ID R9A9M0_WALI9 Unreviewed; 535 AA.
AC R9A9M0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=J056_002834 {ECO:0000313|EMBL:EOQ98797.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ98797.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR EMBL; KE007251; EOQ98797.1; -; Genomic_DNA.
DR RefSeq; XP_009270374.1; XM_009272099.1.
DR AlphaFoldDB; R9A9M0; -.
DR STRING; 1299270.R9A9M0; -.
DR GeneID; 20375786; -.
DR KEGG; wic:J056_002834; -.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_4_1_1; -.
DR OMA; HRFCMIC; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000014064; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 147..365
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 535 AA; 61382 MW; 3515428097475715 CRC64;
MSDDSDNYMD AASFEGSDIV EDYQSSNPSE AFSDDDVEIE DNEAFIVNEP VKPKKSKFDV
DYKVYDINDI ISNQQSETEQ VCSIFGLQRQ DATILLRHFG WNREKLIERY SEDPERILKQ
VGLAPGTSAS AQSDSRANSP VRLKRVKGFT CEICFTGSED TSTQTLALAC GHRFCSDCWK
MHCEEKISGQ GESRKIECMQ GDCQTVMSEQ VISQVVPEYI FQRYQTLANK TYVEDNRRGL
RFCPGPDCGN VIECQVRGSD LESLIPIVVC KCGQASCFGC SFSGDHRPAL CGVTKLWVKK
CEDDSETANW ISANTKECPR CHSTIEKNGG CNHMTCRKCR HEWCWICMGD WSAHGTSYYN
CNRFEDKSGK DARDGQQKSR VSLERYLHYY NRFSNHEQSA RLDQELYAKT ERKMDEMQRS
TSLTWIEVQF VKKAVETVTK CRMTLKWTYA MAYYLDRNSM TELFEDNQAD LEKAVENLSE
LLEKPLDVET IPELRSQMQN ATNYVKSRQN ILLEDTLQGH MEDRWSYHIT IPSLA
//
