ID A0A3B4B0M4_9GOBI Unreviewed; 1039 AA.
AC A0A3B4B0M4;
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 Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000022161.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000022161.1}
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 AlphaFoldDB; A0A3B4B0M4; -.
DR STRING; 409849.ENSPMGP00000022161; -.
DR Ensembl; ENSPMGT00000023603.1; ENSPMGP00000022161.1; ENSPMGG00000017936.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261520; 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; 2.
DR Gene3D; 2.20.70.10; -; 2.
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; IPR040524; HECW1_helix.
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; PF00632; HECT; 2.
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 301..334
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 479..512
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 731..1039
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1007
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1039 AA; 116656 MW; B30DF9FD182DBCEB CRC64;
MLDGAVNGDP GSPSDDEDLP HASSSSGVAG GASPTGSEEG SLLVNGACYY DDVWAEPGHS
RRDGDVTAMG RHTHRQVSLN DYLDALEAQR NAQERIAMGP SPKLRSSFPT DTRLNAMLHI
DSDEEEEEET EAGAGDQSVT TETEASGGPA EEEEETQEGT IATTVNAAAS AVADESSPSG
SGEAEGGDVP SSSPQPEGAE GGAAASADSR PVVKLSVRWR QSRRPPQTLV HVAFIKRAFH
LDVFRRVDNM NLFVGARAGQ SSRAEQEEQA GSGTAQVNGH QSVRTLPSVH HDISRYQRVD
EPLPPNWEAR IDSHGRIFYV DHVNRTTTWQ RPTAPPAPQT LQRSNSIQQM EQLNRRYQSI
RRTMTNDSRP EEQPANEILS DETDMQPSTG DLRRDTGLAP SGSRSQLNLL LQSPSAKFLT
SPDFFTVLHS NLSAYRMFTA NTCLKHMISK VRRDAHHFER YQHNRDLVAF LNMFANKQLE
LPRGWEMKQD HTGKPFFVDH NSRATTFIDP RLPLQSSRPP SLLAHRHHLT RQRSHSAGEA
GEDPRHPGPP VLPRPSNTFT SSSRGQCQDV VPVAYNDKIV AFLRQPNIFE ILQERQPDLS
RNHSLREKVQ LIRTDGVSGL ARLSGDADLV MLLSLFEDEV MSYVPPHALL HPSYCQSPRG
SPVSSPQNSP GTQRANARAP APYKRDFEAK LRNFYRKLET KGYGQGPGKL KLIIRRDHLL
EDAFNQIMCY SRKDLQRSKL YVSFVGEEGL DYSGPSREFF FLVSRELFNP YYGLFEYSAN
DTYTVQISPM SAFVDNHHEW FRFSGRILGL ALIHQYLLDA FFTRPFYKGL LRIPCELSDL
EYLDEEFHQS LQWMKDNDIE DMLDLTFTVN EEVFGQITER ELKPGGANIP VTEKNKKEYI
ERMVKWRIER GVVQQTESLV RGFFEVVDAR LVSVFDAREL ELVIAGTAEI DLSDWRNNTE
LRLLQFVTGT SSIPYEGFAA LRGSNGPRRF CVEKWGKVTA LPRAHTCFNR LDLPPYPSFS
MLYEKMLTAV EETSTFGLE
//
