ID A0A158Q1A2_BRUMA Unreviewed; 3645 AA.
AC A0A158Q1A2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JUN-2023, entry version 41.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=Bma-eel-1 {ECO:0000313|EMBL:CDP92870.1,
GN ECO:0000313|WBParaSite:Bm7004c.1};
GN ORFNames=BM_Bm7004 {ECO:0000313|EMBL:CDP92870.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDP92870.1};
RN [1] {ECO:0000313|EMBL:CDP92870.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP92870.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP92870.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP92870.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm7004c.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; LN856865; CDP92870.1; -; Genomic_DNA.
DR STRING; 6279.A0A158Q1A2; -.
DR EnsemblMetazoa; Bm7004c.1; Bm7004c.1; WBGene00227265.
DR WBParaSite; Bm7004c.1; Bm7004c.1; WBGene00227265.
DR InParanoid; A0A158Q1A2; -.
DR OrthoDB; 5396290at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14288; UBA_HUWE1; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041918; UBA_HUWE1.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 2.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1227..1267
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1469..1550
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 3309..3645
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 683..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2358..2381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3030..3052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3129..3150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1997..2033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2041..2055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3035..3052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3130..3150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3612
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3645 AA; 406321 MW; 557D9584E97A5BBB CRC64;
MKIDPKTLRP CSAEIFPRCM QLIEHIKSAS DRRTFVERLT EVHEWQPQFG KSEMARWSDV
LNMCDDVLKD AVTCSSSPGA AMAIDEDQTL LTDVTSVLSF TAMLFENTFT RSVYSSTDRL
LNLLDSGNVE IVVETLRLLL VISKRSRFLS QHLSDVQQKK LTVRLSAIAQ CWNGKLRSMK
MDECCTTNVR PSALLPIGFQ TDTNNLVRSV HLDKSFAAEL EHLLSGKNIE EDERASFIAR
LRLVRSFNTS RGRRLSIIAR LLSLSILVYT RSLIEEWAMT TMLYDGLIEE ITRLLLINNT
SESIIDAVKT EALRTLTSIV SLGRPAKLNI VIESLGVNSY HGFLARMTRQ CVDDLRCGRI
GSGYTTVPFC TALFSLLYHL AGFENGGEAL VSCALTETLL GVVSCETLPL ELITFVTRAV
RVIDIMTSLD ANGFISCNGM STIVHRLIFD VNICMKHLAE LSITGPTTEQ CHQQRAALIK
SLLNFIKRAV QDTQFADSTR HIMDSGLPIA LVHILSNCGF FGASLFHNAV CLITNFIYQE
PSLLTSLQDK GVTNAILKTI FREELPTSRD VIAALPNTFT ALCLNDRGLK AFMSENPFDH
FCDIFVSTKY IYAMKCRRNE MNEVALNLGT SFDAFLRHHP TLRESFLNSF AKMLSKLLDV
ASTDSPRCVM SFASCRSTQA TVAVSSTSPS QEEENIMGGN VSSDDDDEDP TSAVANMDEL
HTTENECNQL DLGLSLSIVC DGIPLIPLGE YLLNIGKFLE TLLTHNASPE QADVFVQSGT
ADKLLSLLFV RQIPLELSQS LFPQLVTNII RFLFQHTRSS DVMDMVANRL NKFCLDMLSS
CNTSEDSSKL SLLAMSSSEA SLANICAISV FCSVLSSLSK AALGSNTATK TAVLRFWTNE
GCRLLASCNH AQRIVVWESA VLQIFNATNK CIASTQTDDV QTSEPTEEAN ITLQEDSVGA
DSVPQRIGRP KYLLDDYWLR SKSGTSALNR CNRHCTELLS MLVKISIGGM TRTRRIQENE
GGTPCENAVQ LALQIMKGFQ QALEWKPHDE TDPAIMLPYL AIWINNLSNI LFDERKIPYH
LMLSAFYRTG THDTFFNIIS NYFAPDRDQN YCEVGQLLQA WLSLTERLVS AHLFRHSRYK
MSERLAEAKR FPTEKYLAKC QQDAFRQSNV VFGVLSALPL SEAVSFNICD MIISIYREIV
KGIVPLTEKQ KQAVVTTSED RKKMEAELDG ASIGLLVDMG FDRDAAVDAL LEYSTVPEAA
EYLIATDSLG RLRQSSTDER IDTDETDAED GSGQNGDLNV EFEDVLLKEP ISLNEVPSLD
TRLILSSLCK DVIPILLNLM EHGAELVFST SEVMLVILNE VDDDWRKNML IGEYLVQDIL
LMVDELRCDE TDEKAVISLS TRLHFVCLLW PGIATTYMDV CTEYRLHSVL ISVLDMVVIH
CSKRPAFIRL IAPICLWLDL YDKMLKLLDS KDKVEKAVES YAWKYWDTDE RGGVYTWINY
PPAASHTLTN AFLAGRRNCN ISVGGRQYTV DFPSMSHRNA ESHIERPITI SGRLKDGAIL
SEILTEGNEH KEWDEVVHDR LVPAIIGLLG LANIDAASIH AIFILAARIT RDFKIAREFL
QQGGVQTMIN VSGAAVPSSA VLGALIIRHC LDDEISVRQI FEKTVRTIAA GGYTISPPLT
RWNHIRTPRT TRDWLHAIRA LSPLCARHPQ IFAATMERVT RKQNGQITVL PMTPVDPSCK
QWTACSPIKQ VLTHLLNHTL DFSWEDSNRV VNRASLVRLI AELAKSYSIV ATLVAESHDL
NGQPFMVSIL DKCIIPSGSP TADGSLYMAV KTFVAAIASC NHSPKAQETL ISSIISSLHI
VFCEANSKAA CTKLRLLADL FLLARDACPA GPQDMRNNTN SNAVLRLIIK KRVCIELSRV
PWYLNLSAKE GIETLNYVLR VLEELTRTIN SNHSAQNAVR ENMSESLSVT QNASASVTLV
ATSENDASVT VTAREGEHSQ DNQHVEDSSS TADEHRFETH EFQVTVERNR PDDDDYCADD
DEDRGRTRHP DAVEDSSESE EDEDDVDDDD DDEGAGLNEM DVDDESDDEH DDVMEEEGRV
SVEEEDDFGM VEIEPGALSR FTLVDSVDDS GPADRFEDGD SEENFVNTNI FVENLDDIDA
LTNGAFTGAR LFVNTSMEAA HADRSLATVS SVHPLLQRSS QTTGSDSVIG QRPTSYRLLV
GQRRGTGSMA STGLHRQNAV RRWTTFGTQS EFIERLLDGS TTANGSHLFD VAPSRQRFLN
VVMQDHGLDS TTTVTGEERR QTSVPLPLER FSDAARIIDG HAHLYLWVMV ASYITSVMDA
IEKDENEKKT EEEIMKTQKD FTEESSKRTL DDVTSNESSS TTRLFIDEEE HGDVGNVDDN
VADAQLEYSS ESVDITVQAP SVSEPMDQSG TLYYDTSESL ENQIHRTCEQ EQENITSNVN
SEISTDASVH TVLVTANEAE EQGNVEQLSA PEVTPEASLA NQDDFREILG DIEIPEGVDP
AFLAALPEDI RTEVIRDHIR QQRSQRLIQT SANLEAASQA NGEVPVVEPL DQEFLNALPP
DLQEEILAQH ERTVRLAQER VESNSVPTAD APVATDDAAA LIESLPPTLR AQVLADADDT
VLQVLPQNVA AEARRLRASY EAQQVMRFAR MLTPTQRFRP ANGRSVPGTS TSSTPVGALA
GVTTLASKNA TQLLDRDAIV TLLLLFFIDP ARLNTQRLQK LIKSLCAQNV TCDFVIWCLI
ALLDKVDEEA VQYEDFGGTV SGWLDQICVY SGIGQHEQAI KFFKSTHIVA LHPAVLATVC
RLVLDTLISL AKTYPGHFLP ANLRDPGYLS NAGLFTPPFS QFWAIVHSLS KADVLSRATH
RHGLSLETAL GPGGLNASMA AFSLEDSAIG VLMEHIKRPV ILSSSILQDK LLRLVCTIVQ
TLPEETITKL AIDSTAEKPP LSQQLEHIVL VLTEGDCSEE GLADGRTLLL ELIRALTPST
KTFIMSLLIN AAERLGARLL PHVEKLEEEL KELPNDGNPS SSVDQQPSGS KVAVNRYDES
VIVISGILNS RAVMNASGCY ELQLPAMKAL TDKSGIQNIF LRTLQTIIKI REVLQSHARC
IEIDVSTDTA GEQDDERGTG ENTANATEEY ERKRFAEKEE SMSVLLNTLE PLWELVSRCL
KRLTNADAHA ALALQPSAEA FFLVYGSELS SADPSKLHDH PDAQKLLHFA EKHRNMLNQV
LRQNGGGLTD GPFAVLTQMP KLLDFDVKRI YFRKQMQKID ERVRGEDVAV RIRRSHLFSD
SFRELFRLRG PEWKARFYII FEGEEGQDAG GLLREWFSII TREIFNPNYA LFITSPGDRV
TYMINKSSYI NPEHLEYFKF VGRIIAKAIY ENKLLECYFT RAFYKHILSV PVRAQDLESE
DPSFYKSLEF LLNNPIEDLG TELTFSLEVE EFGVRKMRML KENGSSVPVT DGNKEEYVKL
VCQMKMTGSI NQQLNAFLEG FYEIIPKHLI SIFNEQELEL LISGLPNVDI DDLYANTEYK
TYTKSSSQIQ WFWKALRSFE QEDRAKFLQF VTGTSKVPLQ GFAALEGMNG TQKFSIHLDS
RSSDRLPTAH TCFNQLDLPQ YETYDKLRDM LLLAVRECTE GFGFA
//
