ID A0A1L7XVN5_9HELO Unreviewed; 505 AA.
AC A0A1L7XVN5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 02-APR-2025, entry version 31.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=PAC_19013 {ECO:0000313|EMBL:CZR69112.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR69112.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR69112.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR69112.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
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; FJOG01000065; CZR69112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XVN5; -.
DR STRING; 576137.A0A1L7XVN5; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000184330; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330};
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 202..416
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 206..262
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 86..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..190
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 57268 MW; 98B57EC4CC001780 CRC64;
MASNDGQRLT VLGLSFRQHH TLHMQQVLRA YERLPENPMD RAALYTGLFQ LAKNLDEDET
KNIEHWLLHG GEFPAPTPKV SEATEKVLDR TSEVDSDEEE DWPEYRPEDF EDDGEAVRDP
MEEDDDEDED HDGVPHTSHI TGEAESENSG SGSMEGHDGD LSEEGSEQDS EDEPEARPRR
PSGRPRRRPA VAKSSKGKSA AESLECLICA ESYLLTEFPP STEVTSTCNH KNNERTCIYC
LQQSIESAVT DGQLNLIVCP FCPEKLSREE IKKYATPEIF ARYDYLALIA TPDLVMCLGL
NCGSGQIHTS EDPMMTCQAC SFKTCAFHKL PWHEGQTCEE FDTNDDQIER LEQAEATAML
LAKEHAQVCP NCGNGVSRTE GCDHMTCRCG HEWCYLCGTS YENMKRLGDE AHAPTCMYHP
RRVQMRRDQE RKVQGHLTEL IHGGPVSETL ERARGARNER VRAELRPKAA EAAERRMREM
DQQNKENKVP EKKRRLNLKP AWEEK
//