ID A0A0A2JTU3_PENEN Unreviewed; 258 AA.
AC A0A0A2JTU3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Chromo domain/shadow {ECO:0000313|EMBL:KGO58834.1};
GN ORFNames=PEX2_091890 {ECO:0000313|EMBL:KGO58834.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO58834.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO58834.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO58834.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO58834.1}.
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DR EMBL; JQFZ01000110; KGO58834.1; -; Genomic_DNA.
DR RefSeq; XP_016600175.1; XM_016746459.1.
DR AlphaFoldDB; A0A0A2JTU3; -.
DR STRING; 27334.A0A0A2JTU3; -.
DR GeneID; 27681879; -.
DR HOGENOM; CLU_045874_0_1_1; -.
DR OrthoDB; 5490924at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0000792; C:heterochromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR CDD; cd00024; CD_CSD; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR PANTHER; PTHR22812:SF112; FI06908P; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 51..134
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 29732 MW; B832CA73EB731318 CRC64;
MPPPVEDMSD EESGDIPFRK ESETNGKDDQ DPPEDEGDEE EDEEEEEEGL YIVEDIIKHD
WLDDGTLKLW VKWKGYERVQ DHTWEDEEGL MYVDMLIELR NLLRAFIDEH HRDGASEVVT
AYYKRIGGRP KKDEEKPAAA KPGRKRKSMG EPKLAKDSPA PAASEVKRQR RKSAPKETNK
QASPSSEENG IQWLPKGKNW DKDVKEVDTI VREGDAGLMA WLEFNNGHKA KLSVQACYEK
CPLKMLKFYE SHLVFKDN
//
