ID S8A0B4_PENO1 Unreviewed; 400 AA.
AC S8A0B4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=UBX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDE_09515 {ECO:0000313|EMBL:EPS34551.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34551.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34551.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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DR EMBL; KB644415; EPS34551.1; -; Genomic_DNA.
DR AlphaFoldDB; S8A0B4; -.
DR STRING; 933388.S8A0B4; -.
DR eggNOG; KOG2086; Eukaryota.
DR HOGENOM; CLU_029402_4_1_1; -.
DR OrthoDB; 5483331at2759; -.
DR PhylomeDB; S8A0B4; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR CDD; cd14348; UBA_p47; 1.
DR CDD; cd01770; UBX_UBXN2; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.420.210; SEP domain; 1.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR23333:SF20; NSFL1 COFACTOR P47; 1.
DR PANTHER; PTHR23333; UBX DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; NSFL1 (p97 ATPase) cofactor p47, SEP domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 204..268
FT /note="SEP"
FT /evidence="ECO:0000259|PROSITE:PS51399"
FT DOMAIN 319..386
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 46..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 42993 MW; E2D5DCD0E7FA3071 CRC64;
MDYNPAEHDE VVSQFCNMTG TKPSEAQEYL SANGWDVEAA VTEYFAEQDE ALQETETSAG
QRLGTEQAAS TAGGGRTLGG EPVSATSSAA PQAPSSSRRT APKKKFATLG DFATASAGDT
SSEDGSEDQD FFAGGEKSGL AVQNPDDLKR KILEKARRAQ PPSSEEPQSR PSHFTGTART
LGGDDAPSRV IEAPSEPQSQ RPQRVHRTLH FWADGFSVDD GELYRTDDPR NAEILEGIRQ
GRAPLTIMNV QAGQEVDVEL KQHEENYVKP KPKYKPFSGV GQRLGSPTPG VQSTQPSAST
ATTTPQASSS EPPKPKVDES QPTVTLQIRL GDGTRLTSRF NTTATIGDVY DFVTAASPDA
RSRGWVLMTT FPSKELSDKA VTLADLPDFK RGGVVVQKWS
//
