ID A0A1J7IQZ1_9PEZI Unreviewed; 888 AA.
AC A0A1J7IQZ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=CONLIGDRAFT_631697 {ECO:0000313|EMBL:OIW29619.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW29619.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW29619.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW29619.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KV875097; OIW29619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IQZ1; -.
DR STRING; 1408157.A0A1J7IQZ1; -.
DR InParanoid; A0A1J7IQZ1; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..888
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011955862"
FT TRANSMEM 406..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 818..882
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 506..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97363 MW; 502D05B5A53F0B80 CRC64;
MPQPQENARA FIVIILIFWL ITSPDNNPGL IGVPSLTAAR LERQRRAHGV LNSTKWGDFS
PRLIDDQADA TPHYLNLTGF REQDGFAWED FGRFKDRCTD WSRNAHGSSK TGENLWDLGL
AEPMWQNVTG VVHGEWARRN GSVERQAASY NLSDIAPTVP WMPTRADFSH NVTGQHGKIT
LYLDDKNDSV EYEDRNGDNG PKAGGLARAI SASVTMQDDA TSSSSWDMKF HGVHWPRQGA
ILLTSTSEKF AGIFALPHLT LGPNFFYSSQ KLLNETLDTV LRKKEKARFS DPSNPWASNI
EPEGQNWSPS PHCEYLLYVQ VHPLNPSRLG IKHFGGNPQE NLGISLVKAL ENELRNPTGA
PVKGYPELRM STVMWSPDCS YFLESKGPPV FASVEGNHLT GKKEEILIYG GKMWLMAFAA
VFLGQVYLLK AQMRESSTPS TVGRVSFYTA GTMLLADGLI FAASSAWSLS ASSTLLPSLL
MTFGAFLSMA LGGVFLGEVY KVQEPERRNR QREQAAANQS PPTPAAAAAA AATARAATAA
PAPPPPPPPP SDSLPRPVTA APLRPATPPI IIPSDQDIDA EIAANVAAGA AAVPTPGIRP
AVTVTAPQQQ RTPFSSISGR FILLGTLLLF ISVAAISWPA RIRAFYCNLL AFIYFSLWVP
QIYRNIIRNS RRAYSWRFMI GQSVLRAAPI AYFYLREDNI LFAKTDPLAF AVLAGWLWIQ
LWVLAFQDVL GPRYGIPKGW APEAWDYHPV LREDNLESGG LPIGLVAGAD DDEPGSPVTR
RASVSEGNKS TRKALDKDRG KDRKDGKSIR AHIHEIDCAI CRETLEVPVV PAGADPDAVG
AGGSVAATLA RRTYMVTPCR HIFHSACLEG WLRFRLQCPI CREELPPL
//
