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Database: UniProt
Entry: H1W5G6_COLHI
LinkDB: H1W5G6_COLHI
Original site: H1W5G6_COLHI 
ID   H1W5G6_COLHI            Unreviewed;       448 AA.
AC   H1W5G6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Chromatin modification-related protein {ECO:0000256|RuleBase:RU361213};
GN   ORFNames=CH063_04266 {ECO:0000313|EMBL:CCF47730.1}, CH63R_01082
GN   {ECO:0000313|EMBL:OBR15902.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF47730.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF47730.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF47730.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [3] {ECO:0000313|EMBL:OBR15902.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR15902.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(2017).
CC   -!- FUNCTION: Component of an histone acetyltransferase complex.
CC       {ECO:0000256|RuleBase:RU361213}.
CC   -!- SUBUNIT: Component of an histone acetyltransferase complex. Interacts
CC       with H3K4me3 and to a lesser extent with H3K4me2.
CC       {ECO:0000256|RuleBase:RU361213}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU361213}.
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC       {ECO:0000256|RuleBase:RU361213}.
CC   -!- SIMILARITY: Belongs to the ING family. {ECO:0000256|ARBA:ARBA00010210,
CC       ECO:0000256|RuleBase:RU361213}.
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DR   EMBL; CACQ02010078; CCF47730.1; -; Genomic_DNA.
DR   EMBL; LTAN01000001; OBR15902.1; -; Genomic_DNA.
DR   RefSeq; XP_018164419.1; XM_018296057.1.
DR   STRING; 759273.H1W5G6; -.
DR   EnsemblFungi; CCF47730; CCF47730; CH063_04266.
DR   GeneID; 28860164; -.
DR   KEGG; chig:CH63R_01082; -.
DR   VEuPathDB; FungiDB:CH63R_01082; -.
DR   eggNOG; KOG1973; Eukaryota.
DR   HOGENOM; CLU_031900_7_0_1; -.
DR   OrthoDB; 3140066at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 1.
DR   GO; GO:0000785; C:chromatin; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   CDD; cd16858; ING_ING3_Yng2p; 1.
DR   CDD; cd15505; PHD_ING; 1.
DR   Gene3D; 6.10.140.1740; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR028651; ING_fam.
DR   InterPro; IPR024610; ING_N_histone-binding.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10333:SF100; CHROMATIN MODIFICATION-RELATED PROTEIN YNG2; 1.
DR   PANTHER; PTHR10333; INHIBITOR OF GROWTH PROTEIN; 1.
DR   Pfam; PF12998; ING; 1.
DR   SMART; SM01408; ING; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU361213};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR628651-51};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR628651-51};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          389..438
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          141..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT   SITE            391
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT   SITE            402
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT   SITE            406
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT   SITE            414
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ   SEQUENCE   448 AA;  48331 MW;  357046A23BA4A5F6 CRC64;
     MPRDDLSIDF VKRMPTAEAL DPAIILDDWL NRVQNLPEEI RFLQDEIADR DRQYCDCVKL
     IEDRDGKIQK WIRANGSHET NPREETMRSQ MRDNFIRADT LATEKIALTQ KLQIIMDKHL
     RNLDQHIKML YDRAEPGFND PDECPSLIRP SAANHSAPSG RSVNPASHLV GTAITATPLN
     PIVNSSSPIT ARVGNPQIRN AQSQQHASSA PATPAASMIL NRQARESSAG PGGGAPKRGP
     RSISGLGSLP TTSSSLARHS SLGPGTPKGA TGPGPNGAVR AGSAGPRSSS TKASSVSGVR
     KGTPGVASRK KPINGNKSSL SRVKKAPGSR NSPASTADSE LSDADSGSGD EGDRTRIDRA
     SGTPARDGKD VDHDDSLLDV EDDEAGDDKK YCTCQNVSFG DMVACDNEDC PYEWFHWSCV
     GLKSEPNGTW FCPVCTENME RERLQKKK
//
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