ID A0A0A0AW30_CHAVO Unreviewed; 906 AA.
AC A0A0A0AW30;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=N301_02673 {ECO:0000313|EMBL:KGL98774.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL98774.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL98774.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL98774.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; KL873469; KGL98774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AW30; -.
DR STRING; 50402.A0A0A0AW30; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
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; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
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; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..98
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 334..367
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 366..399
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 441..474
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 481..514
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 572..906
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 142..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 158..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 874
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL98774.1"
FT NON_TER 906
FT /evidence="ECO:0000313|EMBL:KGL98774.1"
SQ SEQUENCE 906 AA; 102867 MW; 3E263686AABC48C3 CRC64;
QCILLVSSAK LKRKKNWFGT TFYTELTADG EIKKTAKSSS SSNPKWDEQL TVNVTPQTTL
EFRVWSHHTL KADALLGRAT VDLRQALEIH NRKLEKVKEQ LKLSLENKSG MVQTGELTVV
LDGLVVEQES LTNLSSSATI EVQQNGEAVH ESRDASARST SRSACDISNG IDNQVPSNSV
VQNTFCIEAV NGDSAPSPTH VAARPKNTPV PKPLAAQPID STVNGESSTS APEAGNSSVS
EAPIGSVEAP VSSDCTNTTA EPQSTTEATS CSESHTSALP AVSAGLEPTA ATDCAQPNAR
NSTAADAAKP RESSSSSSAA AEPVRQQPGN AGTEPLPPGW EQRKDPHGRT YYVDHNTRTT
TWERPQPLPP GWERRVDDRG RVYYVDHNTR TTTWQRPTME SVRNFEQWQS QRNQLQGAMQ
QFNQRYLYSA SMLSAENDPL GPLPPGWERR VDSNDRVYFV NHNTKTTQWE DPRTQGLQNE
DPLPEGWEIR YTREGVRYFV DHNTRTTTFN DPRTGKSSVN KGPQIAYERS FRWKLAHFRY
LCQSNALPSH VKINVSRQTL FEDSFQQIMA LKPYDLRRRL YVIFRGEEGL DYGGLAREWF
FLLSHEVLNP MYCLFEYAGK SNYCLQINPA STINPDHLSY FCFIGRFIAM ALFHGKFIDT
GFSLPFYKRM LSKKLTIKDL ESIDTEFYNS LIWIRDNNIE ECNLEMYFCV DMELLGKVTS
HELKSGGSNI LVTEENKEEY IGLMAEWRFS RGVREQTKAF LDGFNEVVPL QWLHYFDEKE
LEVMLCGMQE VDLADWQRNT VYRHYTRNSK QIIWFWQFVK ETDNEVRMRL LQFVTGTCRL
PLGGFAELMG SNGPQKFCIE KVGKETWLPR SHTCFNRLDL PPYKSYEQLK EKLLFAIEET
EGFGQE
//
