ID A0A1Y2XDA7_9PEZI Unreviewed; 487 AA.
AC A0A1Y2XDA7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 02-APR-2025, entry version 33.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN ORFNames=K445DRAFT_35809 {ECO:0000313|EMBL:OTB19018.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB19018.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB19018.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB19018.1,
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC {ECO:0000256|ARBA:ARBA00044508}.
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DR EMBL; KZ112930; OTB19018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2XDA7; -.
DR STRING; 1001832.A0A1Y2XDA7; -.
DR OrthoDB; 1431934at2759; -.
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; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd23134; RING-HC_ITT1-like; 1.
DR CDD; cd23820; RWD_RNF14; 1.
DR FunFam; 3.30.40.10:FF:000416; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
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 Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 9..147
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 182..449
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 186..231
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 309..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 487
FT /evidence="ECO:0000313|EMBL:OTB19018.1"
SQ SEQUENCE 487 AA; 54520 MW; 4A2CE445A6C2A2D6 CRC64;
MAEDDVREVE LSTIAAIYPE LQIDENDPYK VSIELPVSLA SPVTVLFPAA TEGAPPVEPV
QDQIPTIAAV DSHSLSNLPS LQVHIELPEG YPQEKPPKVD ISTSPPWLSG DILRKLENDV
VVLWEEIGRD QVIFTYIDNL QQSSEKIFGL VDDEGRLEVS PEHKIAILDY DIKAKQKAFD
KETFECGICL DPKKGSVCHK MLDCGHVFCV QCLQDFYNNA ITEGDIASIQ CLEPNCAKER
EDAVKGSARK KKAKTFISPS ELLQIPLERD MVMRYAMLKH KNELESDKNT VYCPRSWCQG
AARSKKHKKP DGLEFVEASE EESDAEGTAE DDAETKDSDQ DLLAVCEDCG FAFCIRCAQS
WHGQFKYCVP KERKDEITEE EQASLEYLRM HTTPCPTCAA PCQKTHGCNH MRCFRCQTHF
CYLCSAWLDP SNPYQHFNVQ PSGKVNGCYM RLWELEGGDG GDVGIGFEGN AVRNRVAAPG
QYGQHLE
//
