ID G0NM03_CAEBE Unreviewed; 648 AA.
AC G0NM03;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 10-JUN-2026, entry version 78.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN Name=Cbn-siah-1 {ECO:0000313|EMBL:EGT33941.1};
GN ORFNames=CAEBREN_04931 {ECO:0000313|EMBL:EGT33941.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|EMBL:EGT33941.1, ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|EMBL:EGT33941.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT33941.1};
RG The Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EGT33941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT33941.1};
RG WormBase Consortium;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU201113};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}.
CC -!- SUBUNIT: Interacts with tir-1. {ECO:0000256|ARBA:ARBA00064073}.
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 EMBL; GL379908; EGT33941.1; -; Genomic_DNA.
DR AlphaFoldDB; G0NM03; -.
DR FunCoup; G0NM03; 2558.
DR STRING; 135651.G0NM03; -.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_4_0_1; -.
DR InParanoid; G0NM03; -.
DR OrthoDB; 941555at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd03829; Sina; 1.
DR FunFam; 2.60.210.10:FF:000002; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000652; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 1.
DR Gene3D; 2.60.210.10; Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
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 InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 1.
DR Pfam; PF21362; Sina_RING; 1.
DR Pfam; PF03145; Sina_TRAF; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW 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:PRU00455}.
FT DOMAIN 385..420
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 437..497
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 26..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..54
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..316
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71746 MW; DE5850278E14D619 CRC64;
MSNRNGGGGG GGDCQEVIDH LRRTQLFLDD DGSSSDTTPV VGSGGRGGAG GGGTTTTTSS
SGSGNTTNSS STTQSRHRLI QNNNNAVCGE EMSNNNHNSV ACSLTQPHME CTSFDREIFP
LLLHLFTFSV FEKLRLSKCP ALVRVSLLQT LPREPSPRMK IDLLRLFFAM LLFFNNRHMY
RKVYDDFPSV SFHHFSNASC FFSIVHHESS PSLSLFFMII KHISAIFLFF SLSTPFPPTK
TFNTMRSECC EIDLPAYFFH FIETLIDWGQ QWFLGNTPAV PPGITQCQNG MTQRMPSPTS
VMTPTPTVTS GTVQQGKTVG RIQGSNNSGS KKKHGSTSLQ KPEIVTVTHP PPTTTQAMQS
VSPHIPIVGA GADDSSAEIL SVFECPVCLE YMLPPYMQCP SGHLVCSNCR PKLQCCPTCR
GPTPSVRNLG LEKIANTVRF PCKFSNSGCQ LNFHHIDKME HEELCECRPY SCPCPGASCK
WQGALCDVMD HLKKVHKSIT TLQGEDIVFL ATDINLPGAV DWVMMQSCFD YNFMLVLEKQ
EKYDPAQNTQ MFYAVVQLIG SKKEADNFVY RLELSANRRR MSWEATPRSI HEGVAFAIQQ
SDCLAFDTNA AQLFAENGNL GINVTISRID TPPRRHPNEM DPTDVEYD
//
