ID A0A093HJY4_STRCA Unreviewed; 184 AA.
AC A0A093HJY4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
DE Flags: Fragment;
GN ORFNames=N308_14199 {ECO:0000313|EMBL:KFV82046.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV82046.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV82046.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV82046.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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. {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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU201113};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, 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 EMBL; KL206408; KFV82046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HJY4; -.
DR STRING; 441894.ENSSCUP00000014792; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; 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; cd03829; Sina; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF4; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR Pfam; PF03145; Sina_TRAF; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU201113}; Zinc {ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455,
KW ECO:0000256|RuleBase:RU201113}.
FT DOMAIN 1..55
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV82046.1"
FT NON_TER 184
FT /evidence="ECO:0000313|EMBL:KFV82046.1"
SQ SEQUENCE 184 AA; 20593 MW; DA0BF413A165D756 CRC64;
QYATTGCSLT LHHTEKPEHE DICEYRPYSC PCPGASCKWQ GSLEAVMSHL MHAHKSITTL
QGEDIVFLAT DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YEGHQQFFAI VLLIGTRKQA
ENFAYRLELN GNRRRLTWEA TPRSIHDGVA AAILNSDCLV FDTAIAHLFA DNGNLGINVT
ISTC
//