ID A0A091DBJ8_FUKDA Unreviewed; 267 AA.
AC A0A091DBJ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN ORFNames=H920_10749 {ECO:0000313|EMBL:KFO27863.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27863.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27863.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27863.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KN122849; KFO27863.1; -; Genomic_DNA.
DR RefSeq; XP_010635338.1; XM_010637036.1.
DR AlphaFoldDB; A0A091DBJ8; -.
DR STRING; 885580.ENSFDAP00000022044; -.
DR Ensembl; ENSFDAT00000010469; ENSFDAP00000022044; ENSFDAG00000007266.
DR GeneID; 104871195; -.
DR CTD; 283514; -.
DR eggNOG; KOG3002; Eukaryota.
DR OMA; AQVTPCM; -.
DR OrthoDB; 222086at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; 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 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 SUPFAM; SSF49599; TRAF domain-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113};
KW Zinc {ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|RuleBase:RU201113}.
FT DOMAIN 159..253
FT /note="Seven-in-absentia protein TRAF-like"
FT /evidence="ECO:0000259|Pfam:PF03145"
SQ SEQUENCE 267 AA; 30309 MW; 12220F268325086E CRC64;
MLFFTQCFGA VLDLIHLRFQ HYKAKRVFSA AGQLVCVVNP THNLKYVSSR RAITQSTAEQ
GGFHPHHLPH HHCHHHHHCH LRHHTRPLLL HHQEAGLHAT QVTPCMCPLF SCQWEGHLEV
VVPHLRQIHR VDILQGAEIV FLATDMHLPA PADWIIVHSC LGHHFLLVLR KQERHEGHPQ
FFATMMLIGT PTQAGCFTYR LELNRNHRRL KWEATPRSVL ECVDSVITDG DCLVLNTSLA
QLFSDNGSLA IGIAITATEV HSTEAEI
//
