ID A0A3B4D5W0_PYGNA Unreviewed; 1284 AA.
AC A0A3B4D5W0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000018304.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000018304.1}
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}.
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DR RefSeq; XP_017560525.1; XM_017705036.1.
DR STRING; 42514.ENSPNAP00000018304; -.
DR Ensembl; ENSPNAT00000027433.1; ENSPNAP00000018304.1; ENSPNAG00000024688.1.
DR GeneID; 108431704; -.
DR CTD; 619412; -.
DR GeneTree; ENSGT00940000158905; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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; IPR035892; C2_domain_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 535..568
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 688..721
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 806..839
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 857..890
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 949..1283
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 9..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1251
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1284 AA; 144038 MW; 64F40A5BA8129284 CRC64;
MARRLRLHFA TRRSNTDPLS ETLSHGTEDG LGIPARSPAD GPYILNSFHM KVTPGQLALA
LPPLSPDYGS LQRHTTVFVP KVNSGGGSKK STLQISLQPG SKQNGDIEIN GSGGDEMDAV
TCDGGAGASS DGGSCSSSTA SDVGYCSSSS IFESDVLERK AAHDRGVCRR KARAPLRRCS
SLVIFPRSPC TTPPASPVSP MASPLIPPLP PSARGSFQTS HQLQLSAADA SQDEVQPKVS
VASAVNGLRL SKSSCPPAEF RDAKPILHFS VPVEPLPSSE QSERHSSVLL HYANQPPLPP
GKGNRTVVNV DCSKPPEQSE EANVKPANRN PKLYRSTSAC GLPRPKISTE KRHHTCPTIG
KSAVLQDFHR GLQRSISLEV PCSNAGISCR MSNTKQLGSM NGMAHVHIHV SRGSGAKVSD
SPKDAWTIDQ RDQTLTFSGE TTTTRDDFLG QVDVPLHQIP TEAPGSERPY TFKDFLLHPR
SHKSRVKGHL RLKMTYLPKN GSEEEQAEQP EELDPSWEFL ESQEMCGPRH PHQLPALPPG
WEERQDNLGR TYYVNHENRT TQWHRPTMQD AQREAEQRQS THTQHPFITR RQISEHEESS
DRRESPESWE IITEDDGTLY SSQSQVSPPP PHSPLDYTSF CEEFCRLQTG NERRTSLTPQ
GHGSRRGSAQ MLTVEEHPVH PVMLPTTPGL PPGWEEKQDS KGRVYFINHN SRTTTWTRPL
VQLIQPSEAG ATGAGGATGY RCQSPTIYVP PLLSSDASPL HSPAPLYSPG AHHSPGPHHS
PGPHHSPGPQ HSPGPHAHTH TFEYAGCMPV GWEVRSAPNG RPFFIDHNTK TTTWEDPRLK
IPAHMRRRPS LDPNDLGPLP PGWEERIHSD GRIFYIDHNT KTTQWEDPRL QNSAITGPAV
PYSRDYKQKY EYFRKKLKKP ADIPNRFEMS VRRNALLEDS YRCILSTKRT DLLKARLWIE
FAGEKGLDYG GVAREWFFLI SKEMFNPYYG LFEYSATDNY TLQINPNSGL CNEDHLSYFK
FIGRVAGMAV YHGKLLDAFF IRPFYKMMLQ KPITLQDMES VDSEYFNSLK WILENDPADL
DLRFTIDEEL FGQTHQHELK PGGADIIVND SNKKEYIHLV MQWRFVNRIQ RQMTAFKEGF
YELIPQDLIK IFDENELELL MCGLGDVDVN DWRENTKYKN GYGANQPVIQ WFWKTVLLMD
AEKRIRLLQF VTGTSRVPMN GFAELYGSNG PQLFTIEQWG TRDKLPRAHT CFNRLDLPPY
ESFEELREKL NIAIENAQGF DGVD
//
