ID A0A1W5D7P1_9LECA Unreviewed; 826 AA.
AC A0A1W5D7P1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Phd finger domain protein {ECO:0000313|EMBL:SLM38919.1};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM38919.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FWEW01003107; SLM38919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5D7P1; -.
DR OrthoDB; 1333597at2759; -.
DR Proteomes; UP000192927; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 412..468
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 160..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92171 MW; EBBD4877F6526B7E CRC64;
MSRKRGRAEM EASHPPQELS LLDRLRNMWQ FSNLMQYIFI FGKAVKIDED FDIEDLETEC
VKPEPSEKLS EIGLALLKFV SSHRGLTPDI FDEYTRRQYV AKAPGRNPFG SEEAPNKFAD
FDIFTKIRVL FQLSQWTLRV EDIGMDKKNR LYFVLDDNRL YRRTDPPPPP PPPNTKAKGK
SKKAKAGARA SKRRKVIDTD ESADNVEEEV AGDGQAAVAP EDDGFGGSKW ECVAITLGQY
RDFLETIRKS KNTDEKELHT RITEDVLPII EKAEEAQQRK IARRERELMT LQKLATAKRS
GRIASKMDKE REEREAAEAE RKRQADLVEA KKEQERQKKM EEARESRMMT REQRLKEREY
KRILHEEELA NLSEDSRKLE TGEARMSERH LKAEMEKRKK ELDKLAQEDE WFFDCSKCGV
HGENLDDGSH SVACEKCNVW QHSACLGISQ ADAEKDDFHF VCDDCKRREE DAKKPKIPAL
KFRLGSSSSP PSDQTIRLNG VADKSKKRKL EDEHAYLPPV KKFSHVHVQP NTIKSPSQGP
PHVASNGMHG GLMNGPTLSP QGQLPLPPYQ NGHITEGAPP PPGLASPLRP GSSANGYAQH
VSQPNGYESQ PHSQPNASLP NTPSAATHTS HGSPGSAWPA QYPPLLSAQH AQDHQQIPPQ
PPNPFLNSFD RQHPSSSHST HNLASPMKNR LSMSPTQGNL ETSAIVNPAH QPNTSIDTSS
YLPGVAHTPG FSPTKQLSSP AAPLQAPPSS PIIRPPIDQQ QQNRQSSLGL SPTKHSPPRP
PSAPSMADTP VVPPVLDLSP SPRQQQTFQA PVKSPTPERP SEVNGS
//