEGNPMLDVRGKGGTFFDDRSIEPYGVKLMGSYTFETENEKGTGYVSPGHNS... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose.... |
A5IKD4 | MRFLFLMITLTALTGYILADEQPTFRWAVVHDPSIIKVGNMYYVFGTHLQVAKSKDLMHWEQINTSAHDKNPIIPNINEELKETLSWARTRNDIWAPQVIQLSDGRYYMYYCASTFGSPRSAIGIAVSDDIEGPYKHYAVIVKSGQVYSVDGPSEDGTPYDSRKHPNALDPGVFYDKEGNLWMVYGSWFGGIYILKLDPNTGLPLPGQGYGKRLVGGNHSSMEGPYILYSPDTDYYYLFLSFGGLDYRGGYNIRVARSKNPNGPYYDPEGKSMENCMGSKTVISNYGAKLVGNFILSESNTIDFKAFGYVSPGHNSAYYD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and... |
P0C6Z0 | METTQTLRFKTKALAVLSKCYDHAQTHLKGGVLQVNLLSVNYGGPRLAAVANAGTAGLISFEVSPDAVAEWQNHQSPEEAPAAVSFRNLAYGRTCVLGKELFGSAVEQASLQFYKRPQGGSRPEFVKLTMEYDDKVSKSHHTCALMPYMPPASDRLRNEQMIGQVLLMPKTASSLQKWARQQGSGGVKVTLNPDLYVTTYTSGEACLTLDYKPLSVGPYEAFTGPVAKAQDVGAVEAHVVCSVAADSLAAALSLCRIPAVSVPILRFYRSGIIAVVAGLLTSAGDLPLDLSVILFNHASEEAAASTASEPEDKSPRVQPL... | Function: Acts as a DNA polymerase processivity factor; a transcriptional activator for several EBV promoters and inhibits the host DNA damage response (DDR) to double-stranded DNA breaks. Plays an essential role in the viral lytic DNA replication by acting as a polymerase accessory subunit. Stimulates the viral DNA po... |
P52869 | ITEIKADKTTAVANGKDAVTYTVKVMKDGKPLSGEEVTFTTTLGTLSKSTEKTNTNGYRKVSLTSANQGKSLVSASVTMPQLMLKLLEVEFFTQLTIDNGNVEIVGTGAKGKLPNVWLQYGQVNLKANGGNGKYTWYSANPAIASVDPSSGQVTLKDKGETTITVVSGDKQTAIYTIAMPNSIVSVNSSGRVDYNTANNICKNIKGSLPSSIKELKDLYDDWGAANKYQHYSQESITAWTLQTSENKVQGVASTYDLVRKNPLIDKVDIAGNYAYAVCVK | Function: Necessary for the production of attaching and effacing lesions on tissue culture cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30146
Sequence Length: 280
Subcellular Location: Cell outer membrane
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D9XD61 | MPQDVRFDLPFETPVSKHLESARARHLRWVWEMRLVHSREGFEEYRSWDLPQAAARTYPHASADDMVVLMNWFSLAFLFDDQFDASRPDRADRIAEVARELIVTPLRPAGTPPRVACPITLAWTEVWKHLSHGMSLTWQSRFAASWGRFLEAHCEEVDLAARGLEGTLGLVEFTEFRRRTVGIHHSIDAGERSRGFEVPAQAMAHPVMERMRDLAADTIGFMNDIHSFEREKRRGDGHNLIAVLRRERGCSWQEATDEAYRMTIARLDEYLELQERVPQMCDELRLDEAQRDGVRLGVEAIQHWINGNYEWALTSGRYAA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpenol 7-epi-alpha-eudesmol via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation . The only accepted ... |
P43261 | MITHGCYTRTRHKHKLKKTLIMLSAGLGLFFYVNQNSFANGENYFKLGSDSKLLTHDSYQNRLFYTLKTGETVADLSKSQDINLSTIWSLNKHLYSSESEMMKAAPGQQIILPLKKLPFEYSALPLLGSAPLVAAGGVAGHTNKLTKMSPDVTKSNMTDDKALNYAAQQAASLGSQLQSRSLNGDYAKDTALGIAGNQASSQLQAWLQHYGTAEVNLQSGNNFDGSSLDFLLPFYDSEKMLAFGQVGARYIDSRFTANLGAGQRFFLPANMLGYNVFIDQDFSGDNTRLGIGGEYWRDYFKSSVNGYFRMSGWHESYNKK... | Function: Necessary for the production of attaching and effacing lesions on tissue culture cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 101836
Sequence Length: 934
Subcellular Location: Cell outer membrane
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A0QNJ0 | MAGFRLTTKVQVSGWRFLLRRVEHAIVRRDTRMFDDPLQFYSRAVFAGVVVSVLICLGAALMAYFKPLGKQGSDQLLVDRTTNQLYVMLPGSNQLRPVYNLTSARLVLGNASNPVAVKSEELNRISKGQSIGIPGAPYATPTGTPASQWTLCDTVAKPDSSAPKVETSILIRTLAIDSGVGPIRADQGMLVSYEGANWLITEGGRHSIDLADRAVTSAVGIPVTAKPTPISQGLFNALPNRGPWQLPQIPAAGAPNSVGLPENLVIGSVFRTATESDPQHYVVLPDGVARVNNTTAAALRATNSYGLMQPPAVEASVVAK... | Function: An ATPase (shown for residues 72-479) . Part of the ESX-1 / type VII specialized secretion system (T7SS), which exports several proteins including EsxA and EsxB . Plays a role in DNA conjugation, in both donor and recipient strains .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51022
Se... |
Q8R7Y5 | MPIKVENVSFIYNEGTPYATVALKDINFSIDDEEFVGIIGHTGSGKSTLIQQLNGLLKPSKGKIYINGIDITDKKVSLKDIRKQVGLVFQYPEYQLFEETVFKDIAFGPSNLGLSEEEVKERVYEAMEIVGISKELADKSPFELSGGQKRRVAIAGILAMRPKILILDEPTAGLDPKGKQEILNKIKEIHDKYKMITILVSHNMEDIARIADKIIVMNRGKIELIGTPREVFREAERLEKIGLSVPQITSLARELRKRGVPIPPDVLTIEEAKEHILRYLRGTKNV | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32136
Sequence Length... |
Q97EK9 | MPIKIENLTYTYMPGTPFEKKALDNVNITIEDGEFAVFIGHTGSGKSTLIQQINGLLKPTSGSIFIDDVDITDKSVKLNDIRKKVGLVFQYPEYQLFEETIEKDIAFGPRNMGLSEEEVSTRVKKAMKMVGLEYNDFKDKSPFELSGGQKRRVAIAGVVAMEPKVLILDEPTAGLDPKGRDDILYEIKKLQKEYKMTIILVSHSMEDVAKVADKIFVMYDSRCILSGNLDEVFNEIDTLEKVGLAVPKVTYLVRKLREKGFDISKDIFTIEAAKKEILRVLESAKR | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32239
Sequence Length... |
A0PXX8 | MSIEIKNLTHIYMPGSPFERKALDNVNISIEDGEFVALIGHTGSGKSTLIQHINGLLKASSGNIIIDGVDITSEKVKLSEIRKKVGLVFQYPEYQLFEETIEKDIAFGPKNLGLNDEQVSKRVKKAMNIVGLDYDVYKDKSPFDLSGGQKRRVAIAGVVAMEPKVLILDEPAAGLDPKGREDILEKVKQLKEEYNMTIILVSHSMEDVAKIAERVLVMDKGRCILDGTIKEVFNEVDILESVGLAVPQVTYLVRALKSKEFNIPEDIFTIEEAKNEILKLIRGANKHD | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32062
Sequence Length... |
Q0TMS8 | MSIKIENLNHIYMPKTPFEKIALNNINCEIEDGEFVALIGHTGSGKSTFIQHLNGLLSPTSGNIIVDGVNIADKKVKLSDIRKKVGLVFQYPEYQLFEETIEKDIEYGPRNLGISEEEISKRVKKSMEMVGLDYETYKDKSPFDLSGGQKRRVAIAGVIAMEPKVLILDEPTAGLDPKGREDILAQIRLLHKEYGMTIIMVSHSMEDVAKIADRVIVMNSGEIVLDGKIAEVFKEVETLEKIGLAVPQVTYLIRELRNKGFNISEEIFTISQAKEALLEIIRNNN | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31962
Sequence Length... |
Q890R3 | MSIKIENLTHVYMQETPFEKKAIDDVNLEIKNGEFIALIGHTGSGKSTLIQHINGLLKPHSGRIIIDDIDITKKEVKMSEIRKKVGLVFQYPEYQLFEETIEKDIAFGPKNLNLSEEEINKRIKRAMNIVGLDYEKYRDKSPFELSGGQKRRVAIAGVVAMEPEVLILDEPTAGLDPKGRDEILGEIKDLHKEYNMTIILVSHSMEDVAKLATRVLVMHKGKCILDGEPSQVFNEVDTLESVGLAAPQVTYLMRSLKEKGFNISENIFTIEQAKKELLKIFNNKATNC | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32541
Sequence Length... |
Q8RHK9 | MKISLKNLGYEYPTFENNKNGIYDVSLEIDSHKRIAIVGHTGSGKSTLLKLIKGLLKKQTGEININGKIEDIGYIFQYPEHQIFETTIFKDISYGLKRLKLNEKEVLERVEKILELVGLDKDCLHHSTLNLSGGEKRRVALAGVLIMQPQLLLLDEATVGLDLNGKEQLFKILLDWQKEENKSFLFITHDMNDVSEYAEEVIVMDKGKLLYHTNPSELFEKYSDELESLGLELPECISFFNKLNQKLKNPIKISGDIKEESILKVIEEKIK | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31024
Sequence Length... |
Q9KGD6 | MKGSPFEKVALSDVSFTIPSGSFTAIIGHTGSGKSTLAQHFNGLLRPSKGTVRLGELEITADQKPPSLKEIRRKVGLVFQYPEHQLFEETVEKDICFGPMNYGVSEARAKKRAKELLHLVGLPDTYLQASPFSLSGGQMRRVAIAGVLAMEPDVLVLDEPTAGLDPEGQRLIMDMFYRLHQEKELTTVLVTHNMSDAAKFADQIIVMSQGNVAMTGDRQTVFARADELVALGLDVPETLQLLLQVKERFGLHDVPPLFSLEELADFLAKELQQKEGQPCSKI | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31060
Sequence Length... |
D4AZK9 | MAITKYLVSALAVAGLAFAKDCAGDLTIENQQDVSTLSSCEKWDGDIVISEVVKSSISLTGVKQITGSLKAKNSSITELSAPNLNSIGDALSLSTCTALRSLDLSSLTKVKTLSLEALPKLQALGFTRTVSQATSILITNTDLTSLQGLDLETVGDFMVTNNPHLMEINVNKMTNITGYLNFAANNKQLSVKFPNLEGAHNMTFRNVSDASLPSLHKMDGLLGFYSNFFMNISAPNLTATGDLVFTSNSAVMNISMPKLETVKGGLQLANNSLLEDIEGFPALKLITGALDITGKFKTVKLPSLKEVRGDANLQSTETFG... | Function: Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleave... |
Q4WNS8 | MAFLKYALPALAAAQAVLAANCGKTDETITISSQSDADGYSSCSTIKGTIEIDEHLSGAITFNNVKQIDGTLSCTGGANISSIAAPMLNSIADTFKLDGLTTLTTLSFPSLTSVGSIQWTALPQLQSLDFTKGVNEAGDVTITNTGLANLNGISLNTVGKFDITENTQLKSININNLKNATGLINFAGNLNSLEVELPNLSSGTNMTFRNVSAVSVPSLHNLTGQLGFWGDTFKSFSAPNLTETGDLVFNSNSKLTNISMPALETVNGGFLITRNDELSSIDLPSLKVVTGAVDFSGKFDEVSMPKLENVKGQFNLQSTG... | Function: Involved in conidial and mycelial cell wall biogenesis.
PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 41505
Sequence Length: 398
Subcellular Location: Cell membrane
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Q5AGC4 | MQIKSFLLPIVAALLTSVSAADSSNKCSFSKTSITEATAITQLNACSTLDGEITVSGSGIGSIDLSSVKVLKAKLSILNSPSIVSLNFNQLQNITGALVINNATQLNSIDLTQLTNVETLQLVSLPSFAILNLNQGVQKAGTIVLSDTALTNLNGLASFNTIDSININNNKNISKIEFNDLQTVTDSLILSFNNDDAEVKLDSLKWAGNLTIQDVSSIQASNLTSVNGSLLISYNTFDELEFPNLKSVGNSMQIFAHDELTKISFPKLSELDGELEMFNNTQLEEIDFGNLTTIKGAVTISGPFDNLTMENLKLVSGDFQ... | Function: Cell surface protein required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43683
Sequence Length: 413
Subcellular Location: Cell membrane
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O13960 | MLFKSFALTLLFAAARVQAASNCSSGPYNISAQGTLDELNSCTVLNGDLYISDAGNSGITTLTVNGIESVQGDVVVSDGQYLTSLSFPSLKNVSGAFNVNNMIRMNNLATPELTSVGSLNLAVLPNLQELQFNAGLSDSDSVVIDDTQLQAIDGISLDSVTTFQVTNNRYIQEITMEGLESAQNIQISANSKGVSVNFSKLSNVTTATFDGISNVFIGNLKSAAGNLYFSNTTLDNISVPYLTEIGQSFAVLYSPELTSLNFPNLTTVGGGFVINDTGLTSIDGFPVISEIGGGLVLLGNFSSIDMPDLSDVKGALTVET... | Function: Involved in the negative feedback regulation of pmk1 cell integrity signaling and is linked to cellular calcium signaling.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cl... |
Q9UNE0 | MAHVGDCTQTPWLPVLVVSLMCSARAEYSNCGENEYYNQTTGLCQECPPCGPGEEPYLSCGYGTKDEDYGCVPCPAEKFSKGGYQICRRHKDCEGFFRATVLTPGDMENDAECGPCLPGYYMLENRPRNIYGMVCYSCLLAPPNTKECVGATSGASANFPGTSGSSTLSPFQHAHKELSGQGHLATALIIAMSTIFIMAIAIVLIIMFYILKTKPSAPACCTSHPGKSVEAQVSKDEEKKEAPDNVVMFSEKDEFEKLTATPAKPTKSENDASSENEQLLSRSVDSDEEPAPDKQGSPELCLLSLVHLAREKSATSNKSA... | Function: Receptor for EDA isoform A1, but not for EDA isoform A2. Mediates the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48582
Sequence Length: 448
Subcellular Location: Membrane
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Q9R187 | MAHVGDCKWMSWLPVLVVSLMCSAKAEDSNCGENEYHNQTTGLCQQCPPCRPGEEPYMSCGYGTKDDDYGCVPCPAEKFSKGGYQICRRHKDCEGFFRATVLTPGDMENDAECGPCLPGYYMLENRPRNIYGMVCYSCLLAPPNTKECVGATSGVSAHSSSTSGGSTLSPFQHAHKELSGQGHLATALIIAMSTIFIMAIAIVLIIMFYIMKTKPSAPACCSSPPGKSAEAPANTHEEKKEAPDSVVTFPENGEFQKLTATPTKTPKSENDASSENEQLLSRSVDSDEEPAPDKQGSPELCLLSLVHLAREKSVTSNKSA... | Function: Receptor for EDA isoform TAA, but not for EDA isoform TA-2 (By similarity). May mediate the activation of NF-kappa-B and JNK. May promote caspase-independent cell death.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48434
Sequence Length: 448
Subcellular Location: Membrane
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Q90VY2 | MKMWKRRGQKKSMFLSSLLVCCMFASAEYSSCGEYEFFNQTSNSCQACPQCRPGQEPNMSCGHGMKDEGFACVPCPQGKYSKGKYEICRRHKDCNALYKATVREPGTAEKDAECGPCLPGYYMLENRARNLYAMVCHSCQNAPLNTKECKKTTEAIIKPPINPGSTTVLPHPGSPGQGHLATALIIAMSTIFIMAIAIVLIIMFYILKAKPNGQACCSGQVVKAVEAQTNKLEDKKDVPDNVVIFPEKEEYDKLKASPQKTVKSENDASSENEQLLSRSIDSDEEPTSDKLRSSEATNHNLCQANVGYKPDLCLLSLGLL... | Function: Receptor for EDA (By similarity). May mediate the activation of NF-kappa-B and JNK.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56066
Sequence Length: 514
Subcellular Location: Membrane
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Q9BEG5 | MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRFSGPGTPGTSGTLSSPGGLDPNGPITRHFGQRSPQQQPLEPGETTLPPDSQDGHQMALVNFFIPKEKSYSEEESRRVRRNKRSKSSEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASY... | Function: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform A1 binds only to the receptor EDAR, while isoform A2 binds exclusively to the receptor EDA2R. May also play a... |
Q92838 | MGYPEVERRELLPAAAPRERGSQGCGCGGAPARAGEGNSCLLFLGFFGLSLALHLLTLCCYLELRSELRRERGAESRLGGSGTPGTSGTLSSLGGLDPDSPITSHLGQPSPKQQPLEPGEAALHSDSQDGHQMALLNFFFPDEKPYSEEESRRVRRNKRSKSNEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKAGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASY... | Function: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R . May also play a role in cell adhesion (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II m... |
O54693 | MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCCYLELRSELRRERGTESRLGGPGAPGTSGTLSSPGSLDPVGPITRHLGQPSFQQQPLEPGEDPLPPDSQDRHQMALLNFFFPDEKAYSEEESRRVRRNKRSKSGEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKTGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASY... | Function: Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R (By similari... |
Q502M5 | MALDWVGNLVSIHCGPTLGVYQGEISSVDQTSQTISLRNPFHNGVKCTVPEVTFSAMDIKDLKILEISKNSIEVSKQNGPESSSTTLMPHVGRKDKGGGGGGGGAPANSAPVMVPNKAEPRLQEGGVSPVPHYSKSYGERHIDMAVQGKGFRRRHNSWSSSCRGPNQATPKKNGLKNGGHMKNKDDECFGDGMDDVLDEDFDFEGNLALFDKAAVLSQIESSERRGNGARSRGTPGEQTPSRYRHDENILEAKPVVYRQITVPQNGSKEYSTDSGLVVPSISFELHKRLLAAAESHGLSLERRLEMTGVCASQMALTLLG... | Function: Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping (By similarity).
Sequence Mass (Da): 54852
Sequence Length: 507
Domain: The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with other proteins (By similari... |
Q96F86 | MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGTGKFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLL... | Function: Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis.
Sequence Mass (Da): 56078
Sequence Length: 508
Domain: The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction... |
Q17152 | MVNFTIDQIRHMMNMTHNIRNLSVVAHVDHGKSTLTDALVSKAGIISKKAAGDARFTDTRADEQERCITIKSTGISLYFEYDPETIDKQAAAPLNPTEEGDPTEEDIEIKQNSYLINLIDSPGHVDFSSEVTASLRVTDGALVVVDSVGGVCVQTETVLRQALAERIRPVLSCMCNKLDRVIAELQLDPEEAYHKLMKSVESVNVIIATYPDEAVGDIQVYPNQGTVAFGSGLQQWGFTRKFARLYAKKFGIDETKMMERLWGDYFFDAENKKWAKTDKKDERKAQGKKPLKRAFVQFVLDPVYGLYRALNEGRTEKYMK... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
Q1HPK6 | MVNFTVDEIRGMMDKKRNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAGARAGETRFTDTRKDEQDRCITIKSTAISMFFELEEKDLVFITNPDQREKSEKGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPILFMNKMDRALLELQLEAEELYQTFQRIVENVNVIIATYNDDGGPMGEVRVDPSKGSVGFGSGLHGWAFTLKQFSEMYADKFKIDLVKLMNRLWGENFFNPQTKKWSKQKDDDNKRSFCMYVLDPIYKVFDAIMKFKKEEIDDLLKKIGVTIKHEDSDKDGKA... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
P29691 | MVNFTVDEIRALMDRKRNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAGSKAGETRFTDTRKDEQERCITIKSTAISLFFELEKKDLEFVKGENQFETVEVDGKKEKYNGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLFMNKMDRALLELQLGAEELFQTFQRIVENINVIIATYGDDDGPMGPIMVDPSIGNVGFGSGLHGWAFTLKQFAEMYAGKFGVQVDKLMKNLWGDRFFDLKTKKWSSTQTDESKRGFCQFVLDPIFMVFDAVMNIKKDKTAALVEKLGIKLAND... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
Q23716 | MVNFTVEQIREIMGKPHNIRNMSVIAHVDHGKSTLTDSLVCKAGIIASKAAGDARFTDTRADEQERCITIKSTGISLFFEHDLEDGKGRQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDAVDGVCIQTETVLRQALNERIRPVLHVNKVDRALLELQWEAEDIYQNFTRVIENVNVIISTYSDELMGDVQVFPEKGTVSFGSGLHGWAFTIEKFARIYAKKFGVEKSKMMQRLWGDNFFNPETKKFTKTQEPGSKRAFCQFIMEPICQLFSSIMNGDKAKYEKMLVNLGVELKGDDKALVDKPLLKKVMQLWLSA... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
Q6P3J5 | MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIASARAGETRFTDTRKDEQERCITIKSTAISMYYELTENDLAFIKQCKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEDEGGPMGNIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVAKFASKGEAQLSPADRCKKVEDMMKKLWGDRYFDPAGGKFTKTANGPDGKKYPRTFAQLILDPIFKVFDAIMNFKKEETAKLIEKLD... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (By similarity). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the... |
P15112 | MVNFTIDQIRAIMDRRENIRNMSVIAHVDHGKTTLSDSLIQRAGIIADKVSGDMRYMSCRADEQERGITIKSSSVSLHFEMPKEDKLPAGCTSHEFLINLIDSPGHVDFSSEVTAALRVTDGALVVIDCVEGVCVQTETVLRQAVAERIKPVLFVNKVDRFLLELQLNTEEAYLSFRRAIESVNVIVGNTEDKEFGDVTVSPEKGTVAFGSGLHGWGFTLGRFAKLYAAKFGVPEDKLMGRLWGDSYFDATAKKWTSNPQSADGKALPRAFCQFVLEPIYQLTRAIVDEDAVKLEKMMKTLQITLAPEDAEIKGKQLVKA... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
P13060 | MVNFTVDEIRGLMDKKRNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAGAKAGETRFTDTRKDEQERCITIKSTAISMYFEVEEKDLVFITHPDQREKECKGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPILFMNKMDRALLELQLDAEELYQTFQRIVENVNVIIATYNDDGGPMGEVRVDPSKGSVGFGSGLHGWAFTLKQFSEMYSEKFKIDVVKLMNRLWGENFFNAKTKKWQKQKEADNKRSFCMYILDPIYKVFDAIMNYKKEEIGTLLEKIGVTLKHEDKDKDGKA... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
Q8SQT7 | MADFHISKVHELMMNQKNIRNISVIAHVDHGKSTLTDCLVIKAKIVSKDSGGGRYMDSREDEQQRGITIKSSAISLHFQVQKDVLEAYTKEGDTNGTEFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVDGICVQTETVLGQAMNERIIPTLVLNKLDRAILELEYPQEKLGEVLRRRVEGFNAKLSTLGYNFKVESLLPEKNEISFCSGLQGWGFTLRQFARFYLEKFNMNGFEGERKLTNFLWSHKVSCTSDDPFDASIKHIAKPNPARSPFVVYVLNPIYKVKELCNNGKVEEIKEYLKFYKVDFKGVVLTGS... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
Q06193 | MSSTGVKTMKDFMLNKSNIRNMCVIAHVDHGKSTLTDSLVTLAGIISNEKAGVARYTDTRPDEQERCITIKSTSISMYYEIEDKEDIPADANGNGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALTERVKPIVIINKVDRVILELKEEPEEAYQSFCRSIENVNVLISTYKDELLGDVQVSPGEGTVAFGSGLHGWAFTLEKFAKMWSAKFGIDRKRMLEKLWGDNYWDAKAKKWKKNGKGDHGEVLQRGFVQFCFDPITKLFNAIMEGRKADYEKMLTNLQIKLSADDKEKEGKELLKT... | Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, ... |
P0CP45 | MSQDPILTSKGSQEEEDFFGLDNFFPEPESPLPPPFSFASYDIPANIDFYVPDHRKSLILRLVGSHPLWGHHLWNTARTLSTYLLETPQITQSRHVLELGAGAGLPSIVCVLAGSSKVIVTDYSDEGLLDNLRFNVDVNLEGEEKERIAVDGHVWGQSVDPLLGHLPKGQKYDLLILSDLVFNHSQHDALIKTVEATLTSSSTQSYDPSNPSAPLTEPSILVFFTHHRPHLAHADMAFFPRLAESGNGWAYEKVVEEWAGAMFENDPGDKKVRGTVHGWRAWRVRDGEERGEKPSRISL | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 33358
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q5BAD0 | MADDFDTGDMFKDPEGFYPPEKEPTFAEHRMLSGQVVRVRLVGSHPLYGNMLWNAGRISSEYIETHAPTLIAGKDVLEIGAAAGVPSIVSAIMGARTTVMTDYPDPDLVDNMRQNADASASMIPTDPPSSLHVTGYKWGSDVEPLKAYLPEESRADGFDVLIMADVVYSHREHGNLVKTMQETLKRQKDAVALVIFTPYEPWLLPQTERFFPLAEQGGFTVTKVFEKLTEKLLFENDPGDERLRRTVFGYELRWKDELR | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 29157
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q4I2X5 | MSGEVDYGFGDLMDDPEDYCPPTPPPTSQVFTMQSGKPITLHLVGASPTEAHHLWNGAKMIADFFEEDLSRVKGKTVLELGAAAGLPSLVAAILGAHKVVVTDYPDPDIIRIMQKNVDECDETVEPRGRIVDTVDAMGFVWGADSVPLLARLNPTDDSHKERFDILILADLLFRHSEHGNMVKTIKETLKISRESVAYVFFTSYRPWKKELDMGFFDIAREQGFEVEQIAERRLDKPLFENDPGDLDVQKTVKGFAVRWSAEACN | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 29613
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q7S634 | MSKPEEVVNHVPEDEGSDIEAGGLFEDPPDFYPPSPPPTTEHYTMKNGDDITLHLVGHSPLEAHTLWNGAVIISQYFEEHPEEVKDRTVLEIGAAAGLPSLVAAVLGAKKVVVTDFPDPDIVDVMWKNIRGCPMLAVDREEDRNIVADGYVWGGKEAPLLAHLGEQKEGEAGFDVLILADLLFRHSEHSKLVDTIQFTLKKKPGSKAFVVFTSYRPWLQHKDLAFFDLARERGFIVDKFLEVKTEKPLFENDPGDEEIRKTVTGWTVRWPTDDEKAAAKADA | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 31452
Sequence Length: 282
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9UT28 | MADNDFEGFGIFEEPEGFRPSTPPPKEVLHTRVIVPNGPEEIKLRLVGSHSLWAHYLWNSGIELANYIDKNPDTVRAKKVLELGAGAGLPSIVSAFDGAKFVVSTDYPDPALIDNLEHNVKQYAEIASKISAVGYLWGSNIKEVMSNAGFKDNEVFDILLLSDLVFNHTEHSKLIKSCKMAIEGNPNAVVYVFFTHHRPHLAKKDMIFFDIAQSEGFQIEKILEEKRTPMFEEDPGAPEIRATVHGYKMTIPIPV | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 28490
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q6CHE9 | MSDIEDLASGGLFDEPKDFYKPEEQPGSDSYARQEKHVAASEYKEPTNFNLRLTAKNPLWGHLLWNAGKVTSDYLDEHSKELVEGKKVIEFGAGAGLPSLLCHAVGAKQVVITDYPDADLLYNLKYNVDQLKKDWDAKNADFSGPSPCADVSSMKVEGFIWGNDASELIEMSGGTGYDLVILSDVVFNHSEHAKLVRSAKELLAPGGKVFVVFTPHRAKLFNEDLDFFRRAKDEAGFESEKLFELKYYPMFEEEEETKELRSMVFGYMLTLKE | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Sequence Mass (Da): 30729
Sequence Length: 273
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q05874 | MSDIESLGEAAGLFEEPEDFLPPPPKPHFAEYQRSHITKESKSDVKDIKLRLVGTSPLWGHLLWNAGIYTANHLDSHPELIKGKTVLELGAAAALPSVICALNGAQMVVSTDYPDPDLMQNIDYNIKSNVPEDFNNVSTEGYIWGNDYSPLLAHIEKIGNNNGKFDLIILSDLVFNHTEHHKLLQTTKDLLAEKGQALVVFSPHRPKLLEKDLEFFELAKNEFHLVPQLIEMVNWKPMFDEDEETIEVRSRVYAYYLTHEK | Function: S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of 'Lys-3' . May be involved in rDNA silencing and in lifespan determination .
Sequence Mass (Da): 2963... |
Q17QF2 | MSDSENEGPPQLSSYALAALQEFYAEQQHHHSDLCGDDKYNIGIIEENWQLSQFWYSPETATCLAEDAVAAAGEGGRIACVSAPSVYQKLRERHRDDVSVCIFEYDRRFAIYGEDFVYYDYKNPVDLPERIATHSFDIVVADPPYLSEECLRKMSETIKLLTRGKILLCTGAVMEDAAAKLLGVKMCKFIPEHTRTLGNEFRCFVNYNSGLDCNLSVQLPVQEGPK | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 25495
Sequence Length: 226
Subcellular ... |
Q5ZKT6 | MDDDDDDIPQLSSHTLAALQEFYLEQQQREGMKTSQGFNQYSVGSIEEDWQLSQFWYSDETASCLANEAIVAAGKGGRIACVSAPSVYQKLREQGGADFSVCILEYDRRFSVYGEEFIFYDYNNPLNLPEHLLPHSFDIVVADPPYLSEECLQKTAETIKYLTKGKILLCTGAIMEEQAAKHLGVKICKFIPKHSRNLANEFRCYVNYASGLD | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 24079
Sequence Length: 213
Subcellular ... |
Q6NYP8 | MSQFWYSEETASRLAEELLQQAGEHGRIACLSAPSVYQKLKQLESVRSDGVSAVLLEFDRRFAAYGDEFVFYDYNNPLCLPEDLLPQSFDIVIADPPYLSEECLSKVTLTVKHLTKGKILLCTGAIMEEHAGKLLDLKMCSFLPRHNHNLANEFRCYVNYESRLLS | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 18915
Sequence Length: 166
Subcellular ... |
Q8WVE0 | MSDLEDDETPQLSAHALAALQEFYAEQKQQIEPGEDDKYNIGIIEENWQLSQFWYSQETALQLAQEAIAAVGEGGRIACVSAPSVYQKLRELCRENFSIYIFEYDKRFAMYGEEFIFYDYNNPLDLPERIAAHSFDIVIADPPYLSEECLRKTSETVKYLTRGKILLCTGAIMEEQAAELLGVKMCTFVPRHTRNLANEFRCYVNYDSGLDCGI | Function: Protein N-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 24506
Sequence Length: 214
Subcellula... |
Q9CY45 | MSESEDDDIPQLSSHTLAALQEFYAEQKQSVNPRGDDKYNVGVIEENWQLSQFWYSQDTALRLAREAIDAAGEGGRIACVSAPSVYQKLRELCREDSSVYIFEYDRRFAIYGDEFIFYDYNHPLELPERIAAHSFDLVVADPPYLSEECLRKTSETIQFLTRGKILLCTGAIMEEQAAQLLGVKMCKFIPEHSRNLANEFRCYTNYDSGLDCEA | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 24499
Sequence Length: 214
Subcellular ... |
Q5D013 | MNSSVSTHGTGDCPVNCTKSEDFAPSKLGTKEYWDGAYKRELQTYKDIGDVGEIWFGEESMHRVIRWMEAQNISENAAILDIGTGNGMFLVELARHGFSNLTGIDYSKAALELTTNILVEEGLKNINIQVEDFLNPSTELKGFDVCIDKGTFDAISLNPEDREEAKKHYVTSLRAVMRPNGFFIITSCNWTKEQLLEIFKPGFELVRELPTPNFQFGGVTGNSVTALVFKQTD | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 26033
Sequence Length: 233
Subcellular... |
Q5JPI9 | MSSGADGGGGAAVAARSDKGSPGEDGFVPSALGTREHWDAVYERELQTFREYGDTGEIWFGEESMNRLIRWMQKHKIPLDASVLDIGTGNGVFLVELAKFGFSNITGIDYSPSAIQLSGSIIEKEGLSNIKLKVEDFLNLSTQLSGFHICIDKGTFDAISLNPDNAIEKRKQYVKSLSRVLKVKGFFLITSCNWTKEELLNEFSEGWSTVAGFWLTAALTSWAQAIFSTSASRVGGTTGTHHHAWIIFVFLAETRFCHVVQAGLELLGSSDSPTWPPKVLGLYHARPSLAF | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31830
Sequence Length: 291
Subcellular... |
Q9D853 | MNADAEGHSGAVVPAQSPEGSSAADDFVPSALGTREHWDAVYERELRTFQEYGDTGEIWFGEESMNRLIRWMQKHKIPLDASVLDIGTGNGVFLVELVKHGFSNITGIDYSPSAIKLSASILEKEGLSNINLKVEDFLNPSTKLSGFHVCVDKGTYDAISLNPDNAIEKRKQYVMSLSRVLEVKGFFLITSCNWTKAELLDAFSEGFELFEELPTPKFSFGGRSGNTVAALVFQKRGTSLDKIS | Function: Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 26864
Sequence Length: 244
Subcellular... |
B9E6R3 | MISVNDFKTGLTIEVDNGIWRVIEFQHVKPGKGAAFVRSKLRNLRTGAIQEKTFRAGEKVGKAQIDNKRMQYLYASGDQHVFMDTESYEQIELSEDTIEYELKFLKENMEVHIQMYEGETLGVELPNTVTLQVTETEPGIKGDTAQGATKAATVETGYTLNVPLFVNEGDTLIINTTDGSYVSRG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
... |
A0L673 | MLSHTEMKQGKRVLIDDQPWIIVKADFVKPGKGQAFTKIKVKNLMDGRVIERTFKSSDSVAKADVVDVEMQYLYNDGELYHFMNPATFEQVALSEKQVEECKKWLKENEVYEVTLWENRAINVVPPSFMILEITECEPGVRGDTVTGATKPAVVESGASIKVPLFVEIGARVKVDTRTGEYMERAKG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
... |
Q6F157 | MSVNDLRPGTTFIYEGNLFVVIEQSFSKTGRQQGKVSVKAKNLRTGSRVEITFTGGEKVEKAMIERKDMQYLYNDGTDAYLMDTDTYEQIQIPMTRLEWESKFLTDGLMIKMTEYDGEVLGISLPDKVELEVTEAEAAVKGDTTSGALKKAVVETGLDIMVPLFVNVGTKVIISTTDGKYSGRAQ | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
... |
Q22024 | MSIDTDFLTSVEVKEDELHGNVLIAVTQIALGRTIGVIDKATPNDSNALLILNLIKEADDGEDANICMRQEDRKTFLQTSKIINIGERLLLQRLSEEECDEEDQDDLENLILLKDEDRPDSTQSCTKSSSEDSNLNGFEEYIREHGELVPGQTPPDGSHKCGVCPKSFSSASGLKQHSHIHCSLKPFRCHLCPKSYTQFSNLCRHRRVHSDGWTCPTCQSQMPSQAALTKHRPVCEMTALYKPLMAQLAGLSGAGGLGSVPYWPHILQMATQAPHFPLAFLAANPEAYKLMQQTTCASPDAECSSGHASESSPTTTEPVD... | Function: Probable transcription factor, required for migration of the hermaphrodite-specific motor neurons (HSNs) from the tail to the gonad primordium during HSN cell differentiation . Required for phasmid neuron development . Required to specify the pi-cell fate of ventral uterine precursor cell (VU) cells .
Sequenc... |
O76360 | MSSGSRPSSGGGGGGGGASGGAGGGAPGGGGGGIRGFFSKLRKPSDQPNGNQVQVGTRTFEAHELQKLIPQLEEAISRKDAQLRQQQTIVEGHIKRISELEGEVTTLQRECDKLRSVLEQKAQSAASPGGQPPSPSPRTDQLGNDLQQKAVLPADGVQRAKKIAVSAEPTNFENKPATLQHYNKTVGAKQMIRDAVQKNDFLKQLAKEQIIELVNCMYEMRARAGQWVIQEGEPGDRLFVVAEGELQVSREGALLGKMRAGTVMGELAILYNCTRTASVQALTDVQLWVLDRSVFQMITQRLGMERHSQLMNFLTKVSIF... | Function: Promotes chemoreceptor gene expression in response to increased cGMP levels by antagonizing the gene repression functions of the class II HDAC hda-4 and the mef-2 transcription factor . Regulates gene expression via recruitment of a histone deacetylase complex containing hda-2, saeg-1 and saeg-2 . Represses b... |
G5EBV0 | MSSAPNDDCEIDKGTPSTASLFTTLMLSQPSSSTAVLQCTYCGSSCTSSQLQTCLFCGTVAYCSKEHQQLDWLTHKMICKSLQTSGMVPSNLMPQAAPAVMAPIPPTVSFDDPALTTSLLLSLQNNPILNQTISNFPPTFSITSKTEPEPSIPIQIPQRISSTSTVPFSSEGSAFKPYRNTHVFNSISSESMSSMCTSHEASLEHMSSASLAMFPTSSTAQSDISRLAQVLSLAGDSPASLALVTTSVPSTASTATIPPPATTTSSATSSGKSETITVGKEKIIQTDDPDIQIIETEGGSKPTVSRTRKRPTPSNSADPK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cellular oxygen sensor which regulates the stability and the activity of hypoxia-inducible transcription factor, hif-1. In normoxic conditions, hydroxylates hif-1 targeting it for vhl-1-mediated proteasomal degradation . In addition, regulates hif-1 transcriptional ac... |
Q5BDU5 | MRSLVLLSSVLALVAPSKGAFTWLGTNEAGAEFGEGSYPGELGTEYIWPDLGTIGTLRNEGMNIFRVAFSMERLVPDSLAGPVADEYFQDLVETVNGITALGAYAVLDPHNYGRYYGNIITSTDDFAAFWTILATEFASNELVIFDTNNEYHTMDQSLVLNLNQAAIDAIRASGATSQYIFAEGNSWTGAWTWVDVNDNMKALTDPQDKLIYEMHQYLDSDGSGTNTACVSSTIGSERVTAATNWLRENGKLGVLGEFAGANNQVCKDAVADLLEYLEENSDVWLGALWWAAGPWWGDYMFNMEPTSGIAYQEYSEILQP... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cel... |
O74706 | MKFQSTLLLAAAAGSALAVPHGSGHKKRASVFEWFGSNESGAEFGTNIPGVWGTDYIFPDPSTISTLIGKGMNFFRVQFMMERLLPDSMTGSYDEEYLANLTTVVKAVTDGGAHALIDPHNYGRYNGEIISSTSDFQTFWQNLAGQYKDNDLVMFDTNNEYYDMDQDLVLNLNQAAINGIRAAGASQYIFVEGNSWTGAWTWVDVNDNMKNLTDPEDKIVYEMHQYLDSDGSGTSETCVSGTIGKERITDATQWLKDNKKVGFIGEYAGGSNDVCRSAVSGMLEYMANNTDVWKGASWWAAGPWWGDYIFSLEPPDGTAY... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cel... |
Q1HFS8 | MKVNTLLVAVAAGTAMAAPQLKKRAGFTFFGVTEAGAEFGEKSIPGVWGTDYTFPDTESILTLISKGFNTFRIPFLMERLTPEMTGSFDEGYLKNLTSVVNAVTDAGAWAIVDAQNFGRFNGEIISSASDFQTWWKNVAAEFADNKNVIFDTNNEFHDMDQTLVLDLNQAAINGIRAAGATSQYIFVEGNSYTGAWTWTDNNDNLKSLTDPQDKIVYEMHQYLDTDGSGTHETCVSETIGAERVESATQWLKDNGKLGVIGEFAGGNNEICRAAVKSLLDALKENDDVWLGALWWAAGPWWEDYMFSMEPTDGIAYTGML... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cel... |
A1DME8 | MKFGSIVLIAAAAGSAVAAPAKRASVFQWFGSNESGAEFGQNTIPGSYGKEFIFPDPSTISTLIGKGMNIFRVQFLMERLVPSSMTGSYNEEYLANLTSVVDAVTKAGSYAILDPHNFGRYNGQIISSTDDFKTFWQNLAGKFKSNNLVIFDTNNEYHDMDQALVLNLNQAAINGIRAAGATSQYIFVEGNSWSGAWTWVDVNDNLKALTDPQDKIVYEMHQYLDSDGSGTSESCVSTTIGKERVTAATKWLKDNGKVGIIGEFAGGVNDQCRTAISGMLEYLAQNTDVWKGALWWAAGPWWGNYMFNMEPPSGAAYVGM... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic... |
Q4WG16 | MQFTHLVALALALATSEAAHQGFNYGNTKSDGSAKSQADFQAEFSTAKNLVGTSGFTSARLYTMIQGGTANTPISAIPAAITEQTSLLLGLWASGGNFANEIAALKAAIAQYGDDLAKLVVGISVGSEDLYRNSVDGVKANAGIGTNPDEIVSYINEVRSTIAGTKLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMANSISDAKALFDESVAKTQAVAKGKEVWITETGWPVSGKTENLAVANLANAKTYWDEVGCPLFGKTNTWWYILQDADPVTPNPSFGIVGSTLSTTPLFDLSCSASSSSSAAA... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in... |
A2QH21 | MQLAQLAAFAMTLATSEAAYQGFNYGNKFSDESSKFQADFEAEFKAAKNLVGTSGFTSARLYTMIQAYSTSDVIEAIPAAIAQDTSLLLGLWASGGGMDNEITALKTAISQYGEELGKLVVGISVGSEDLYRNSVEGAEADAGVGVNPDELVEYIKEVRSVIAGTALADVSIGHVDTWDSWTNSSNSAVVEAVDWLGFDGYPFFQSSMANSIDNAKTLFEESVAKTKAVAGDKEVWITETGWPVSGDSQGDAVASIANAKTFWDEVGCPLFGNVNTWWYILQDASPTTPNPSFGIVGSTLSTTPLFDLSCKNSTTSSSSA... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in... |
Q9H4M9 | MFSWVSKDARRKKEPELFQTVAEGLRQLYAQKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCAQLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNKADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPN... | Function: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes . Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes . Recruited to endosomal membranes upon nerve growth factor stim... |
Q7Y0W5 | MDHRELWPYGLRVLVIDDDCSYLSVMEDLLLKCSYKVTTYKNVREAVPFILDNPQIVDLVISDAFFPTEDGLLILQEVTSKFGIPTVIMASSGDTNTVMKYVANGAFDFLLKPVRIEELSNIWQHIFRKQMQDHKNNNMVGNLEKPGHPPSILAMARATPATTRSTATEASLAPLENEVRDDMVNYNGEITDIRDLGKSRLTWTTQLHRQFIAAVNHLGEDKAVPKKILGIMKVKHLTREQVASHLQKYRMQLKKSIPTTSKHGATLSSTALDKTQDHPSRSQYFNQDGCKEIMDYSLPRDDLSSGSECMLEELNDYSSE... | Function: Transcriptional activator that acts as floral inducer to promote short-day (SD) flowering pathway. Activates HD3A and other FT-like genes independently from HD1. May also activate MADS-box transcription factors involved in flowering regulation . Functions as a response regulator involved in His-to-Asp phospho... |
B3LF48 | METSSTISIGSCLKEHQKIYKEWFNIADSDGDGRVSGNDATKFFAMSKLSRQELKQVWAVADSKRQGFLGLSEFITAMKLVSLAQEGHEITSDLLKGSIDMKSVELPVLEGLENVVSKQKVSKTNVDVEDNVVTKPQVTAKTPWFKSKSIIKPQVNVVTIVDGLKRLYTEKLKPLEVTYRFNDFASPVLTSSDFDAKPMVMLLGQYSTGKTTFIKHLLGCDYPGAHIGPEPTTDRFVVAMSGPDERTIPGNTMAVQADMPFNGLTSFGGAFLSKFECSQMPHPVLDQITLVDTPGVLSGEKQRMQRSYDFTGVISWFASK... | Function: Involved in endocytosis negative regulation, probably by influencing actin organization. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Exhibits an inhibitory effect on endocytosis when over-expressed.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location To... |
Q9NZN3 | MFSWLGTDDRRRKDPEVFQTVSEGLKKLYKSKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMQGDMEGIIPGNALVVDPKKPFRKLNAFGNAFLNRFVCAQLPNPVLESISVIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKMRVVLNKADQIETQQLMRVYGALMWSLGKIVNTPEVIRVYIGSFWSHPLLIPDNRKLFEAEEQDLFRDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPS... | Function: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis . In vitro causes tubulation of endocytic membranes . Binding to phosphatidic acid induces its membrane tubulation activity (By similarity). Plays a role in endocytic transport. Involved in early endosome to... |
Q9H223 | MFSWMGRQAGGRERAGGADAVQTVTGGLRSLYLRKVLPLEEAYRFHEFHSPALEDADFENKPMILLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRISRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKRARLAKVHAYIISYLKKE... | Function: ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61175
Sequence Length: 541
Domain: The EH domain interacts with Asn-Pro-Phe (NPF) motif... |
Q9EQP2 | MFSWMGRQAGGRERSGGMDAVQTVTGGLRSLYQRKVLPLEEAYRFHEFHSPALEDADFENKPMILLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISIIDSPGILSGEKQRISRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKRARLAKVHAYIISYLKKE... | Function: ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61481
Sequence Length: 541
Domain: The EH domain interacts with Asn-Pro-Phe (NPF) motif... |
Q6TH15 | MAKFHAPVIQDNPSGWGPCAVPEKFKDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDEASFQLVDTAKTQKTAYQRNRMRFAQRNLRRDKDRRTLTQFNMQTLPKSAKQKERDRMRLQKKFQKQFGVRQKWDQKSQAQLKPRDSSVEVRSDWEVKEEMDFPRLMKMRYMDVADPLDIECCGALEHYDKAFDRITTRNEKPLKSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMCCTRSVNSWDIIVQRVGNKLFFDKRDNSDFDLLTVSETANEPPQDEGSSLNSPRNLAMEAT... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
Q554U9 | MSLELNTIKVNPTGWGPVGKLEKFTDIPYAPFSKGDKIGKCSDWNSNVRNYQRQNYGSNAFNPFTFKLEDDEDSFTLVDYTRVQNKLKNKGKTYQKQFYQQNKRGGSNAGGRGGRGGMRGGRFGSNNKYWNDRRQRNRESSIEILSSWESKEEFDLSTFKQYTVEQLPEPETIGTYGQVKYYNKVYDRINAKNEKKLQKTENSVPLIPTSDDKVIRSEYMNGNVYATDSILAVLMSAQKSVYSWDIVVQKVGARLFFELRPGTSEHLTVNENLTAHHQDDKDPINTTSSLSQEATQVNLNYWQQVLSQNVEPFKFDNELP... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
Q5AVZ0 | MAPISIADIVAALPAEDTWGPVTSADNMLDGVPYAPFSKGDKLGRMADWTADSKDRDRGGRQAYNRNYRDQQVYGAGSSSLFAVQVAEDESTFSVVDNTRTSAKRTFGRGGGTVFRGRAQRGGAGQRGGRAGFQRVGAGRGQGGDRYYDNRGARGNRGRRFGWKDYDKPQRTREPSVNIRPDWSMLEEVDFNRLSKLNLQAPEGEDVDTYGFLYYYDRSYDKAPVKNAERRLQALDRAAYNVTTSQDPVIQELAEKNQATIFATSDILSMLMCAPRSVYSWDIVIVHQGNKIYFDKREGASLDLVTVNENAADAPLEVAE... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
O15371 | MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDESSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQILPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYIN... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs . The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, ... |
O94236 | MATGFKLPELAPVKSAWGPPETEQIGGDIPYAPFSKGDRLGKIADWSVDQPKDGREQRGRQGAFAGRFRDQYQTYGYGASSIFGYQHSEDESSFSVIDRGSVNRTRTSARNGGTLLKVRGRGQNVQRGGRGGRYGSSGGRGAGDTVVSRSSGAGGARGRRFGWKDYDKHQRLRNASVTVGDDWQLLDEVEFSHLSKLNLAAAAPVTVDSYGYIYPYDKSFDKIHVKSEKPLQALDRVHYNPTTTEDPVIQKLALNSDANIFITDSILSLLMCSTRSVYPWDIVITHQSGKLFFDKREGGPFDYLTVNENAYDSPMDADNR... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
Q4PEZ2 | MASFKLPELQPDNDLWGPASGSNALPAELKDIPFAPYAKNDKVGRIADWNNASGASNDAANARGGRQGRARDVQQNFGTSAASSAFAYFHGDDEASFSVVDNTRTVASRRGGLGQMSQRGGRGGRGGAGGAGAAGGRGASKFGAGAGRGARGGRGGAAGARRGGGRFGWKEWDKPQRIREASVTVGQDWEQVEEIDFVRLGKLRLEVEEPQDISSYGSLFEYDRSYDRVTVKTAQSLSSIDRIRYNTTTSEDPVIHDISAKEDAQIYMTDSILALLMCATRSVYSWDVIITKTADGKVFFDKRDGGAFDYLTVNENAADP... | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifica... |
O75822 | MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis . The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre... |
Q5R8D1 | MAAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNTVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-... |
P19957 | MRASSFLIVVVFLIAGTLVLEAAVTGVPVKGQDTVKGRVPFNGQDPVKGQVSVKGQDKVKAQEPVKGPVSTKPGSCPIILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ | Function: Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis. Has been shown to inhibit the alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor and to produce a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation c... |
Q6UXG2 | MAEPGHSHHLSARVRGRTERRIPRLWRLLLWAGTAFQVTQGTGPELHACKESEYHYEYTACDSTGSRWRVAVPHTPGLCTSLPDPIKGTECSFSCNAGEFLDMKDQSCKPCAEGRYSLGTGIRFDEWDELPHGFASLSANMELDDSAAESTGNCTSSKWVPRGDYIASNTDECTATLMYAVNLKQSGTVNFEYYYPDSSIIFEFFVQNDQCQPNADDSRWMKTTEKGWEFHSVELNRGNNVLYWRTTAFSVWTKVPKPVLVRNIAITGVAYTSECFPCKPGTYADKQGSSFCKLCPANSYSNKGETSCHQCDPDKYSEKG... | Function: May protect cells from cell death by inducing cytosolic vacuolization and up-regulating the autophagy pathway . May play a role in apoptosis and cell proliferation through its interaction with HSPA5 .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 111382
Sequence Length: 1013
Subce... |
Q6DDW2 | MGVFCWSGCLVISLQLLLGAALDNLSTCKEEDYHYEYTECDSTGSRWRVAVPNPGKACAGLPDPVKGKECTFSCAAGEFLEISSQLCSKCEPGTYSLGTGIKFDEWDKMPQGFSNVATYMENTAEFSDNKPDSCVNSSWIPRGNYIESNSDDCTVSLIYAVHLKKAGSVSFEYQYLDNNIFFEFFIQNDQCQEMSSSSDKWVKLSDNSDWMNHMVSLKSGTNILYWRTTGILMGTKVAKPVLIKNITIEGVAYTSECFPCKPGTYSDEAGSSSCKICPRNTYSDRQAKECIKCFEEKEYSEEGASKCEERPPCTKKDLFQ... | Function: Functions as a regulator of the BMP signaling pathway and is involved in epidermal differentiation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 109731
Sequence Length: 995
Subcellular Location: Cell membrane
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P14756 | MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase . Autocatalyses processing of its pro-peptide . Processes the pro-peptide of pro-chitin-binding protein (cbpD) . Involved in the pathogenesis of P.aeruginos... |
Q15717 | MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFK... | Function: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability . Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). Has also been sho... |
P70372 | MSNGYEDHMAEDCRDDIGRTNLIVNYLPQNMTQEELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAISTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNMALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGISGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFK... | Function: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation . Has also been shown to be capable... |
Q9VHX7 | MDYLTMFYDGWRDLMDNKSDPRTRDYPLMSSPFPTIAISLTYAYIVKVLGPKLMENRKPFELRKVLIVYNAAQVIFSAWLFYESCIGGWLNGYNLRCEPVNYSYSPKAIRTAEGCWWYYFSKFTEFFDTFFFVMRKRYDQVSTLHVIHHGIMPVSVWWGVKFTPGGHSTFFGFLNTFVHIFMYAYYMLAAMGPKVQKYLWWKKYLTVMQMIQFVLVMVHSFQLFFKNDCNYPIGFAYFIGAHAVMFYFLFSNFYKRAYVKRDGKDKASVKANGHANGHVKALKDGDVAPTSNGQANGFHNTFSKFTTDMCNPALNSSTRQ... | Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle.
Catalytic Activity: a ... |
A1L3X0 | MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN | Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with... |
Q9D2Y9 | MAFSDLTSRTVRFYDNWIKDADPRVEDYLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHAFLNTAVHVVMYSYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTIHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTLENGNCKSKRH | Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with... |
F4I1S7 | MSENTKVEAKRVFIGAGCNRVVNNVSWGASGLVSFGAQNAVAVFCPKTAQILTTLPGHKASVNCTHWLPTSKFAFKAKKLDRQYLLSGDSDGIIILWELSTLNNDWRHVLQLPLSHKKGVTCITAYMVSETDAMFASASSDGVVNVWDVSFPSQPSEECKVVCLDSICVDTKAIVTLSLAELPQNPGRFALALGGLDNKIKLYSGERTGKFTSVCELKGHTDWIRSLDFSLPLHTTEEIPNSIMLVSSSQDKVIRIWKLVLVGDVGSWRREITLASYIEGPVFVSGTFTYQISVESVLIGHEDWVYSVEWQPPVIDFIDG... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in ... |
Q05AM5 | MAAPVMDTCHVSCCANRAPNVVSWGRGGLIAFGTCNSVAIYNPEEIRVVDLLNKHTGRVNAVQWVHEPDCSPENQLISGGSDNNVIVWEKLDGKFRACAVCSGHSGPVCAVDAVSLSSSHLLVASASSDSTVKLWTYSSDAAECLQTVAFGSGFMMDVSLALLPGSRVPVLACGGDDSRVHLYVQLSGQFQRVLTLTGHEDWVRGVEWANKDGELWLASCSQDCLIRVWRLFAKTAAEPDLQTDGIIKMKENIFQVSGEEFAVTLETVLAGHENWVYGIHWQPPSVKGDSVEQSLKLLSASMDKTMILWGPEEDSGMWVE... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble b... |
Q86H45 | MNVSSDVDFISVGCNCLGDCLVWGQNKLAAYGAQNFIALFDPIQSKVLATLPGHKDRVNHICWVPNINEEYKNRYSSYENELLSCSSDNTIISWKQIKGGLNYQYKVVEVLKGHSDSVTNISVLDFPDGSLLMCSTSADNTVKLWRRESLTKENIDTDTLPKWECIQTIDFTPKCMECSSLAFIPGTTIPLLAVGGLEPKIHIYIQNLDSTTATLQFKKLMSLQGHQDWIRSLSFKTINEGEGEGEEEELILASSSQDFKIRLWKISKFTAEKQKQQQLDESGNGGANLLGSLSTQLSGVTSLSTKGYLFNCNSVKYIIL... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base ... |
Q7K4B3 | MQVENLHTSVACNRCTECADWGPNGWIAYGACNAIAIMDPKFQGNSAKVLFTLVEHTKRVNTVRWLDCDKLLSGGDDAIAILWELDETGTTKSFTLKGHTSGVNTVDGIRQQDGSWLLATAAADTTIKLWTFQDNNYVCFQTISLSDGFCFCLRLQLLPKSNQVLLAFSGDDETVSLWSEQVETAGEGDSLGRQFQRKHKLTGHEDWVRGLDFVVDGEDLLLASGSQDNFIRLWRIAPRSKEQMQENRVDLHQLSHNDDEIKVEEKILQLGKEAWYAVSLESVLYGHEGWIYGVHWHKTPDQELRLLSASIDKTVIIWAP... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes the formation of carboxymethyluridine... |
Q6IA86 | MVAPVLETSHVFCCPNRVRGVLNWSSGPRGLLAFGTSCSVVLYDPLKRVVVTNLNGHTARVNCIQWICKQDGSPSTELVSGGSDNQVIHWEIEDNQLLKAVHLQGHEGPVYAVHAVYQRRTSDPALCTLIVSAAADSAVRLWSKKGPEVMCLQTLNFGNGFALALCLSFLPNTDVPILACGNDDCRIHIFAQQNDQFQKVLSLCGHEDWIRGVEWAAFGRDLFLASCSQDCLIRIWKLYIKSTSLETQDDDNIRLKENTFTIENESVKIAFAVTLETVLAGHENWVNAVHWQPVFYKDGVLQQPVRLLSASMDKTMILWA... | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes the formation of carboxymethyluridine in the wobble ... |
Q19967 | MDQFQALIEPARQFSKDSYRLVKRCTKPDRKEYQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGA | Function: Required for oocyte development and ovulation . Required for the translocation of secretory and transmembrane proteins into the endoplasmic reticulum in vitro .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7761
Sequence Length: 68
Subcellular Location: Endoplasmic reticulum membrane
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B2UQE3 | MPYIGCHLSSAKGYEAMGRVALSIGANTFQFFTRNPRGSKAKAIDEQDIARFLELARNNGFGTLLAHAPYTLNPCSADPSVARFAAQVLKEDLELMEHLPGNLYNFHPGCHVGQGVEKGIELVADQLNDVLSPEQKTIVLLETMSGKGSEVGRTFEELAAIMERVDLKDKLGVCLDTCHVYSAGYDIVNRLDSVLEHFDAVLGLERLRAIHLNDSMTPFSSFKDRHETIGKGSLGEQAFINIINHPVLRELPFFLETPRDDAGHGEEITWLKEHYRN | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
O67551 | MALFGAHVSSAGSILKTFKRAKDIGAEVFQFFLRSPRAWYWKGVDKETKQAFIEKLKDFKNPVMVHAPYLLNLASPNEELREKSVKVFLEELKFCDEVGIHFYNFHPGTAKGISDEEGLRNVIKSLEEVFSEYTPKFTTVLLENTAGERGDLGKNFKELKEIMNVFRGIKLGVCLDTCHAFAYGYEINTKEGFENFKREIEKMVGLESVKAVHANDSKVPLGGRKDRHEHIGKGYIGLEGFKNLLKDEYFSTLPYYIETPKENNMDPVNLSVLREIYQNNDL | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q2NJF9 | MLFLGSHVAMKKPHNFQGSIQTAISYGANALMVYSGAPQNTIRSKTEELKIKEALKIAQNNNLSLNNLVGHAPYIINLANPDKTKRAFAIDFLSQELERFAAMKINKMVLHPGNYLKTNPQEGISLIAQSLDLIFAKTKHLKTQISLETMAGKGTEIGKRLEELQQIRTLVKNKTRVSFCLDTCHLFDAGYDLKENLEEIIQKIDSILGFQNVSVIHINDSKNECNSHKDRHENIGFGKIGFETLLKIIYHRAFVCIPKILETPYINEKEPYKHEIEMIKTKNFNPELKNLF | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
B2A499 | MRLGFHMPLSGGVGKQLNRASELGMECIQIFSGNPTSWKPGKITPKSRDLFIKKQEELQIKPLVFHTPYLINLASPKNDIREKSIYLLNAALEKAKAYDAPYVVTHIGSHVGEGVEKGIDLVSYSLEKIMEDWPEGVELLLENTSGAGSTLGGSLTELKKIIDKFSGTQVLGCCFDTAHAWGAGYDISNVKEVETTLELVNEQLGLDLIKVCHANDTNVPLGSTKDRHQHIGEGNITDEGFGALLTHDSFTPKAVIMETPKNGTDCDQINLQRLKKVVGRHEEE | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
A9A555 | MQIGCHVSISGSIDKSVDNAVERECSAFQIFTRNPRGWHAKTLTKDDITNFKSKLKESKIDRFATCAHMPYLPNLATPKEDGFEKSVKTLVDEVERCAQLGIPYLVTHLGSHLGTGEEAGIKKLVKGLTEAGKTKNDVMILLENTAGQKNSVGSDFKQLGEIFKQLKPAKKFGVCLDTCHAFVFGYDLRTEAKVKETFSEFDKYVGIDNLKILHLNDAKGDLGCNLDRHYHLGMGGIGEKGISAIVKFANKKKIPIILETPIDDDRDDFENIRKAKEFA | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q30YP7 | METISRQNKPQQQLIGAHMSAAGGVHKAVERAEAAGATALQVFTRNQRQWNAPPLEEHDAELFTAAVRRWGGYPVSSHASYLINPAADTPEGAERSVALMADELQRAGRLGIEMVVVHPGAHKGQGEAAGAALAAARLDEALERCGSPAVMVLLENTAGQGTMLGASFAGLAAVIEASRMPERYGICLDTAHAFGAGYDLRDAALYDAAIRELDVCAGLDRLRLVHANDSLTGLGSRRDRHTHIGQGELGEAAFRLLMRDERLHHVPKVLETPKGKGPEEDMMNMAVLRRLACP | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q6MED0 | MSHSNLLLGAHTSAAGGVYRALLEGKKIGATTIQFFTSNQKQWKGRQFTTNDIELWQSTLKETNLTHLMSHDSYLINLGCPNQENLLKSRQAFQEEVIRCTQLGINYLNFHPGASLGEDVQKCLDSIVESLLLVRPFIQGNLRLLLEATAGQGTSVGHKFEQLAYIINGVKDELPIGVCIDTCHIFVAGYDIRTSSAWDFTLKGFDRIIGLPYLYAFHINDSSKDLGSRVDRHQPLGEGKIGWESFEFLMKDSRTRHLPKYLETPGGVDLWEKEIQKLKEFA | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
C0QRI1 | MVKIGAHVSSSKSLDLVFDRGREIGADTIQFFLSSPRSWHWKERSDEEKELFIQKRRETGISPVIAHSSYLFNLASSDPVLRKKSINGVIRELKLCEELKIDYYVIHAGKSKGLKESEAVKNIIDSVKEIFSKVKLKHTFFLYETLAGQKGEIGKTTDELAQLMEPFKKENTGVCVDTCHIYSAGYKINDEEGFYSYRSELSKKIGLENVKVIHCNDSKTPFNSKRDRHEHIGEGSIGYKGFEFFLNDEYFRRLPFILETPKTADWDIKNMERLRRLIRTAPVAQ | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence ... |
Q74MP4 | MIGYLFGNRVLVDDKELPLIEAYYLLDKGELEVYEDDKKLSKEEFLKKCLTYDERFLIRYKAYKELRDKGYTLGTALKFGADFRVYDIGVIPKKGKRSEREHSKWVLYPVSKDETFDFYEFASKNRVAHSTRKKLLLGIVSDKIEFIEVSWKKP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
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