ID A0A0D2BJI4_9EURO Unreviewed; 892 AA.
AC A0A0D2BJI4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=PV08_03054 {ECO:0000313|EMBL:KIW18765.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW18765.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW18765.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW18765.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847493; KIW18765.1; -; Genomic_DNA.
DR RefSeq; XP_016238981.1; XM_016377411.1.
DR AlphaFoldDB; A0A0D2BJI4; -.
DR STRING; 91928.A0A0D2BJI4; -.
DR GeneID; 27330137; -.
DR VEuPathDB; FungiDB:PV08_03054; -.
DR HOGENOM; CLU_015602_0_0_1; -.
DR OrthoDB; 1333597at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0031213; C:RSF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028938; Rsf1-like.
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; PTHR14296; REMODELING AND SPACING FACTOR 1; 1.
DR PANTHER; PTHR14296:SF3; REMODELING AND SPACING FACTOR 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 Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 442..498
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 101428 MW; F1022C572BFE10A3 CRC64;
MPRKRTRDEM EASAPEEKKT GPSILQRIRN MWEFASIMQF IFIFGKAIKI DEDFDIEDFE
EECLKPGYSE KLEEIGLTLL KWISSHRGLD YTIWDEYTRR QYLAKAPHLN PYGEEETPKR
FRDFDIFTKI RVLHQLTVWT FWNPDRIREK MPDHPREVDQ LEWRIEEFGY DGDDRQYYLL
DDNRFYRRTD PPPPPVPKAK PKANSKKAIA ARRRESKRRR LEAELEDTAD EHHEGNDESH
MADEKTQEPW EIDTFGGFKW ECIAITLTDY RELCESLKRS KDPNEKFLRE RLISEVLPVI
EAAEEKQRRK IERRQRELLM MERMVGAKRS SRLADKHDRE RREAEEAEAE RKKQADLAAA
HREMERQEKM EQERQFRMLT REQRIRDREY KRLLKEEELA RDAIEQKKIE EGEIRGSDRH
LKQRIEKNKK ELEDLNNEEE WTFDCSGCGV HGKNIDDGSH SVACERCSVW QHSKCLNISK
SAAEKDDFHF VCRDCRRKEA EANKPKISLK FKVGTSSSPA PPSPALPVPQ SPQKSSFASV
EIPRQNAAGP SSQGSTMNGS PAHQSSPSSR PPSSPYHPRH IQSNGFPQQY PQGAGISQQG
SPSAGLHQQP SGSHQFIQYV PGYPPQQSAH MVGNGFARNP PQPSAHAPSH NGTAYQFQNY
PYEQRHLASA QDMPRQQTQS PANRQATNST GRLPSPVFNR PMMSPTQGNM DVGPVAGIPQ
KSPSLGQNAT NGVSVNGLQP QPNGVASQVH ATPRASSQPY EAQTPTTQPI SGLSPRKQPT
PQHFPPPSIM IQKRNSMSPT LQASAVASGH AEKRTVSGTP VLPPIENLRP SPEQMRKMSS
NEPVPTPSKQ PQPSPTMAGA DPGEFSNFHS SSSPPDKMED VQHVTGAEVK TS
//
