ID R0G1J6_9BRAS Unreviewed; 339 AA.
AC R0G1J6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CARUB_v10025552mg {ECO:0000313|EMBL:EOA29277.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29277.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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 RING-type zinc finger family.
CC {ECO:0000256|ARBA:ARBA00038033}.
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DR EMBL; KB870808; EOA29277.1; -; Genomic_DNA.
DR RefSeq; XP_006296379.1; XM_006296317.1.
DR AlphaFoldDB; R0G1J6; -.
DR STRING; 81985.R0G1J6; -.
DR GeneID; 17888748; -.
DR KEGG; crb:17888748; -.
DR eggNOG; ENOG502QQHB; Eukaryota.
DR OrthoDB; 901818at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd23127; RING-HC_BAH1-like; 1.
DR CDD; cd14482; SPX_BAH1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033326; BAH1.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46764; E3 UBIQUITIN-PROTEIN LIGASE BAH1; 1.
DR PANTHER; PTHR46764:SF2; E3 UBIQUITIN-PROTEIN LIGASE BAH1-LIKE-RELATED; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51382; SPX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..166
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT DOMAIN 235..284
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 339 AA; 39391 MW; CACD5A05318478F8 CRC64;
MKFGETFTEY LRGEEEWFLE KCRHVEYKKL KKVLKRCKTT CNSSTRSNND EQIIISSATS
LSDSSCQCQS CPWCDEMFFE ELMKEASDIA GCFRSRVRHL LHLHVATGMQ RYLMSLRRCF
KDEKQALLQE GQILIQYITM NAIAIRKILK KYDKVHSSVN GKKFKLKMRA ERIELLHSPW
LIELGAFYLN SGLDKVGNFK NSSFGRVSCE YLNDDQPMIQ LTLPNSIELE FDLTCAICLE
TVFNPYALKC GHIFCKSCAC SAASVMIFQG MKAAPKDSKC PICREVGVYA EAVYMMELHL
LLKIRSKEYW KERMVSERSE MVKQSKMFWN EQTKHMIGY
//
