ID A0A7K5JQ40_9TYRA Unreviewed; 242 AA.
AC A0A7K5JQ40;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 15.
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 Name=Siah3 {ECO:0000313|EMBL:NWS95940.1};
GN ORFNames=MIOMAC_R06378 {ECO:0000313|EMBL:NWS95940.1};
OS Mionectes macconnelli (McConnell's flycatcher).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Tyrannidae; Mionectes.
OX NCBI_TaxID=254557 {ECO:0000313|EMBL:NWS95940.1, ECO:0000313|Proteomes:UP000525714};
RN [1] {ECO:0000313|EMBL:NWS95940.1, ECO:0000313|Proteomes:UP000525714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-003-16 {ECO:0000313|EMBL:NWS95940.1};
RC TISSUE=Mixed tissue sample {ECO:0000313|EMBL:NWS95940.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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|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}.
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:NWS95940.1}.
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DR EMBL; VYZC01000048; NWS95940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K5JQ40; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000525714; 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: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 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 InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR008974; TRAF-like.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF5; SEVEN IN ABSENTIA HOMOLOG 3; 1.
DR Pfam; PF03145; Sina_TRAF; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP000525714};
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|RuleBase:RU201113}.
FT DOMAIN 134..228
FT /note="Seven-in-absentia protein TRAF-like"
FT /evidence="ECO:0000259|Pfam:PF03145"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWS95940.1"
FT NON_TER 242
FT /evidence="ECO:0000313|EMBL:NWS95940.1"
SQ SEQUENCE 242 AA; 27091 MW; 9D1F4239B462B875 CRC64;
MLFFTQCFGA VLDLIHLRFQ HYKAKRVFSA AGQLVCIVNP THSLQYAPTL CAAAQTSTEQ
GILPPCHHHE AVHDPQLVPC MCPLFSCPWE GHLEVVVSHL RQTHHINILQ GAEIVFLATD
MHLPAPTDWI IMHSCLGHQF LLVLRKQEKY EGHPQFFATM MLIGTPTQAD NFTYRLELNR
NQRRLKWEAT PRSVLECVDS VISDGDCLVL NTSLAQLFSD NGSLAIGIAI TTSKVHSSEA
EV
//
