ID G0SHA8_CHATD Unreviewed; 1329 AA.
AC G0SHA8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS51805};
GN ORFNames=CTHT_0069350 {ECO:0000313|EMBL:EGS17597.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17597.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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DR EMBL; GL988047; EGS17597.1; -; Genomic_DNA.
DR RefSeq; XP_006697215.1; XM_006697152.1.
DR STRING; 759272.G0SHA8; -.
DR GeneID; 18260973; -.
DR KEGG; cthr:CTHT_0069350; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_002663_0_0_1; -.
DR OMA; NTSKWSH; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001965; Znf_PHD.
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; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 514..633
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1255
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 146225 MW; 80639AB616182508 CRC64;
MAPSPATPRR TARGRPRGRP RTSGSASASR SRRAAADAPT TEPPPKRRRY IPGGPGGGGR
FVEEDGTEIP TESHGASTST GTASASARPR ASQRTSSPTA AYPRRERSTR LRNANAASAV
NRDQQDDMQY SSAAAVAAAV VQNEGYKPRE ERGWEEFHPN LDIDGIFMVY AAAEVDGLVK
PGQQQPQAAS QTGPDAPAVN GTALPTKQDN TGSAAPAAED AANGTPGRQP QEGKLTLGAG
PVPPETPSRR RVGRPPRDSV SLYANRPPEP APAPKIPKPL PIYGQTSKER LDLKMPSYRR
TNRVALFESK SFGQARYVDK SMSNVGYQES DHFIRPERRL IKASDANLDE EIEQWGVSKL
DGEAAVQNPA GNVGRVEYDM DEQDDMWLEK LNAQRKANDL DPITREIFEI AITKIEKEWH
ALEKRIPKPN PKPPQTHRPR SSSAAAVNGE PHVGEEQDSK CAICDDGDCE NTNAIVSVMA
AIWPSIRSAT VFRLFRRANG SVASASLLDA AFRYVTCIFC PNTDGAFKRT NSSKWAHLLC
AMWIPEVSLG NHTFMEPVME VEKVPKTRWK LTCYICNQRM GACIQCSNKN CYQAFHVTCA
RRCRLYLKMK NSQGALAVLD GTLPLKAYCD KHCPEDYAQE NKVAEATREA KKFYKKTMKG
RIWADSRASA LQLAQTHHHY YHQNVVPEHH ASDEALKNGV SGGDKKKDKP PKNMWKLPSG
APIIPQAVFD VVESALARFP IRKRKDFVGE CCRYWTLKRE ARRGAALLKR LQLQMETFTS
MELTRRNFAA MGPTGKTRLS RRIDFCRTLI ADLEQLRGIT EEVVEREADK YEAVEMEQDF
VDTCYFPVAR ELQPVLDKAF SLDKNVFKKA FLEMQDRLDE RFYTTTLLFT HDFCQAICTG
INTDPAPSAQ EVRPDPIDAS PNKSNNYAEA RDRRRLAKRI VRAVQPMLES ALRAEADICN
KPYDELRAQL EAMLEASLDI KQAQQAASIT VSNPASVAAD QEDVDMADAP ADGQIIVVDQ
STGHDEDAEG EPDGDAEGDL DEPMPDVKEQ SVEVSADEIK VDTSAHLSRQ GTPPQPNEHN
QQQQAKALIN GFSEAAKHHN PPGNLSPNSF PGGPYTTATL QLDSSITINN PTTTAPPESD
PLTPPQSTSS FSHPVPAPTA SGSTLPIITT TAPDPPSGYS LPANVQDDSF LTKGGVPWYL
SGFEPHGTTA LAEETWTTGR EAWGGNKKMG KKKKKKKKKE KEKEKKKKKE KEKEKKKKKX
XXXXXXGGGG GGRRRGIRKG GWLLRVEGGA EGLEVAGSTG SNTKRKNRKG SAGNGRVLRR
GVRSSNRRR
//
