ID A0A4Q4YY99_9PEZI Unreviewed; 1196 AA.
AC A0A4Q4YY99;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DL769_002978 {ECO:0000313|EMBL:RYP79394.1};
OS Monosporascus sp. CRB-8-3.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211644 {ECO:0000313|EMBL:RYP79394.1, ECO:0000313|Proteomes:UP000292472};
RN [1] {ECO:0000313|EMBL:RYP79394.1, ECO:0000313|Proteomes:UP000292472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRB-8-3 {ECO:0000313|EMBL:RYP79394.1,
RC ECO:0000313|Proteomes:UP000292472};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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:RYP79394.1}.
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DR EMBL; QJNZ01000157; RYP79394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4YY99; -.
DR STRING; 2211644.A0A4Q4YY99; -.
DR Proteomes; UP000292472; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000292472};
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 429..479
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 483..602
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 762..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1196
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 131950 MW; AE0356D5FC2AC3A7 CRC64;
MAPSPRTPRP SATSRVRGRQ KITSSSLRRS RDGSITAATE PPLKKRRYFP GGPGGGGRFI
DRNDDVPNTV GPATTRQRAR PIVTNAASPS IYPRRERSTR TRISTRADDD DEMQISSAAA
VAAAVVQSEG YKPREERGWE EFHPNLDIDA TFPIFHAEDV DGTAKSMPGT PSLTYTNNGT
NDAASPVKDQ NGASASQMND PAIQPSGTAA TGLGILPGTP SRVRRTSRAP RDSLYATRSE
SGIPPRAPTV LPIHNQTPKE RLDLKQPQYR KTNRIALFES KTFGQARYVD KAMMNVGYQE
SDNYIRPERR LIKATDYNAE DEAEHAAAAA RADGELSQHP ANVLGRVEYD MDEQDDMWLE
GYNAQRKSQG LNAVTREVFE ITITKIEKEW HALEKRIPKP NPKPPQTHRP RSSSAVAVNG
EPQAGEDQDS KCAICDDGDC ENTNAIVFCD GCDLAVHQEC YGVPFIPEGQ WLCRKCQLIG
RGIPTCIFCP NSDGAFKQTN SSKWAHLLCA MWIPEVTLGN HTFMEPVMDV EKVPKSRWKL
TCYICNQQMG ACIQCGNKAC YQAFHVTCAR RARLFLRMKN SSGALDVLDG GTNLKALCDK
HCPSEYAKEN DVVQATKNAK KFYKKTMRGR IWANSQASAM ALAATHRNAL TEHPPDESQM
TGAKLSAVLG DKKGQPGKPI WKLPSGAPVI PQAVFETVEA SLQRFTFLKR KEFISDACRY
WTLKREMRRG AALLKRLQLQ MESFSSMELT RRNFAAMGPV GKARLTRRVE FADTLIKDLE
QLKTMSEEVV ERERNKLEAA ELEQDFIDTC YFPIHKFLPA VVEKAIALDK NLFHEGLVEL
QRRLEERFYT TVLPFARDLC SIISSGINTE PEPQSEAQQF TTALTLLPKN DFSDIRDRKK
LGKRILKAVQ PLLETALHLE ADASHRSFDT LKQELEKMME AGVEARATKQ ATASGEGEGE
HSQDVIMVDA AAAEITVGGA DDEAHAAETD GAPADTMMAD REEQDLAGSA NIEVKTADHE
YDVKIEDGSL SQHSVTDIEQ GAVSQKPHAA SVNGVAPLDT PPATNGFEAT SQQPPQSGPP
TPPQSNGSLG RHPSDTLTEG GILWYLRDFE PEGTSAVRDQ WPGRDAVRSL SEELTDIDED
ELEGLGVELN KESITATAST TEGDAATEET TNSNTSSTKK SAKSKRRRTT TYTRRR
//
