ID A0A087XS56_POEFO Unreviewed; 1553 AA.
AC A0A087XS56;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HECW2 {ECO:0000313|Ensembl:ENSPFOP00000008609.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000008609.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000008609.2}
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}.
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DR EMBL; AYCK01022853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01022854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000008609; -.
DR Ensembl; ENSPFOT00000008621.2; ENSPFOP00000008609.2; ENSPFOG00000008113.2.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000155466; -.
DR OMA; TAGQHRE; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 170..301
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 788..821
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 966..999
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1217..1553
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 329..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1521
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1553 AA; 173161 MW; A62F9C8FC0F4C01D CRC64;
SNSSAHEHLL AVHRRAPHSR PYTVGLDNLS SLSVQITAGS SAGLGLQRAN SDTDLVTSES
RSSLTASTYQ LTLGQGHLVI SWDIKEEVDA TDWIGLYHID ETCVANVWES KNRGVNGTQK
GQVLWRLEPE PYFMEAETKI CFKYYHGISG ALRATTPCIT VKNPGVPVRS EGQVEEQSGS
EHCRKLVSFT LSDIQAVGLK KGMFFNPDPY LKMSILPGKR SGLPKFTHHG QERRSTIIAN
TINPVWHGEK YTFVALMSDV LEIEVKDKFA KSRPIIKRFL GHLIIPVQRL LEGPTTVTQI
QVSYNLCRRL PTDNVSGQLQ FRVDITSTGQ EEASPDAAGG SLLGSGDPGS PSDDEDLPQA
SSSSRVTSGP SPMDSDDGPL LVNGLCCYGE NIMWREPGRV GENDLPSVAP GQHTHRQVSL
NDYLDALEAP TGHGDRLLVP PLPKLRSSFP TDTRLNAMLH IDSDEDEDSV GQHRDLSQNT
RAEQSTDSVS RSPAQNEDLK EDVGAGAEEG SSSAVQLPAE PPNARNEVAE DEGGNEACAL
TRALVDGAEG SAGAAQATEE MAVFSSQKPG TEAAAADLQG DSVPQCSCQE QSSRMGTCSP
SLGPLSPIQV SKSSESKPHM TKYHDVNAAG GGAERSVRKQ TSTNQTSCRQ EVEARKELAP
KAEEEGAESS SSEANGPVGA SAPNSSRDDI ADVTSVPPNR EKGMRAEGGN KEGGQKGTDV
WRRQSMQTSA DQAQNQQKEQ GSSGERQGTP ETCCIFNAGA TAQVYGHQSV RSLPSVRHDI
SRYQRVDEPL PPNWEARIDS HGRIFYVDHV NRTTTWQRPT APPAPQTLQR SSSIQQMEQL
NRRYQSIRRT ITNDSRQEEQ PANELLGDET DMHPSVPELR RENGAAQASS RSRISLLLQS
PTAKFLTSPD FFTVLHSNPS AYRMFTTNTC LKHMISKVRR DAHHFERYQH NRDLVAFLNM
FANKQLELPR GWEMKHDHSG KPFFVDHNCR ATTFIDPRLP VQSSRPSLLS HRQHLTRQRS
HSAGEVGEET HHPGPPVLPR PSSTFTSASR GQCQEVVPVA YNDKIVAFLR QPNIFEILQE
RQPDFSRNHV LREKVQLIRT DGVSGLTRLS GDADLVILLS LFEDEVMSYV PPHALLLPSY
CQSPRGSPVS SPQNSPGTQR ANARAPAPYK RDFEAKLRNF YRKLETKGYG QGPGKLKVTI
RRDHLLEDAF NQIMCYSRKD LQRSKFYVSF VGEEGLDYSG PSREFFFLVS RELFNPYYGL
FEYSANDTYT VQISPMSAFV DNHHEWFRFS GRILGLALIH QYLLDAFFTR PFYKGLLRIP
CDLSDLEYLD EEFHQSLQWM KDNDIEDMLD LTFTVNEEVF GQITERELKP GGGNIPVSEK
NKKEYIERMV KWRIERGVVQ QTESLVRGFY EVVDARLVSV FDARELELVI AGTAEIDLSD
WRSNTEYRGG YHDNHIVIRW FWAAVERFNN EQRLRLLQFV TGTSSIPYEG FASLRGSNGP
RRFCVEKWGK ITSLPSRAHT CFNRLDLPPY QSFSMLYDKL LTAVEETSTF GLE
//
