ID A0A443RKT3_9ACAR Unreviewed; 1079 AA.
AC A0A443RKT3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=B4U79_03598 {ECO:0000313|EMBL:RWS15862.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS15862.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS15862.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS15862.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS15862.1}.
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DR EMBL; NCKU01000348; RWS15862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443RKT3; -.
DR STRING; 1965070.A0A443RKT3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000285301; 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 GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
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; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF320; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00632; HECT; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 227..260
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 490..523
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 742..1079
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1047
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1079 AA; 121803 MW; D80EC213B93CE6C4 CRC64;
MEYMLHTSSS SSTSSSDIPP PLPPKQKLGK TPLRTQHKPL ERTGPILERI QCLPPPSLES
AARNDECDNE SPPPTPPLRQ RNTRPVNPLS PEREEMQETA RREQPLTPAA PVSETDDAVN
SEAIESCSSS SSSPDPVNDE SDNSDNNEQR EESAPPRPPH HAPLLRSPPP INSVIPKPLQ
RRTFSTVGSS SSITARNGLR PGDAATITRL PSIPEKTVRY QKVDIEEPLP PHWEARIDAH
RRIFYIDHVN RITTWSRPSL QQYQQQQQQK QLNPNMVANL NDDISQHRQQ LDRRYQSIRR
TITSKSSQNK SVGSSSTSNN DFSSNGTIDA SEPGCSSQPD GLTVTDSSTD LAESVETVDS
PTMPSVSSPE GISAPSTTTT TTTIITPTST TSTVSATSST NTTNLTPTAS TTSESTSSQQ
LPPALRFLTR PDFFNLLHLN DEALAQYNQS SSLKHMITKI RKENSRAYFE RYQHNRDLVS
LINKFAERDR SLPPGWETKT DRNKKPFFID HSTRSTTFID PRLPVEMPIV NPHHIVMAPS
RRRCRTPNDI EINQNTNSPI PPPRPPTTSS SSATVVTPQV PTAYSDKVVA FLRQPNIFDI
LKERRPQISS NQSLRDKVNA VRVDGTLALD RYSCDLELTI LLSLFEQEIM SYVPCSPPSG
AVGGVPQTNP LSPQASPNVQ RSIRVPQTAH SPYRRDFEAK LRNFYKKLEQ KGYGQGPNKL
KLNIRRDHLL EDAFTKIMSA NSKKDLQKSR LYISFVGEEG LDYGGPSREF FFLLSRELFN
PYYGLFEYSA NDTYTVQMSP MSAFVDNAQE WFRFSGRVIG LALVHQYLLD AFFTRPFYKA
LLRLPCSLSD LEYLDSEFHQ SLLWLKDNDI SDMDLDLTFS VIEEIAGQVV EKELKPGGKS
MPVTERNKKE YIDRMVKWRL DRGVEEQNES LVKGFYEVID PRLVSVFDAR ELELVIAGTA
EIDVVDWRKN TEYRGGYHDS HPVIQWFWAA IEKKFDNERR LRLLQFVTGT SSIPYEGFSA
LRGSNGPRKF CIEKWGKPSS LPRAHTCFNR LDLPPYYSFD MLYEKLLLAV EESSTFGIE
//
