ID A0A2K6STP0_SAIBB Unreviewed; 1247 AA.
AC A0A2K6STP0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=NEDD4 {ECO:0000313|Ensembl:ENSSBOP00000010746.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000010746.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000010746.1}
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010344427.1; XM_010346125.1.
DR AlphaFoldDB; A0A2K6STP0; -.
DR Ensembl; ENSSBOT00000027524.1; ENSSBOP00000010746.1; ENSSBOG00000022142.1.
DR GeneID; 101028535; -.
DR CTD; 4734; -.
DR GeneTree; ENSGT00940000158905; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233220; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 538..571
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 695..728
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 768..801
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 820..853
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 912..1246
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1214
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1247 AA; 140366 MW; C1EDFBFE04AB7B29 CRC64;
MAQSLRLHFA ARRSNTYPLS ETSEDDLDSR VHMCFKRPTR ISASNIVQMK LTPRQTALAP
LIKGNVQSQE RSSVPSSENV NKKSSCLQIS LQPTRYSGCL QSSNVLADGD DASFTCILKD
GVYSSVVTDN ELNAVNDSNL LSSPAICSGS LSNFSASDNG SYSSNGSDFG SCTSITSGGS
YTNSVISDSS SYTFPPSDDT FLGGNLSSDS TSNRSVPNRN TTPCEIFSRS TSTDPFVQDD
LEHGLEIMKL PVSRNTKIPL KRCSSLVIFP RSPSNTPPTS PTSPCTLLSK GSYQTSHQFI
ISSNEIAHNE DGTGAKGFLS TAVNGLRLSK TVYTPGEGRD IRPLHRKGLL QKKIVISNNT
PKQTACEKSS EGYSCVSVHF TQQKATTLDC GTTNGDCKPE MSEIKLNSDS EYIKLMHKTS
ACLPSSQNID YEINISGELE RPDSQMNKSH GILQRSISLG GAYPNISCLS SLKHNCSKGG
PSQLLIKFAS GNEGKVDNLS RDSNRDCTNE LSNSCKPGWV VLDQPDAACH LQQQREPSPL
PPGWEERQDI LGRTYYVNHE SRRTQWKRPT PQDNLTDAEN GNIQLQAQRA FTTRRQISEE
TESVDNRESS ENWEIIREDE ATMYSSQAFP SPPPSSNLDV PAHLAEELNA RLTIFGNSAT
SQPVSSSNHS SRRGSLQAYT FEEQPTLPVL LPTSSGLPPG WEEKQDERGR SYYVDHNSRT
TTWTKPTVQA TVETNQLTSS QSSAGPQSQA STSDSGQQVT QPSETEQGFL PKGWEVRHAP
NGRPFFIDHN TKTTTWEDPR LKITAHLRGK TSLDTSSDLG PLPPGWEERT HTDGRIFYIN
HNIKRTQWED PRLQNVAITG PAVPYSRDYK RKYEFFRRKL KKQNDIPNKF EMKLRRATVL
EDSYRRIMGV KRADFLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT
DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM MLHKPITLHD
MESVDSEYYN SLRWILENDP TELDLRFIID EELFGQTHQH ELKNGGSEIV VTNKNKKEYI
YLVIQWRFVN RIQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVNDWREHTK
YKNGYSANHQ VIQWFWKAVL MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQLFTVE
QWGTPEKLPR AHTCFNRLDL PPYESFEELW DKLQMAIENT QGFDGVD
//
