ID K1WWN2_MARBU Unreviewed; 717 AA.
AC K1WWN2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 02-APR-2025, entry version 53.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=MBM_04509 {ECO:0000313|EMBL:EKD16932.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16932.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16932.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16932.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921437; EKD16932.1; -; Genomic_DNA.
DR RefSeq; XP_007292398.1; XM_007292336.1.
DR AlphaFoldDB; K1WWN2; -.
DR KEGG; mbe:MBM_04509; -.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_015887_1_0_1; -.
DR InParanoid; K1WWN2; -.
DR OMA; PWFNYET; -.
DR OrthoDB; 9977870at2759; -.
DR Proteomes; UP000006753; 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 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; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
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 286..477
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..211
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 81552 MW; 0AC239ECBB626BD7 CRC64;
MAKSSYAIDS KGRRRRRRGS HADEGAGDEW RVEDEVTRSC EAGRTEGRRR GRVVLVDRSE
RERLEDERRD GEKDEVVVES EIMPSESRET LRSKGRSGES YGKRRRDRGK GGGQAVEYVY
GPPKGKAGKP EKLRVRETRV LGRNGESSSS EEEIVEVRRS KTSRESPRKI KVVYATKEEG
KASKHKEPKV RTVREEDPVR RSRANTSRRK PVGVEAMPPS PPKRSATTRT MHSDIRALRR
SNTLTTHVPS TRHLSSAAES NPAMRRASFM GSFFGSGVPL HNEPEKLIEC LICLSDDIPR
SKSAKLKCGH RMCHSCLKRS FRLSVTDPAH MPPKCCSVEH IPLKHVEKLF NIEFKKTWNR
KFQEFSTKNR IYCPARRCGE WIKPANMHKE DGKKYGKCGQ CRTKVCCACN GKWHGARDCP
KDEETNRLLE TAKKAGWQRC YSCRTMVELK EGSEFCMICG LKWKTCDCPW FNYEAVEQDR
LNHMQIPRDL PIDGEAEDRP RRLRRPRPPN TYLEEITERQ RQERRDEALA RRMQRAIIAD
DHNDDYQGGI GDIHGVGNGA GHFMNQDYVR EAHNILTGNF DHARAAANYV MGVANARARP
PVAVRQMNDR YPGPPPPPVL RRHNVRDQAY NDAQPRAADR VVPRRSRGDY EAEAAVHDPS
GRDPFIPPSP RVSRTKVREP RPSVLAGLGG RGNRVSAWRS HVEPGVEPEE GVLSMVS
//
