ID A0A3B3WKU5_9TELE Unreviewed; 1139 AA.
AC A0A3B3WKU5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000003418.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000003418.1}
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR AlphaFoldDB; A0A3B3WKU5; -.
DR Ensembl; ENSPMET00000010890.1; ENSPMEP00000003418.1; ENSPMEG00000004700.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 501..534
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 687..720
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 940..1090
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 130..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 128255 MW; FDCD2D5C8491946A CRC64;
NCDSFLHQHS HCSKQRFNFV SLPTDVLEIE VKDKFAKSRP IIKRFLGKLS VPVQRLLEKH
AIGDRVVSYS LGRRLPTDHV CGQLLFRFEL TSSIHPDDEE ISLVMEPACN EVETPAEGNH
AADAADDDTL NVSLDMPDLP LDAPLDTDTS TPAAQSQDIP LTDQQEDSGA AEVEPGRVEE
QRASEEPNEK GESSCEPCSC QSLFSNCNFQ ALSRRKARPC SLPVSELETV IASACGEPET
PRSHYIRIHH LLHSLPSARP PSQEEEGEVT NITVDSHATS PTLKHSKEEE KDEEEEDTTQ
SPSQVKLDEL LEGEGGRGGL AVTRRISPSW LDSEEGDSNL EGGLRMCSRT HRPPGENECE
FCDTSCYSTS CYSTSCYSTS CYSNSGYEGR GRFCSHNRLS SVDSNRLSGS TVFSSQDEEE
DEESAFESVP NPVQPNSHDS GGDRGERMTG RWNEAKRGEQ GEPAEAGPSD KNCIDLSPPV
GHLPVLRPSH DPNHFPAATD PALPPNWEAR VDSHGRVFYV DHVNRTTTWQ RPSHGAKCNH
AIPRSGSTQQ MEQLNRRYQN IQRTMATEED SGSRSSDGES EPAQTGTSFT NLFHQQIMIL
FLFAVPSSPV NHQKITYLLQ SPAVKFISHP EFFTVLHSNY AAYRMFTSSS CVKHMILKVR
RDARNFERYQ HNRDLVVFLN KFADTQLELP RGWEIKTDPQ GKSFFVDHNS RATTFIDPRI
PLQNGQLPGH LAHRQHLQRL RSYSAGEASE VSRSRGASLM GRPSNSLVAA IRSHHQTDPK
QLTALSYNDK IVAFLRQPNI FDMLQERQPS LSRNHALREK VHCIRTEGTQ GVEKLSCDAD
LVILLSLYEE EIMSYIPPHP IHPGFSFSPR CSPASSPQSS PGLQRARAPA PYRRDFEAKL
RNFYRKLEAK GYGQGPGKIK LLIRREHLLE GTFNQVMAYS RKELQRNKLY VTFLGEEGLD
YSGPSREFFF LLSQELFNPY YGLFEYSAND TYTVQISPMS AFVENHLEWF RFSGRILGLA
LIHQYLLDAF FTRPFYKALL RLPTDLSDLE YLDEEFHQSL QWMKDNDITD ILDLTFTVNE
EVFGQVRTHL PASTKMYYVN NLLKDIHLEA GRVAGAYLQL TFRTRGGVHP GQVASLLQG
//
