ID A0A2C5XN34_9HYPO Unreviewed; 1198 AA.
AC A0A2C5XN34;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD80_973 {ECO:0000313|EMBL:PHH77069.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH77069.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH77069.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH77069.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-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:PHH77069.1}.
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DR EMBL; NJES01000135; PHH77069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XN34; -.
DR STRING; 2004952.A0A2C5XN34; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 421..471
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 475..594
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 130700 MW; B975A7B6B90C6A4D CRC64;
MAPASPSPRR TPTGRRRGRP LGSTNAARAA RQASLAAAAA AAAAAAASPS EPPPSKRRRY
VPGGSGGGGR FVQGAESREA QAVVASRQVP VGRERSTRAR AAGGDDMADS RWSSTAAAMA
ASVKQAEDYK PREERGWEEF HPNLDIERPF IVFLADEVDG APHLTPATPA AQTPGTPLAN
GSVTPSRQGG KPPTSTDNTP MPQDRTDGEA ASNGTPSRRP RRQPRDVVSF YGARPIDTPK
TPKILPIQNQ TPKERLDLKL PSYRKTNRIE LFESKTFGQA RYVDKSMSNV GYQESDHFIR
PSTTLIKAID GNADDEHPDP SPSAKVDDHA PHSRLGRVEY DMDEQDDMWL EQYNAQRKQN
ELETITREVF EITMTKIEKE WHCLEKRIPK PNPKPPQTHR PRSSSDAAVN GETAQAGEEP
DSKCAVCDDG DCENTNAIVF CDGCNLAVHQ ECYGVPFIPE GQWLCRKCQL CGRGVPTCIF
CPNTDGAFKQ TNSSKWAHLL CAMWIPEVSL GNHTFMEPVM DVEKVPKTRW KLSCYICHQK
MGACIQCGNK NCYQAFHVTC ARRARLFLKM KTNQGALAVL DGGMVLKAFC DKHCPPDYSQ
ENKVHQATRV AKKFYKRNMR GRIWADNHAM ANVIAAQHRN AITEHPPDES QMTGAKNSAV
LLGDKRKGGQ APRNLWKLPS GAPIIPQAVF DTVEASIQRF PFRKRKDFLS EACRYWTLKR
EARRGAALLK RLQLQMETFS SMELTRRSFA SMGPGGKARL ARRIEFAEGI IRDLAQLKAL
AEDVVQREQI KVDAAELEQE FVDECYFPVA KLLPPVIEKA TLYVALDHQC LDKNLFADGL
AKLQGRIEER FYVSALCFAQ DLGDVICAGI ATPPATDEVS EPRFEPVDAA PVRNVFADIR
ERRKLGKRIL KAVQPYLETA LRAESEIANK PFESLQKELE ALIDASIEAT RAPAGAEVKL
EGGEEEEDDD TIMVDASHPS EITVKSTFQQ AAGSAAGAAT DVEAVEEGGN IEVKASGLGI
VNRDGTEVAR RSVRGGPAQV GLEGGTSATP PEGDGFVPLS RPGQQQPQQQ TTTTTTTTTT
TTGPPTPPQS NGSFGKEPGD PLAEGGILWY LKAMQPAGTS ILGEHWAGRD AVRMLSEDLT
DLDDEELRGL GADVEDAVEA AAAMESETTA VVHEGGGGAA KGRASGRVKK RRASGRRR
//
