ID E5A9F3_LEPMJ Unreviewed; 1569 AA.
AC E5A9F3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 28-JUN-2023, entry version 55.
DE RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
GN ORFNames=LEMA_P014240.1 {ECO:0000313|EMBL:CBY00294.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929138; CBY00294.1; -; Genomic_DNA.
DR RefSeq; XP_003843773.1; XM_003843725.1.
DR STRING; 985895.E5A9F3; -.
DR EnsemblFungi; CBY00294; CBY00294; LEMA_P014240.1.
DR GeneID; 13293222; -.
DR eggNOG; ENOG502S6DU; Eukaryota.
DR HOGENOM; CLU_001892_0_0_1; -.
DR InParanoid; E5A9F3; -.
DR OMA; THSIEHI; -.
DR OrthoDB; 1881880at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR CDD; cd00024; CD_CSD; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.40.50.12360; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR038609; HDA1_su2/3_sf.
DR PANTHER; PTHR22812:SF112; CHROMATOR, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR22812; CHROMOBOX PROTEIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 101..142
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 43..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1326..1357
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1456..1483
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 54..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1569 AA; 171190 MW; 6FDE1E81CB53C201 CRC64;
MHARHSVQAG TALARLTPSL GPRVQHAFTS LYFTNHVGNH QFSFHPSDQS LGVMEGTKRK
RASTRDKPEK RPKYTDSSDL EADSQTQIQA KGQNNEDDNL WLAEAILDEK VEKKTQKYLV
QWEGLDPRTG VPWEPTWEPR QNCTDLLLAS WEIEKTKKGW TDRTTGKGTG RRGKARSRTT
DRERPVQLKL HLSHKAAVPA TSPSPSTSRS TTSDIWPSTP EAHSIIHEAS LASSAATSPV
RVGAGLDART SPHQSPRITI LRRGSSFDAE EYEHYSQLAT SQSQPQSQSQ SQSQSQSTNL
DSSQLIAATC APSYPYSSGS IIPDSQDSAG EASFLPATQH SEDSNQQSTA TTDLQEAEDD
EDADSGILEI IQQGVLGGLS PARSIAETIP DSNTVGYSQG PIEISGSNTQ TQVVIEVSDS
SATTSEGQSQ GIQGSSQGGN LHVQKHQQEE PQAHQGPMHR SESACGSIVP QSSHNPEDPS
TILDETVQSV IQVPHTQSQD EIIPNRPAQD IDSWIEEPLG QENGGQAVVT QSSASAVELN
LGDGHTQFPF QSQHPLRHSQ DFQNSHEALD EEVNEVAGGG VPSLSSAEAS ATSVALPPRQ
VTLAPGALAT AFGETNAPSS LSHVKPHQPG PTALGLIPLA EAQEKLLLKK LATRESPSSP
SSGVAQVELR GAERNNTTSQ ATQRSHSVSG IIPRGTFARQ SQPPHSTEPS TASRERIAQV
VPFETDLGTQ EDITESIEIT VEEYQVAERG SSPSRHDSSQ DSPERLRSEC SSSPIFNPPN
FSLATVASKL PSRPSTPLPT SSPKMSGESA GDQVKRALQE ALEKKRAENP FTPSRRLARR
FNANMTPASA SPSAASVSAR RLLGANASPV GNDGTRSPSA VPDHAPVPPA PTSLSAVIAP
PSNDVPETLG EDANKEISVQ PLPTTADVEV LVEANPELPS EDSRDVEVND ADDEDSESLL
DDDLQLEPDE YIIPLFIEGR QLDMYTAHIQ QHKELLQQFL KDPLGFTPLS KAEEVLSYLR
AIETHVDLVF AEAEWSSIGE SATQVEFTAQ FGMENSVKFR FLHAFFHRLR EYEKHVVLVI
ADDNDALFHI IEIFCKAKCI NYSMPTRGHQ ADIMSTVGNM SVTIIPSSAT PVIRAPDVIL
CLDGMQEAAK IRQKNWAQSP TRENVPVFHL VIPRTVGHIE RYVSKSLSHP DQLHTIVAGL
AQMSVNAEIG QPVDEATQRA SVLAGMAVDW LVAGDNGDPC SLPSIGSIKD VIEYQTQVLY
SQELTTPPAP ERNKRPLDDE DLDSAKRMRY TPQPHNTSSV NNDQEVTHVS DSMPGTAANL
NGTAIESNLR RQLARMEEAL QEKLQMWERQ LTEHEDLRRE HRIVIDHDRA TEAKLEAATK
NLEITRDRLL TRTAESNEKS RQLDEQRATD ALSTDEKTAE ITRLRQELAT AHLERTRAVN
DCNSANALLE YTKEARRAAE QSLSAAQATI QQLTAENEKL TYQASGQAAK LKALHLDRQT
SNLTRQLQSV RNENVILKKA LAQKEEELLR AKNGRQGVGT RMQSVTPQPK TRSRAGSPLG
GRFSNLRKE
//