ID A0A3M2S1R2_9HYPO Unreviewed; 700 AA.
AC A0A3M2S1R2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RMJ11448.1};
GN ORFNames=CDV36_008893 {ECO:0000313|EMBL:RMJ11448.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ11448.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ11448.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ11448.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RMJ11448.1}.
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DR EMBL; NKUJ01000167; RMJ11448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2S1R2; -.
DR STRING; 2010991.A0A3M2S1R2; -.
DR Proteomes; UP000277212; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 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 PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR Pfam; PF01485; IBR; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000277212};
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 10..151
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 186..460
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 190..235
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 309..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 77381 MW; 2E1277AAC528E560 CRC64;
MDESDDPRFM ELGSLEAIYP EIRHPDAKDP FAFEIELPVE PAAPVTVTFP AASAPAHPGL
NTPGQAAENG QPEVDSLEVS YLPSLRLQIR LPEGYPVDAP PKVQISTTPQ WLTKETIKRL
EDDGPRLWDE IGRDMVAFTY IDHIQRAAED VFGTITPEGT LEVDPEHKLA VLDHDIKSKK
AAFEKETFEC GVCLDPKKGS KCHKMLDCGH IFCIQCLQEF YNDAIKDGNL STVRCLAPNC
AKERAASKET KKPKVAVSPS ELLQIGLAED MVKRYVTLKY KTELESDKNT IYCPRQWCNG
AARSKRHKKP EGLDFAETSD AESEKEDEEK EGDNNAKKKK KKDIFNRADL LAICEDCGFA
FCGQCYQSWH GEFVRCAPRR DKGELSEEEK ASLEYLQLHT SPCPTCNAPA QKTHGCNHMI
CSRCDTHFCY LCSSWLDPVN PYQHYNQQPG GKVTSCYMRL WELEGGDGDD VGLGFIGGRG
PAQAQAQAQA QEPAAPLEVV EFESDDDSDN EDQGNAADAN QPQAQLGAQG QAIEVAREGP
LVIRLVDNHA RDGRRAVPPA APDAPQQPAA GRGHHGPLRG PAGRGRGARG GGRHQPAAPA
PRGRGRGRGG AARQRPNQQH QHQQHQPPAH HNQPQQQQQQ QQQQPVQNQG DNNNNNNNNQ
AGLDPAQEAW VRRFVQMALL DEEDLVEGDS DEEGDNWIIQ
//
