ID A0A066XGP2_COLSU Unreviewed; 1195 AA.
AC A0A066XGP2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative PHD-finger domain-containing protein {ECO:0000313|EMBL:KDN64921.1};
GN ORFNames=CSUB01_05744 {ECO:0000313|EMBL:KDN64921.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64921.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN64921.1}.
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DR EMBL; JMSE01001085; KDN64921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XGP2; -.
DR STRING; 1173701.A0A066XGP2; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_002663_0_0_1; -.
DR OMA; NTSKWSH; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000027238; 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:UP000027238};
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 437..487
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 491..610
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1018
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1195
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 132550 MW; 03637E90A716320A CRC64;
MPSKPSTPRR PPTGRKRGRP PGTTNAARIA REAGDSPAPP SSRSAREHAT PSAAPQTEPP
PKRRRYIPGG AGGGGRFIDD DGTQTPITVR RQPREPRTVS TVVPRRERSA RLRTAADRDD
MEFSSAAAVA AAVAENEGYK PREERGWEEF HPKLDIDATF MVFRSEEVDG IPLPTSKSPP
RTPAAARPST PMNGSSTPLR EMNPVSTGNT PVPTTTSYFA LPIVGSESPQ KRRTRPPRES
VSFLNRDLAP ASTPRVPQVL PIRNQTPKER LDLKAPSYRR SDQVEQFESK SFGQARYVDK
SMMNVGYQET DRYMRPEGRL IKAAEPNLEE DLELAAVKVD GDVHPTSGTN VGRVEYDMDE
QDDQWLEAYN KEHRKGHELE PITREVFEIA ITKIEKEWHA LEKRIPKPNP KPPQTHRPRS
SSAAAVNGEP QVGEEQDSKC AICDDGDCEN TNAIVFCDGC DLAVHQECYG VPFIPEGQWL
CRKCQLIGRG IPTCIFCPNT DGAFKQTNSS KWAHLLCAMW IPEVSLGNAT FMEPVMDVEK
VPKTRWKLSC YICNQKMGAC IQCSNKSCYQ AFHVTCARRS RLFLKMKNSH GALAVLDSNM
VLKAFCDRHC PADYAKDNGV AQAAREAKKF YKRAMKGRIW ADSQAAAHAL ATTHRHALTE
HPLDESQMTG AKFASFVGGD KKKGQPGKQI WKLPSGAPVI PQAVFEIVEQ ALSRFPFRKR
KDFVSEACRY WTLKREARRG AALLKRLQLQ METFSSMELT RRNFAQMGPS GKSRLARRVE
FAETLLKDLW ELKLLSESVV QREQEKLDAA ELEQEFVDTC YFPIAKLFVP VVEKAIFLDK
NIFKDGLLEL QEKLERRFYT NTLVFTHDLC EVINVGINTE PQFTESTSQG GALSPVKQNF
NDPRQRKALG KRILKAVQSQ LETALKTEAE ITHKPYDTLA KELEGMLEAS IEFRQPSIIV
SHTEESTEPS QDTIMVDATN EQITVANDDD PRAEEEPAAA GDQMDMDAEG EDDDEGNIEV
NTSTLGKPSD VHSSSSSVAG HEGNGKAAVK TEGSLASSIQ PSDTPPETNG YVTVSRPAQP
APPTPPQSNG SLGNESTDPL SEGGVPWYFS DFKPKGTTII EEQWTGREAL RSLSEDLTDM
DDQELEGLAF DVEDSTITAS PTVNDEVAAD TIVSKAKSNS KVRKRTSARA SARRR
//