ID   A0A1Y2XAM8_9PEZI        Unreviewed;       751 AA.
AC   A0A1Y2XAM8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   02-APR-2025, entry version 26.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=K445DRAFT_315372 {ECO:0000313|EMBL:OTB18537.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB18537.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB18537.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB18537.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112931; OTB18537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2XAM8; -.
DR   STRING; 1001832.A0A1Y2XAM8; -.
DR   OrthoDB; 9977870at2759; -.
DR   Proteomes; UP000243732; 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; cd22584; Rcat_RBR_unk; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732};
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          244..435
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          24..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          433..501
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        24..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  86885 MW;  56D8B8E8423694E2 CRC64;
     MLVIEPTSVV EDFSGASAIL VQHPEGDGEE FPKWKGKGKA VAGSINGESL PTGSPNNEVT
     VDWTEYELPE GLRDTANSKS DVVVQIIQES IDKVKARIAE EKERRKEDSA KKSKQNKKPV
     QEKEIQSIEI SDAPLDEKSE EQDVAIQTPA PALTRVESIN HNSIAPVQPV KSKKHSFRNL
     FRRLNNVGER GESSTTGAAR HRRDISWSSL EKSNYTSKRG LVSGVLRKTT TNSNGSPTSS
     VHGTEVECVS CLDDFNPKDM IKAPCHSYCK PCFLRLIRTA CDNEQQWPPK CCLNSIPSST
     IILNVDSELK KLYHDRGAEW DLPISERVYC NFAGCSLWLR PDQINRARNI ARCSTGHWTC
     IICRGPQHEG DACPEDRDMM KTDELAEEEG WKRCYGCHAY VEHREACQHM TCRCGAEFCY
     VCGARWRTCM CTMEQLAAVK RSAEERRQAR QDREAQEEAE IQEALRLVAE FEREEALKAE
     LLRKEQERLA EERRARLLEE RIRREGERRR AIEVKYLELR EVFVNVHELQ RIIVQRNHNT
     EETRLKSQGD TALEELQEKH KAERENLSTV TKAKLAKRER VLKREYAARV AEERHIEEQY
     HVQLKEYWSR KEDGEIKIEA AMKQLRRRMD ASFTKWEKWR NAELENYNWK VKEEQGIREE
     LMQEAERRLV DGTREAQTAF SLRKAAELRW VDVLIEERNR MLNDMEIDEI ESGENVDAWF
     EEGGLDEDEL DVTDLPAEFR LPITYEQYLN M
//