ID A0A165UBA2_9APHY Unreviewed; 1014 AA.
AC A0A165UBA2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=DAEQUDRAFT_734278 {ECO:0000313|EMBL:KZT74661.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT74661.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT74661.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT74661.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV429032; KZT74661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165UBA2; -.
DR STRING; 1314783.A0A165UBA2; -.
DR OrthoDB; 124870at2759; -.
DR Proteomes; UP000076727; 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 CDD; cd16039; PHD_SPP1; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 649..700
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 109539 MW; 430473122F276F12 CRC64;
MTGPSSPSML FSGSPPSSLL PMSESRTSSL SHESPGEIES RPAAASLPNI LNSSSPALRP
NTGLGGLEAL VQAATEERRR LSGELGQGLS RMDSSPKPSE SPVPERVPMQ LPVAMNAATK
PLSPFAVRTS FGGRRDILND DVSASPLRIQ DSDGEPPRKR RKSSGVPNSS PSPMVIQQPI
TPCDVAVPAS PTEVTQVLSP TVNDKKTGTV IDDDLRTTSI PVAPHEVGGS TSDAEVLEVR
PAVGPQPRDE TLEEQILDAV DGSSARVGEK DRVREKEDKM REKEKKKREQ KSKEKRASEQ
KRRTASVARE TEANAGDQDA HEWLLEHYAS TSPRVDPASS SSGNKAATSP TTTALPASSS
RAVKAEEGHR GRHHIDESGV TRPSKDTKKA RSRTPTPLAM LEEELDSVLP ASYTIASSID
DELILDVASP VMAPSVGGGV TDDNDVDNEL LSLVDDVPPV PHTSRPKPAN IPKFDIHSRT
KSSLSQPASE RGSMPPPASP VKDGGTPHPP STGDSFGGAS AVAGHRKKDP SQKPVPKQKA
PPKPKPKAAT TTTTKTKSKV AKDAVSSAPN PTLGMLTPST STFSAKGKKN TAASSANPAT
KRPVSAAGGQ SRSRSTSAMP TAPVTEGDGK PTSEIADPGE VKEQNQDDKL YCICKTRYDE
DRAMIACDRC DEWYHTQCVN MPELEIDLVD QFICPLCVRN NPHLRLQTTY KKRCFNGLNH
PDPSSPSACH RPARGTYSKY CSDECGILHM QARIHAWRGD KDSLWESVKN APKREGVVVL
VKDASDNGNK ATGNDYMSPA PSSAQPILEV VKPSRTKVER ERERLNGLLD KISCRRDELK
KEMDVLLWRE KLIELAVARA EQVDECGWDQ RLCFGEEEYA EFGASVLESY EEVDQSVADA
MQMDGTQTEE GEWWCRGQKK CARHAGWQKL RLTEVDCDKE ALDGVLSKLT TQEREIRKRI
EDVVNPTAGT SATDPTGPTA GSPLQRLNGK TVTNGHARSK VNGESAKKGK KKKI
//
