ID K1XN52_MARBU Unreviewed; 266 AA.
AC K1XN52;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Heterochromatin protein one {ECO:0000313|EMBL:EKD13924.1};
GN ORFNames=MBM_08125 {ECO:0000313|EMBL:EKD13924.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13924.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13924.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13924.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH921448; EKD13924.1; -; Genomic_DNA.
DR RefSeq; XP_007296014.1; XM_007295952.1.
DR AlphaFoldDB; K1XN52; -.
DR STRING; 1072389.K1XN52; -.
DR GeneID; 18764060; -.
DR KEGG; mbe:MBM_08125; -.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_045874_0_0_1; -.
DR InParanoid; K1XN52; -.
DR OMA; LMAWLEF; -.
DR OrthoDB; 5490924at2759; -.
DR Proteomes; UP000006753; 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 CDD; cd18657; CSD_Swi6; 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; SM00298; CHROMO; 2.
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:UP000006753};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..266
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003855531"
FT DOMAIN 81..132
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 21..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 29023 MW; 3F7F4923A5E7E340 CRC64;
MMTAIAALFG IGLPCAEISD DEASEVSSND YAPAAPIRVK PEKNSKSKSK TPVDDPEPEP
VAAVESDGGD DDEEELAEDE YTVEAITNHF VDEDTGVLRF EVKWLGFEKK SDRTWEPEEN
LFETASEILD KYLSSVGGKE AILAAWEERK AEAGTGKKGK KRGRTSAGEK TNGTKKGRKS
KEHPASGTPP LSATSAEFKP PGGTWEDAVI AIDACEGNDS NVVVYLTWKG GHKTQHPLAQ
VYKRCPQKML AFYESHLVFK KNDDLS
//
