ID V2YS63_MONRO Unreviewed; 615 AA.
AC V2YS63;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Chromatin-associated protein swi6 {ECO:0000313|EMBL:ESK94509.1};
GN ORFNames=Moror_7976 {ECO:0000313|EMBL:ESK94509.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94509.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94509.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94509.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK94509.1}.
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DR EMBL; AWSO01000130; ESK94509.1; -; Genomic_DNA.
DR RefSeq; XP_007846135.1; XM_007847944.1.
DR AlphaFoldDB; V2YS63; -.
DR STRING; 1381753.V2YS63; -.
DR KEGG; mrr:Moror_7976; -.
DR HOGENOM; CLU_019187_0_0_1; -.
DR OrthoDB; 1665016at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR CDD; cd18968; chromodomain; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR PANTHER; PTHR22812:SF112; FI06908P; 1.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 6..73
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 83..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..343
FT /note="Disordered"
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 143..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 67096 MW; 48CB31F7D32E6602 CRC64;
MGDEEYEVET ILRARVEKKT SRSKSVVWKY LVKWKGYDDP EENTWEPIES FEGSEHFVET
FWRKTGTGGR DREDLSLFEV GEELEPGSLE RKSSRKSLKS QEIPAPTSRA TSSKKRKREQ
IIPSESTNSR PERSRTRKRT RKTSHKDSPE PSVRRSSTDR DMSFELADTV AGGDAQYIPP
AAQTTADPQT GPAETERPPR YRKRGIGTSK TLPEDSVPEE PLHPESQSEN DDNGPSKTLI
PAHHARTENP LIKMIDEVDN MEGAISAKAR LFTKSAGQEL PSQMQSSLRK YPKPGPTSRI
SKKNTSSLLT AQKGKLTTVK GKYNVPTEGK PGQPSGSSNN PVVQEGSLAR EDVDTQIAGT
SIVAASNGTP ASSQELLQLA GADAVGDDEL KDYEDDVEDN SPAQSKRSNS LFQQSLAMAK
DKLFPASLTS ASLSRINAMT NVWRSTIFGP LSSPSTYPQT SLLLSNSGDE DVVPFFLNID
VSANVPIVLT KYPNSGSIPV NTPNDPPGKF YGKDAALAVL NTLRTGGPSA RVSLDANCTE
EQRQLFHQFM QKLAQDMLFV AMAGSDVLAF CSSSSVLISS RLNFPSALVS ASNVLVGRVT
IQDYSAYADV ALQGI
//
