ID A0A2J6PZE7_9HELO Unreviewed; 1364 AA.
AC A0A2J6PZE7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=NA56DRAFT_200859 {ECO:0000313|EMBL:PMD19378.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD19378.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD19378.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD19378.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613489; PMD19378.1; -; Genomic_DNA.
DR STRING; 1745343.A0A2J6PZE7; -.
DR OrthoDB; 5491843at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15535; PHD1_Rco1; 1.
DR CDD; cd15534; PHD2_PHF12_Rco1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; PTHR47636; TRANSCRIPTIONAL REGULATORY PROTEIN RCO1; 1.
DR PANTHER; PTHR47636:SF1; TRANSCRIPTIONAL REGULATORY PROTEIN RCO1; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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:UP000235672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 813..861
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 146165 MW; 7AC6C697FE1EB2FD CRC64;
MATPSTRPTR SRMASPFLPA SQNAAADTKT TLADASEKTQ GTLDGWSEPP LPPPRPSFMD
AGIERHGVVQ NMAPLGALPT PKVIKLATKP EEVLFGRTAN SKRSVPSAVS TPSESVMTPE
PPTNPPRQRS ASIKTIDEVE SAPQTPQAPL SARKSASRQS VPPPQHNGQG VFQLQPSPIS
ITNNIPRPTP PTPQPAPPVQ LQGTPGPTLG ADGLPLTNLD KTDRVVEEAV QEAVDLQRWP
TAYALRTLYD DHRSNPRIVR LIEAVYYGRA SEANYVEFKS IMRHKKREGK KDRTGEYYFN
GDGSDPAPNT KEITPAPVIP AIPIEVIQPP PRPYQTPYRD MGPKSISLAG RSSSVSALPA
TASPKEGEEN EHISKKHRSN SFQPVSTEVN GTPTANGMGT GSPARANGAS NSAKSTPHKS
RRARSQSTSS SLSSVDPETF EGENPMMAGA DNSSRIVSLS PAANANANAN VNANAHAHAH
APNLVLTRLG GHPLAGLGLS LGGAAKPHVS PYTSHNNFVA AASSAETLAR NQHQPISAPV
PPREKTGPKL GFFKPTPSTP ASAPVTDTTT KSSALKSPTT STSTSLANNP PASTTAAAST
STSMAPAALA ASSSNSSASS FHHFPSSFKA KSLAKFKGDP YDPNDKTSRL RRRARETTNA
INGDIRDSFE RHQVQVASSQ REQETDSEGA DADSVAVPKV SKRPAKVRLL NNKTKTREST
RQRDKYDSDN LSSPTLLSFQ ADVAPGSLSV SRAGTPNNFG RPTRKARTGT GLRVKTSPMK
KKGALPAGIP RASGERNSPT GNGASSHNQD DNDDYCSACG GNGDLVCCDG CTRSFHFKCV
DPPMIQGSLP DEWFCNICQA GRPGREDPIP GTFGPLLLYL DAKNPSAFTL PKSIREYFVD
VKTGADGEYE EAGTGKPKNT RGGWDEAPDY YRLKDGKGKA ILCHECHGAA SHPNRMIISC
SFCGLNWHLD CLPNPLAKEP SQGRQWRCPA HVDDLLAQVP ATLAPAHRFR RIKGASAIKP
AISRGIKNNG YIEIETEPSE DEEEQGFYEQ REYGHVYKLP EQGIKLDFIS KVRREGGGYL
PSRFATRPPK PVSRLTWNQR SVNEQQAALN LASLAARGPQ DSDLSQIINT LLAEAPPAVI
EMMALDQVDA LSDKLPTHLI MSMKLLFDKL YEKITPLEDN HVQVSAPISA RVSTRGSATP
APISALASAR GSVRGSATPA PRSASIPAEV VEPEVEKIVV RDATPNTIEE PAEDAMIEDS
IVEELTADAA SVEAVTDQSP IETATPIEAP EVVVSPIQTQ VEATLIEAAP ISVVTETEHE
HEKMDEDPVE YPVQTSVEKQ VEPVVELRAE PEIQHEDADT EMLL
//
