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Database: UniProt
Entry: A0A150UVP9_9PEZI
LinkDB: A0A150UVP9_9PEZI
Original site: A0A150UVP9_9PEZI 
ID   A0A150UVP9_9PEZI        Unreviewed;       649 AA.
AC   A0A150UVP9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN   ORFNames=M433DRAFT_137327 {ECO:0000313|EMBL:KYG42349.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42349.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG42349.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG42349.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KYG42349.1}.
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DR   EMBL; JPDO01000475; KYG42349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UVP9; -.
DR   STRING; 766039.A0A150UVP9; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR037869; Spp1/CFP1.
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; PTHR46174; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR   PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 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.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          312..363
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          510..537
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        24..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  69959 MW;  149E5029E8CDAC53 CRC64;
     MSFSLSTLLN PEPAPDAPNS SLPPLTGLVH SPEQQQQAQT THSPAVASPV DGPVTWPPSP
     SARRPSSSYS GIELPLPTPS TTARKASSPT LEQYQVASRS PDMRRQSAVL PAQSTFTLPP
     LQGLAQPGPQ IREEKTDVAV DVADVAYAYD ESVSRPASDS KATVHQSGAI DTSADAPNPA
     DGPTALSTDI AKQEAVHAGH TTSTPVETRA PSSHAAQTDI KSTSTALPAI KQEQTDPTPS
     QPHIRESSIP VPSTEKQTPE APPAAPSRKR PAPSRTKKGT AITTKKAPPA KKRKLDPVPK
     RSETPASSKP GDVYCICRKP DNGSFMIGCD GACDDWFHGK CVGIAERDKT LIDRYVCPNC
     TREGRGHTTW KRMCRRAGCR LPARVTAGGK GRTGRSKYCS EECGMMYFRE LLARTRGRGE
     YGERPHRQRK GSIVADEFDD LGARGGILSA SEVKSLAHAA QSARKFQRLG EESVLSPPAT
     PPLAATAGDT TTATTTKEAF PLAPEDVREL EAILLKKDEA RRRHAALKER MRFVETVKSA
     AAAAAEERGL KAKEFCGYDS RLENGEFDGE GEVCERKKCA RHLEWAKLAV DSVRAEMAEN
     SDRMRGLEKE ERAVKGRGAW RASLKEADWR GSGWVEVHIH PAEGGDSQS
//
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