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Database: UniProt
Entry: R0JMH2_ANAPL
LinkDB: R0JMH2_ANAPL
Original site: R0JMH2_ANAPL 
ID   R0JMH2_ANAPL            Unreviewed;       186 AA.
AC   R0JMH2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=Anapl_03027 {ECO:0000313|EMBL:EOA98306.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA98306.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
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; KB743525; EOA98306.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0JMH2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000296049; 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:UP000296049};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113};
KW   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:EOA98306.1"
FT   NON_TER         186
FT                   /evidence="ECO:0000313|EMBL:EOA98306.1"
SQ   SEQUENCE   186 AA;  20810 MW;  DC0CAA0BEDF43F05 CRC64;
     QYATTGCSLT LHHTEKPEHE DICEYRPYSC PCPGASCKWQ GSLEAVMSHL MHAHKSITTL
     QGEDIVFLAT DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YEGHQQFFAI VLLIGTRKQA
     ENFAYRLELN GNRRRLTWEA TPRSIHDGVS AAILNSDCLV FDTAIAHLFA DNGNLGINVT
     ISTCCP
//
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