ID A0A0D2A0R9_9EURO Unreviewed; 1545 AA.
AC A0A0D2A0R9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 56.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_02840 {ECO:0000313|EMBL:KIW18552.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW18552.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW18552.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW18552.1,
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.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000256|ARBA:ARBA00011353}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KN847493; KIW18552.1; -; Genomic_DNA.
DR RefSeq; XP_016238768.1; XM_016377198.1.
DR STRING; 91928.A0A0D2A0R9; -.
DR GeneID; 27329923; -.
DR VEuPathDB; FungiDB:PV08_02840; -.
DR HOGENOM; CLU_000315_29_2_1; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:TreeGrafter.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:TreeGrafter.
DR GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:TreeGrafter.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0034728; P:nucleosome organization; IEA:TreeGrafter.
DR GO; GO:0009889; P:regulation of biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.300:FF:000130; Chromodomain-helicase-DNA-binding protein 2 isoform 1; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR041150; Cdh1_DBD.
DR InterPro; IPR056302; CHD1-2/Hrp3_HTH.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF23588; HTH_CHD1_Hrp3; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023015};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 277..347
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 375..435
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 473..644
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 775..933
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 176847 MW; 21ACD14309AD6A68 CRC64;
MLTLSSTASS ILTQPLPPSI PDHSLSPGDA NERPELIAQN GTNYSDSESE LSEPTEPLVA
ASSLPQVKVD DEDENMQDID EPSSDEPDAE GDADYEMDTG MQVNGVRSEE NDSSSDESIR
PAKRKAPPVE EDEDIRNNPE LYGLRRSGRA RHVPNMAESD AEQDSDSDIA PRPRKRLRQV
SQRSSKQHTP MIETPSLSDD DSDAYGGKRA KLTKKQRRRL LQSADNLTPA HAEIRFSTRR
AAKVSSYNED EDDGMFDEDD ADTMTPNYWV SEQDNSPAID AVLNHRLKAD VTTPTRTKFD
YEFLIKWQLK SHYHATWETL ESLKEVRSLK RLDNYIKKHL MEDIRIVNDP DIAPEDKEKW
FLYREEVAEA LEEHKKVERV IGDREGEEGT EYFVKWKGLL YNDASWESST LVSEIAQAEI
DRYLARRRED FRSNASESNP GTRRSFLPMR EQPSYIQNGT LKDFQLQGLN FLAFNWSRSK
NVVLADEMGL GKTVQTVAFM SWLRHDRGQQ GPFIVAVPLS TMPAWADTFD HWAPDINYVV
YNGPQAARNI IKDYELFPDG NVRHPRFHVL LTTYEFVLQD APFLSQIKWQ FMAIDEAHRL
KNRESQLYDR LREFKAPARL LITGTPVQNN LGELSALFDF LNPGVINIDE SMDLTTEEAS
AKIAKLTEDI KPYMLRRTKN KVEKDLPPKT EKIIRVELSD IQLEYYKNIL TKNYAALNQG
AKGQKQSLLN IMMELKKASN HPFMFPSAEE RLVPEGARKD EVLRALITSS GKMMLLDQLL
TKLKRDGHRV LIFSQMVRML DILGDYMDYR GHAYQRLDGT IAAAPRRIAI DHFNAPDSTD
FCFLLSTRAG GLGINLMTAD TVIIFDSDWN PQADLQAMAR AHRIGQVKPV SVYRLVSKET
VEEEILERAR NKLMLEFLTI QRGVTDKETQ ARRSALVGEP GSSSEISRIL KKRGQKMFEQ
TDNQKKLEEL DLDAVLNNAE DYKVEQPDGT DADGGEEFLR SFDFVDVKVD EMSWDDIIPK
EQLDELKAEE QRKADEKYLA EVIEQNKPRV RNRDAEDREA RKARRQEQRQ KEIDSDSESD
EGPKADPARP LSEREYRYLI KGHLRYGSID DRQEEFLTEA RLRGRDIDVV KAAMKEVWDK
STELFKAEQE RMAELERTAN RPITKKDRKA VLFELHGVKR INAETILERP SEMRLLHEVT
SKEPDFKSFR IPEATKSAGY TCPWGAREDG MLCVGISRHG YGAWEKIRDD PDLGLKDKFF
LEEHRVDKKA ERERLDAKNA KSPGAVHLVR RADYLISVLK SKYGDDPAAK RAVENHHRNN
KKLQAERAAN IGSPVPGSHR KVHRDSEKPR HRHSQGHRDS SERYGTPRAD SRHGHSRHDS
ERRDERERRH RDDHGHTSHH NRHGSEHRRN ENPAGGSSSD VDPLMQVLFK PVRESLKKIK
ATTKSAIPDS QQRANELRVL LKQIGNFITE QIADLDDSHE SVEKRFWDYA ATYWPNKGIK
GQELQTIHGK IVASDNKLAG EASPNDESSN VEGRTNGSYR TSPPH
//
