ID A0A1A6GM07_NEOLE Unreviewed; 270 AA.
AC A0A1A6GM07;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN ORFNames=A6R68_04708 {ECO:0000313|EMBL:OBS66755.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS66755.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS66755.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS66755.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS66755.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) 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:OBS66755.1}.
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DR EMBL; LZPO01087185; OBS66755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6GM07; -.
DR STRING; 56216.A0A1A6GM07; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000092124; 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:UP000092124};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113};
KW Zinc {ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|RuleBase:RU201113}.
FT DOMAIN 162..256
FT /note="Seven-in-absentia protein TRAF-like"
FT /evidence="ECO:0000259|Pfam:PF03145"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 30286 MW; F8BFE50F192CE773 CRC64;
MLHDDNDDNG DGGGDDDGSG GCDDDDNVGG DGDCGNHLWT TNYIPLTQYV SSRRAITQNS
TEQGSFHPHH LPHHHRHHCH HNHLCHHARP RHLHHQEAGM HSAQVTPCLC PLFSCQWEGH
LEVVVPHLRQ IHRIDILQGA EIVFLATDMH LPAPADWIIM HSCLGHHFLL VLRKQERHEG
HPQFFATMML IGTPTQADCF TYRLELNRNH RRLKWEATPR SVLECVDSVI TDGDCLVLNT
SLAQLFSDNG SLAIGIAITA TEVRATDAEM
//
