ID A0A1V6TV71_9EURO Unreviewed; 466 AA.
AC A0A1V6TV71;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CENP-T/Histone H4 histone fold domain-containing protein {ECO:0000259|Pfam:PF15511};
GN ORFNames=PENSTE_c002G09580 {ECO:0000313|EMBL:OQE29780.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE29780.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OQE29780.1}.
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DR EMBL; MLKD01000002; OQE29780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TV71; -.
DR STRING; 303698.A0A1V6TV71; -.
DR OrthoDB; 2730181at2759; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR22980:SF5; CENP-T_HISTONE H4 HISTONE FOLD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22980; CORTISTATIN; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT DOMAIN 358..465
FT /note="CENP-T/Histone H4 histone fold"
FT /evidence="ECO:0000259|Pfam:PF15511"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 51073 MW; 4F085E4EF781C180 CRC64;
MSTPNPRNRL RDVGSATPSG DTTLTGLQRL PSHTRYPLTP RRLVTTATPS GQRSASRFTP
RGRPSIAPST PYGRNARQQR AANTPGRDRR RSGRVQRETT FDILRNLGRT LAPVTKPIQS
SPQEEIKSPP KPRDEIEELD EESETEPPEL TLPIQEVEGS EEGSTARSPP RLSLAFDEDD
ITYQSVEYPR RDTSIRDQER MSIMSRNFGR PSDVFADNQS DSDADVGDET AIVEDDGADD
TMISGGDFDR GGETADLGRF DLVMDFPSPG AMPIEDEVGN NLDETDGFEL SAGEIQPAPI
SPPPPGNDDV NDNVDDGLDF GLNFQPAASP SEHSGIVGGG LRDEDPSTRG KQKQISRHGI
PVPTLPKGIV KKLATRFAGT KAGSKTRINK PALEAIEQAS AWYFEQVSQD LAAYSKHAGR
KTIDESDVAT LMKRQRHVNK STTIFSLAQK HLPRELQQDM RLAMPP
//
