ID A0A1I7XI11_HETBA Unreviewed; 524 AA.
AC A0A1I7XI11;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_17126};
RN [1] {ECO:0000313|WBParaSite:Hba_17126}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. {ECO:0000256|RuleBase:RU201113}.
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=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU201113};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU201113}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000256|RuleBase:RU201113}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC interaction with substrate proteins. It is related to the TRAF family.
CC {ECO:0000256|RuleBase:RU201113}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}.
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DR AlphaFoldDB; A0A1I7XI11; -.
DR WBParaSite; Hba_17126; Hba_17126; Hba_17126.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095283; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd16751; RING-HC_SIAH1; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 1.
DR Pfam; PF00059; Lectin_C; 2.
DR Pfam; PF21362; Sina_RING; 1.
DR Pfam; PF03145; Sina_TRAF; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SMART; SM00034; CLECT; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU201113};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 82..117
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 263..374
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 413..513
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 59590 MW; 8F2ABB1719B8F76E CRC64;
MSCNQPPASS SCSSRSGSPP LPMQGIATPQ QKNLARVQAS APPVVTCSPS ALSTQSVAPQ
IATIGASEHT DSSAEVLSVF ECPVCLEYML PPYLQCQSGH LVCSNCRPKL QCCPTCRGPT
PSVRNLGLEK IANTVRFPCK FASSGCPLFF YHYEKVEHEE LCEYRITTLQ GEDIVFLATD
INLPGAVDWV MMQSCFGYNF MLVLEKQEKF DHGQQVFYAV VQLIGAKKEA DNFMYRLVER
ISFKPVTYEC HWLDQEFIIL KNLNFRCYYF NTNVTSFHEA DRSCAQLGYS LAFIDNAFVN
TFLQQHFEQT YTSYWIGLTS ENGLQWAWDD GEILTYTNWA PGEPRSGFYC AAENVHDGSW
ITVDFSVKLP SVCMRPNDFP STNSSRTSTL KSQQTTASTP GTRCPTNWFY YNTTGECYSF
YYWSDTNNHK WEEAEKACLK RNAHMLSIHS EIEQNVALDM WKNHWLIEST HFGIGLEYIK
KKKQWKWSDG SSYDYQGWLP DEPNVRKGMD LCAAGSFFII IQFK
//
