ID A0A369HAG7_9HYPO Unreviewed; 591 AA.
AC A0A369HAG7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Zinc finger PHD-type domain-containing protein {ECO:0000259|SMART:SM00249};
GN ORFNames=CP533_5593 {ECO:0000313|EMBL:RDA92202.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA92202.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA92202.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA92202.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA92202.1}.
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DR EMBL; PDHQ01000051; RDA92202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369HAG7; -.
DR STRING; 2039874.A0A369HAG7; -.
DR Proteomes; UP000253071; Unassembled WGS sequence.
DR GO; GO:0031213; C:RSF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028938; Rsf1-like.
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; PTHR14296; REMODELING AND SPACING FACTOR 1; 1.
DR PANTHER; PTHR14296:SF3; REMODELING AND SPACING FACTOR 1; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000253071};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 421..471
FT /note="Zinc finger PHD-type"
FT /evidence="ECO:0000259|SMART:SM00249"
FT REGION 185..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 67116 MW; C0A66DBB108D7109 CRC64;
MPSRKRPIQA VEDSASVTNG DEASTTLSRI RNMWQFANLC QWIYIFGKAA KIDESIDIEE
IEADCLKPNQ TLLEDLALAI LKLVSSHRGL NHDIMNDQLH KQYLMRAPES IVYSDNHSSN
FSDLSVFQKI IVLQQLTQWA MTYPERIRDL VGEHKDTEQM SWRIEPYGWD KEDRTYFVLD
DNRVYRSTDK PPGQARVKPK SKSTKSARAH RRSRAVQPED DTPDGVDDDG LGGRTWECVA
VTLQDVQSLL DNFAKTRDEN EKILRRQLEA HLVPILEKQE EAQKRKQAQR ERELLNLSKM
ANAKRSSRIA GKVEKRKLEE LAKEEEQKER VAAESKIRGE QERQRLERER DFRMFSRQRR
LQEREARRLQ HKEELAQLSE DNKQGPTSGG RISERHRVAK LEKTKQRLED LEREEEEWAF
DCVCGLFGQV DDGTHCVACE RCNVWQHSEC LGISKAEADR PEFQFVCDSC KRPNGGVVSD
APFKTVKLKL NPTRNSNGSS RAEPAQDKQS MTQGAPLGDA SMEQSRPGAP LSRDEDSAPD
VSTAAAEPPE GAEKVSPVAD ARESIIVRHN GEVGPGLGDS NAASSHQVQT I
//
