ID A0A1G4MKL0_LACFM Unreviewed; 538 AA.
AC A0A1G4MKL0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=LAFE_0H13102G {ECO:0000313|EMBL:SCW04419.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW04419.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCW04419.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW04419.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT598491; SCW04419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MKL0; -.
DR STRING; 4955.A0A1G4MKL0; -.
DR OMA; HRFCMIC; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000190831; Chromosome h.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 165..378
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 169..214
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 538 AA; 62073 MW; E7970436BB937F9E CRC64;
MLSEHTIPSD YDDEGDEFID FESYYSVEDT DLNGFKDDSD FDITSDMNSD DESGSRISFL
ISTQDSENLG KKSSLSGSEE RGLPKLNYNC LTTDQIYKLM LQRMENLQPI FNIPLEDMII
LLQRYGWSEE RLLEQWTEDM EKVLVASGLR TAKHDKIKRG IKLHPNFMCH ICCESGEKET
FSLECAHEYC LDCYKHYIQD KLPDGKIITC MNCDLALRNE DIDKIMGDNS SAKLMLSSIK
GFIQKHSNHY KWCPFVDCNY VIQVGNISSL SEFPRFHISP YVICDNKHKF CFQCGLESHA
PGDCQVADVW VKTAQAESAN LNWVLKNTKE CPKCGVNIEK NGGCNHMTCK SCAYEFCWIC
EGCWKDHGGS YYECTRFKKE DKNDNVESKG SLRKYTFYYR LFSEHENSAK LDWNLGQTVE
QKVRALQENV GISWIESQFL PESIRALIEG RTTLKWSFPV AFYSDPSHNL TKIFVDNQFL
LVNAVEDLSQ LLQIKEPKKI MEKKLDFYNK ARFVKSRENA LIECGRDLLC KGICIPQK
//
