ID V2XA47_MONRO Unreviewed; 365 AA.
AC V2XA47;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 41.
DE SubName: Full=Ubiquitin domain-containing {ECO:0000313|EMBL:ESK89641.1};
GN ORFNames=Moror_8612 {ECO:0000313|EMBL:ESK89641.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89641.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89641.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89641.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK89641.1}.
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DR EMBL; AWSO01000535; ESK89641.1; -; Genomic_DNA.
DR RefSeq; XP_007851043.1; XM_007852852.1.
DR AlphaFoldDB; V2XA47; -.
DR STRING; 1381753.V2XA47; -.
DR KEGG; mrr:Moror_8612; -.
DR HOGENOM; CLU_024293_0_1_1; -.
DR OrthoDB; 3177594at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR CDD; cd14399; UBA_PLICs; 1.
DR CDD; cd16106; Ubl_Dsk2p_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10677:SF3; FI07626P-RELATED; 1.
DR PANTHER; PTHR10677; UBIQUILIN; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 10..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 318..362
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 81..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 37649 MW; 059E15C388592401 CRC64;
MSDEPSSPEI QINVKGPNEL KLQIAIATDK TVAELKEAIA RQSDVPADRQ RLIYSGRVLK
DEDVLSVYKI QSTHTIHMVK GAARSGASSS STSQSSNGSQ PLPTMQSGQN PSDPLTQLNS
HMGFGAMAGL NPFADMGLNP NDPNMMQSMM SSPEVLQQMA AMMSNPAIVD QIIANNPQLA
SMGPQVREIF QSEGFRNMIS NPDTLRMMMN MSAAMRGGGS PLGGFGGGTG AFPAPGVPGG
GSTAGNATST DTNSNGNNNN GAPNLGANPF LNPAMMQQML SAMGGAGAGG AGGAGAGFNP
WMTGGFPSSP PPPADSRPPE ERFQVQLQQL QDMGFSNASQ NVRALLATGG NVHAAIEYIL
GGGGI
//
