ID A0A8T9BXN8_9HELO Unreviewed; 553 AA.
AC A0A8T9BXN8;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 02-APR-2025, entry version 13.
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 Name=itt1 {ECO:0000313|EMBL:TVY59610.1};
GN ORFNames=LSUE1_G009269 {ECO:0000313|EMBL:TVY59610.1};
OS Lachnellula suecica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=602035 {ECO:0000313|EMBL:TVY59610.1, ECO:0000313|Proteomes:UP000469558};
RN [1] {ECO:0000313|EMBL:TVY59610.1, ECO:0000313|Proteomes:UP000469558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 268.59 {ECO:0000313|EMBL:TVY59610.1,
RC ECO:0000313|Proteomes:UP000469558};
RA Giroux E., Bilodeau G.;
RT "Genome sequencing and assembly of the regulated plant pathogen Lachnellula
RT willkommii and related sister species for the development of diagnostic
RT species identification markers.";
RL Submitted (MAY-2018) 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};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TVY59610.1}.
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DR EMBL; QGMK01002286; TVY59610.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000469558; 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; 1.20.120.1750:FF:000061; RBR-type E3 ubiquitin transferase; 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; IPR054694; Parkin-like_IBR.
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; PF22605; IBR_2; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 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:UP000469558};
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 8..153
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 187..450
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 191..236
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..553
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:TVY59610.1"
SQ SEQUENCE 553 AA; 61254 MW; CAE278548DC41E90 CRC64;
MEDDERTVEL ECIQAIYPEI VLGPENPFSA TIELPVHPQN AVRVVFPASS DGALPTPPQS
DSSGQVDPAV APTNNVESHN LSYLPSLQLR IILPEGYPEE KPPKFEISTS PAWLSQTHLD
ELQNNGARIW EDEGRSATVY GFIDFLQQSA ENAFGFAEGK VLEIPQDLKI SLLDWDIKST
QAAFEKETFD CGVCLDPKKG SVCHQMLDCG HVFCVQCLQD FYNNAINEGD LASVRCLAPD
CAKKRGEAQV RSGRTRKPKT NLSPSELLQI PLEHNVVTRY VKLKHKADLE SDKNTIYCPR
TWCQGAARSK KHRKPVGLEI DTSDDESDTE DNGKKADFLS GNDLLSVCED CSFAFCSRCY
QGWHGEFVGC APKRDNGELT EEDKASMEYL QLHTTPCPTC AAPAQKTHGC NHMICFKCRS
HFCYLCSAWL SPVNPYQHYN TREAPCFMRL WELEEGDGDD VGIGYAGGLH RGQGAPEEII
EIPPEEPDIE ELEIVEMAND EVHAQPAQGP VDEAPQAALQ REGPLVLRIN QLPPQPAPVA
PAVPDAPQMG RRQ
//
