ID A0A0J9YHD2_GEOCN Unreviewed; 527 AA.
AC A0A0J9YHD2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE SubName: Full=Similar to Saccharomyces cerevisiae YDR330W UBX5 UBX (Ubiquitin regulatory X) domain-containing protein that interacts with Cdc48p {ECO:0000313|EMBL:CDO51216.1};
GN ORFNames=BN980_GECA01s02562g {ECO:0000313|EMBL:CDO51216.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO51216.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO51216.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO51216.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCBN010000001; CDO51216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9YHD2; -.
DR STRING; 1173061.A0A0J9YHD2; -.
DR OrthoDB; 5482878at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR CDD; cd02958; UAS; 1.
DR CDD; cd14348; UBA_p47; 1.
DR CDD; cd01767; UBX; 1.
DR Gene3D; 6.10.300.40; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR23322; FAS-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23322:SF6; UBX DOMAIN-CONTAINING PROTEIN 7; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50033; UBX; 1.
PE 4: Predicted;
FT DOMAIN 446..524
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 46..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58973 MW; DB263F371E7834D8 CRC64;
MDQSELIEQF CAITASDAET AERYLAVADQ NLEAAITLFL EGGGQSFASQ QQPPQSNVGS
GPTVSAGSSV GAGAIDEDDE ALVRRLQQEE YNSTDNDGVR EAIRPVTETL VEPGYGGAGF
GSRYRAPPVQ RPRDIFGRDR GLDSDDEDDY GYSRGSSSRH RIDNDYYNDN DDEEEEANDV
DTGMTPAQSR LSKLFRPPYD LISNYDLETA KDYGRLQKKW LLVNIQNSTE FQSHVLNRDI
WANSSIKTLV KNHFVFLQYN HDSYEGQDFK SYYPFEQYPY VGILDPRTGE QMKAWSFQLP
PADEFLDQLR EFLATFSLDP KANNPMSRQK QDVSRMTEED QIKYALKKSL GGAESSDDDI
IELDGSDDDF QDFDEDDEYV VDSDVEILDA PVGSSGSGSS KTIAANDDVQ EASAPQEEES
EEEEDLTEED IFAMIPPHEY PEPPAGVPDT TRIQFRLGDG TRVIRRFELS NTVKQVFGVV
KTINDVTRTS YFSLTKGDTK ENLLSKLDQT IKEAGLSNNS ILVEILD
//