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Database: UniProt
Entry: A0A3Q3VMW9_MOLML
LinkDB: A0A3Q3VMW9_MOLML
Original site: A0A3Q3VMW9_MOLML 
ID   A0A3Q3VMW9_MOLML        Unreviewed;      1496 AA.
AC   A0A3Q3VMW9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000003046.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000003046.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   STRING; 94237.ENSMMOP00000003046; -.
DR   Ensembl; ENSMMOT00000003094.1; ENSMMOP00000003046.1; ENSMMOG00000002448.1.
DR   OMA; TAGQHRE; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd08691; C2_NEDL1-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 2.60.40.150; C2 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; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037795; C2_HECW.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR040524; HECW1_helix.
DR   InterPro; IPR032348; HECW_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF18436; HECW1_helix; 1.
DR   Pfam; PF16562; HECW_N; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          187..318
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          732..765
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          909..942
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1161..1496
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1464
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1496 AA;  166409 MW;  681C59BB9A44A0CC CRC64;
     MAATASSSSS SPSASSSANG SAREQLLAVR RRTPHSRPYT IGPDNLRSLS AQGDQPEATG
     VALPRANSDT DLVTSDSRSS LTASTYQLTL GHSHLVISWD IKEEVDATDW IGLYHIDETC
     VANVWDSKNR GVNGTQRGQI VWRLEPGPYF MEPETKVCFK YYHGVSGALR ATTPCITVKN
     PGVLVGSEGQ VEDQSGTEHC RKLVSFTLSD IRAVGLKKGM FFNPDPYLKM SIQPGKRSGL
     PKFTHHGQER RSSIIANTTN PVWHGEKYTF VALMNDVLEI EVKDKFAKSR PIIKRFLGQL
     IIPVQRLLEG DQPVSYSLCR RLPTDHVSGM LLFRVDITST GQEEASPDAV GTILGGAVNG
     DPGSPSDDED LPHPSSSSRV TCGASPTGSD EGSIIVNGAC YYGEDSVWRE PGQMGEESQL
     PVALGSHTHR QVSLNDYLDA IETPRSPGDR PLVGPLPKLR SSFPTDTRLN AMLHIDSDED
     EESAGQHREQ SQEARTQQSA DLSGSESSKA EPQRQTGATT EAGSSGSEPS GPEPGDQTQG
     STAGTAEAPQ ATGGTSTAST SSQVSEGEAA TAAPGSGASM EECTRQEQRR DAPCTSSLGP
     LSPIQVSSCT VRILECKYFH LQYFPPFQEV ETNKEVAPKA EEEGAESSSS EANGPVAGNP
     RTISVNADRG GGTPEVGRLK LLPFQGDATG LPTSHFDAII FACATAQVNG HQSVRSSPSV
     RHEISRYQRV EEPLPPNWEA RIDSHGRIFY VDHVNRTTTW QRPTAPPAPQ TLQRSNSIQQ
     MEQVRPYQSI RRTITSDNRL EEQPANELPA DETDAQPSIP ELRRDNSVAQ SSSRSRLTLL
     LQSPSAKFLT SPDFFTVLHS NPGAYRMFTT NTCLKHMISK VRRDAHHFER YQHNRDLVAF
     LNMLANKQLE LPRGWEMKHD HTGKPFFVDH NCRATTFIDP RLPLQSTRPP SLLAHRQHLT
     RQRSHSAGEV SEDPRHAGPP VLPRPSSTLT SASRGQCQDV VPVAYNDKIV AFLRQPNIFE
     ILQERQPDLS RNHSLREKVQ VIRTDGGSGL ARLSGDADLV MLLSLFEDEV MSYVPPHALL
     HPSYCQSPRG SPVSSPQNSP GTQRANARAP APYKRDFEAK LRNFYRKLET KGYGQGPGKL
     KLIIRRDHLL EDAFNQIMCY SRKDLQRSKL YVSFVGEEGL DYSGPSREFF FLVSRELFNP
     YYGLFEYSAN DTYTVQISPM SAFVDNHHEW FRFSGRILGL ALIHQYLLDA FFTRPFYKGL
     LRIPCDLSDL EYLDEEFHQS LQWMKDNDIE DMLDLTFTVN EEVFGQITER ELKPGGANIP
     VSEKNKKEYI ERMVKWRIER GVVQQTESLV RGFYEVVDAR LVSVFDAREL ELVIAGTAEI
     DLSDWRNNTE YRGGYHDNHI VIRWFWAAVE RFNNEQKLRL LQFVTGTSSI PYEGFASLRG
     SNGPRRFCVE KWGKVTSLPR AHTCFNRLDL PPYPSFSMLY EKMLTAVEET STFGLE
//
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