ID A0A3Q4HAW5_NEOBR Unreviewed; 4055 AA.
AC A0A3Q4HAW5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HUWE1 {ECO:0000313|Ensembl:ENSNBRP00000020225.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000020225.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000020225.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 STRING; 32507.ENSNBRP00000020225; -.
DR Ensembl; ENSNBRT00000020767.1; ENSNBRP00000020225.1; ENSNBRG00000015437.1.
DR GeneTree; ENSGT00940000156319; -.
DR OMA; ADEMKYG; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000015437; Expressed in blood and 9 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; IPR018123; WWE-dom_subgr.
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; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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:UP000261580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1314..1353
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1599..1678
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 3719..4055
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 711..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2239..2295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2342..2418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2634..2664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2692..2716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2740..2763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3156..3181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3201..3257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3337..3356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3422..3442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3467..3522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3575..3613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2260..2274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2277..2292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2634..2653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2745..2763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3167..3181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3206..3257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3575..3592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4022
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4055 AA; 447678 MW; A9CB3140B081773C CRC64;
MKVDRSKLKK TPTEAPADCR ILIEKLKACN DEQLLVELQH IKTWNIGKCE LYHWVDLLDR
FDGILCDAGQ TVENMSWLLV CDRPENGQLK ALLLAVLNFT ALLIEYSFSR HLYSSIEHLT
TLLASCDMQV VLSVLNLLYV FSKRSNYITR LGSEKRTPLL ARLQHLAESW GGKENGFGLA
ECCRDLPMTK YPPSATTLHF EFYAEPGPEV KVERKTSSNT LHYIHIEQLD KISESPSEIM
ESLTMMYNIP KDKQTLLFTH IRLAHGFSNH KKRLQAVQAR LHAISILVYS NALQESANSI
LYNGLIEELV DVLQITDKQL VDIKAASLRT LTSIVHLERT PKLSNIIDCT GTASYHGFLP
VLVRNCIQAM IDPLMEPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG
DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFICRL EHEVDLSRKE CPFVIKPKIQ
RPSAAVESED MDTDMESMQC IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL
KHIISNAEYY GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV
LGSLPNVFSA LCLNARGLHS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD PLGDTASNLG
SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRAPEYICQ KPSIQKADGT VAVPPARSSH
AAEEASSEDE EEEEALHTFS QQQGEAESSR QVVGTEERIP IPLMDYILNV MKFVESILSN
NTTDDHCQEF VNQKGLLPLV SILGLPNLPI DFPTSAACQA VAGVCKSILT LSHEPKVLQE
GLCQLDSILT SLEPLHRPIE VPGGSVLLRE LANAGHVTDA TLSARATPLL HALTAAHAYI
LMFVHTCRVG QSEIRAISVN QWGSQLGLSV LSKLSQLYCS LVWESTVLLS LCTPNSLPPG
CEFGQADMQK LVPKEEKPSG NTTATSASGS RRTGNAVSVD SSAGGLLEGM GLDGDTLAPM
ETDEPSAADP KTKSKLTPAM ATRIKQIKPL LSASSRLGRA LAELFGLLVK LCVGSPVRQR
RSHHATSTGT TPTPAARATA SALTKLLTKG LSWQPPPYTP TPRFRLTFFI CSVGFTSPML
FDERKYPYHL MLQKFFCSGG HDALFETFNW ALSMGGKVPV SEGLEHADLP DGTGEFLDAW
LMLVEKMVNP STVLDSPHSL PAKMPGVTPT MPQFSALRFL IVTQKAAFSC IRNLWNRKPL
KVYGGRMAES MLAILCHILR GEPVIQERLA KEREGTVRGP ADDSTNSTPR REPQVNQAQL
TQLMDMGFSR EHAMEALLNT STMEQATEYL LTHPPPLLGG AVRDLTMSEE DQMMRAIAMS
LGQEVSMEQR SDSPEEAARR REEEDRRARE RAEEEEARCL ERFMEAEPLD PQELHAFTDT
MLPGCFHLLD ELPDTVYRLC DLLMTAIKRS GPEYRDLILG QVVQQVWEAA DVLIKAAEPL
TTSDTKTVSE WTRQMATLPQ ASKLATRILL LTLLFEELKL LGARVIENSG ILDLLIKLLE
VVQPCLQAAK EHKDIQTPKW ITPVLLIIDF YEKMAVSSKR REQMNKYLQP NGNNWRWFDD
RSGRWCSYSA SNNSTIDSAW RAGESSVRFT AGRRRYTVQF NTMVQVNEET GNRRPVMLTL
QKVPRIPKPS KTGSVTDSER EESDRGKVEE NQSDLDSGTS DYSQGSDIVV QGLTEDMTTV
LIRACVSMIS VPVDPDTLHA TLRLCLRLTR NHHYAMMFAE LKSTRMILGL TQSSGFNGFT
PLVTLLFRHI IEDPATLRHT MEKVVRSAVT SGAGSTTSGV VSGSLGSREI NYVLRVLGPA
ACRNPECFTE TASNCIRIAL PAPRGAGTTS DDEFENLRIK GPNAVQLVKT TPLKLSPLPP
IPDTIKEVIY DMLNALAAYH APEEPVPGGQ DLCQILQDVG DDVYQQYRLT RQGSDFDSQS
AFHINSQVFA ADGGVAESSQ SGTPQGEAST PEEMREEKKE QEGEKGTTSD ESKAAKVKAS
KPLMPTSTIL RLLAELVRSY VGIATLIASY CYTAGQSELI KEDCSVLAFV LDHLLPHTQN
SEDKDTPALA RLFLASLAAA GTGTDAQVSL VNEVKAALSR ALAMPEGAEK HARLQAVMCI
ISTIMESCPS TSSFYSTAAA KTQHNGMNNI IRLFLKKGLV NDLARVPHSL DLSSPNMANT
VNAALKPLET LSRIVNQPSS LFGGKGGSSK NKTEHDPVGT ARDSNSNTQD QGESGEAEPV
DGSHRVQGTD TDLMDGETEG DAVVIAGQPE VLSTQAMQVE NELVDLIDEL LERDAGTVNS
TIIDSMNILE PEDEEHTQEE DSSGSNDDED SQDEEEEEEE EEEEDQVEDD EEGDEDDDDE
GSEMELDEDF PDINAAPHIR FERFDRDDDL IIEFDNMFSN NADIPPSPGN IPSSHPLMVR
HADHGSLTLG VAGTSSRLAQ GMGRSQRTLR QLTANSGHTI HVHYPHNRQP NPPLILQRLL
GPSAAADILQ LSSSLPLQSR GRARLLVGNE DVHIIARSDD ELLDDFFHEQ SSTGGQAGTL
SSIPTALTRW TDECKVLDAE SMHDCVAVVK VPILQHLESL RDEELEERRE KRRRQLAEEE
ESKQNERRAS GAEQAREQSL QVSISLPEGV DPSFLAALPE DIRREVLQNQ LGIRPPSRPP
AATSLPASTA PVLGGPGVTE VSPEFLAALP PAIQEEVLAQ QRAEQQRREL AQQPPQGDTP
LDPVTFIQTL PSELRRSVLE DMEDSVLAVM PPDIAAEAAA LRREQEARQR QLMHERLFGH
SSSSALSAIL RSPAFTSRLG SNRGVQYTRL AVQRGGTFQM GGGTNHRPSS SSVDSLLRLR
GRLLLDHEAL SCLLVLLFVD EPKLNTSRLH RVLRNLCYHS QTRGWVIRSL LSILQRSSES
EVCVETSRLE DSRGKRTSQG SSSSLELLNR VESRSSSQLS WLSVSMDAAL GCRTNIFQIQ
RASGRKHADR HSAGGSTVHI HPQAAPVVCR HVLDTLIQLA KVFPSHFTQQ RCKDLSASSS
DLDSRLCSGI STDFWDLLVK LDNMNVSRKG KASMKTVPLG GSAEAEGAQF SLETSPLGQL
MNMLSHPVIR RSSLLTEKLL RLLSLISIAL PDNKATEVPA GHPTPQAPNP NTATSSGATA
SVTTQGTAAV GAMQSTVAGP GASVGAVAQG TSSGTSIATS QTSSTTISIP TSTGTISTGS
GKQRGAVSNT ESEKLASTGL TEKQLQLSVE VLTSHSCSEE GLEDAANILL QLSRGDASTR
DTVLRLLLSG ARHLGYTLCK QIGTLLAELR EYNLEQQRRA QADSHSPDAP PEDSSISARL
KGKMTSRFDG SESVVIVAAQ KRTLGGRELQ LPCMSSLTSK TSTQKFFLRV LQVIIQLRED
TRRANKKAKQ TGRLGSTSLG SASSIQAAVR QLEAEADAII QMVREGQRAR RLQQAPPPTA
PSASAASAQR DDSPMDVDQP SPLEQDPAPL EGNGQSESEE RLPDLPLLSE QLLLDELWDM
LGECLKELEE SHDQHAVLVL QPAVEAFFLV HATERESKPP VRDTRESQLS HIKDEPPPLS
PAPLTPATPS SLDPFFSREP SSMHISSNLP PDTQKFLRFA ETHRTVLNQI LRQSTTHLAD
GPFAVLVDYI RILDFDVKRK YFRQELERLD EGLRKEDMAV HVRRDHVFED SYRELHRKSP
EDMKNRLYIV FEGEEGQDAG GLLREWYMII SREMFNPMYA LFRTSPGDRV TYTINPSSHC
NPNHLSYFKF VGRVVAKAVY DNRLLECYFT RSFYKHILGK SVRYTDMESE DYPFFQGLVY
LLENDVSTLG YELTFSTEVQ EFGVCEVRDL KPNGANILVT EENKKEYVHL VCQMKMTGAI
RKQLAAFLEG FYEIIPKRLI SIFTEQELEL LISGLPAIDI DDLKANTEYH KYQSSSIQIQ
WFWRALRSFD QADRAKFLQF VTGTSKVPLQ GFAALEGMNG IQKFQIHRDD RSTDRLPSAH
TCFNQLDLPA YESYEKLRHM LLLAIQECSE GFGLA
//
