ID A0A0F7ZSQ7_9HYPO Unreviewed; 812 AA.
AC A0A0F7ZSQ7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=HIM_08803 {ECO:0000313|EMBL:KJZ71783.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ71783.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ71783.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ71783.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000256|ARBA:ARBA00010210}.
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DR EMBL; KQ030561; KJZ71783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZSQ7; -.
DR OrthoDB; 3140066at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
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 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; 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:SF108; FINGER DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G11940)-RELATED; 1.
DR PANTHER; PTHR10333; INHIBITOR OF GROWTH PROTEIN; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 748..796
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 750
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 761
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 765
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 770
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 812 AA; 87402 MW; AF5254EAA109186A CRC64;
MATGGEETGA MAQAAALPAR ERSGSDQAPL EPAVVATATS LESRADPDAQ TTVTDFLDFT
EYLPSDMIRS LTLIGKLDQA YTDASVRVND LTTAWGQLPG CGAHERPDPA KLRADISENL
DQAVSSRVFA HAEAVRMSEN VNRHYNKAKM LLAKLQNMMD NYPAEEPRSP VAAVKSPQLS
RNKVTVRTTD EDGKKISRHR IPRITVPGEV LAPYDIEYDT CSDDSDISTD SESDIPAASR
RTPAPASRIK IVTNKTPKSA SRPARPQYTS AAMSAAAAAN AAALLNPPPE NAVIGSPDAP
WLQLTQYELA KLRKRMKKNA TWTPSDTMVA RELKALGRGP DEYREAKKKA EEEGKVFNPA
MPNPIIDDES GTRQLPAGAL SADALAVEEH PTSNRGMKLN EAKKLKREAL AKLAAEEAEE
SARKMAHAAK LFLGNGPQNA SENSKETGKP RTSSRSNGKR KREGEADSAE PVEPVESSET
PSRPVSKRTK TETPVPPPPR LGLSQGNAPA ADGSANQQVT PGGSVVVTQL ETPVPIPVPP
RGSSVKSAAS PSSVASNGNT VTTSVPTKPP ALETPVPLPR TEQRTASREG NKRETRGEAA
KRHQQQTPVA PQLPPLQITD QVTTRRSASR GHTPSATPAP ESAGGRRPSS RGTAMSQEPP
SLASERSRRA STARNTPVPE LKQPPKRTKR PAPGVVSTTN SGGNSAVGKR KAAPKRKARL
LKREKGQVTE TEMEEVDDEG NPIDPNEPRY CLCNRVSFGT MIQCDNMDEW FHLECVGLSD
IPARTTKWYC PDCRRLLNIG ERGEVSARGV RK
//
