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Database: UniProt
Entry: A0A067QQX7_ZOONE
LinkDB: A0A067QQX7_ZOONE
Original site: A0A067QQX7_ZOONE 
ID   A0A067QQX7_ZOONE        Unreviewed;       253 AA.
AC   A0A067QQX7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=L798_03017 {ECO:0000313|EMBL:KDR07296.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR07296.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR07296.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR07296.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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DR   EMBL; KK853480; KDR07296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067QQX7; -.
DR   STRING; 136037.A0A067QQX7; -.
DR   EnsemblMetazoa; KDR07296; KDR07296; L798_03017.
DR   eggNOG; KOG3002; Eukaryota.
DR   InParanoid; A0A067QQX7; -.
DR   OMA; FANEKSC; -.
DR   OrthoDB; 3184562at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000027135; Unassembled WGS sequence.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR004162; SINA-like_animal.
DR   InterPro; IPR049548; Sina-like_RING.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR   PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          70..131
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   253 AA;  29041 MW;  BF4385EE64988DFC CRC64;
     MENFNRDLNK DFLKELECAA CMELMLPPIH SCEYGHNICS TCKPTRTVCP SCRGPFVNIR
     NLALERMARN VKQRCTSRAF GCSEMCYLNF MTDHKAACAY APYTCPFANE KSCDWGDLYR
     NLKEHLLEKH SDYVTEQNDA TDLVMETGIR GLQERKFVFA YDEIFYTYIY ILQNNCCYFS
     VRYIGAPENA SKYGYKICFS KSNSIENIVV SQVTSSIAED IFAPGKGIML PCDLLKRFIV
     SGKLPYTLEI FQV
//
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