ID Q800S6_TAEGU Unreviewed; 1806 AA.
AC Q800S6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD1Z {ECO:0000313|EMBL:AAO61783.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|EMBL:AAO61783.1};
RN [1] {ECO:0000313|EMBL:AAO61783.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14660691; DOI=10.1093/molbev/msh027;
RA Agate R.J., Choe M., Arnold A.P.;
RT "Sex differences in structure and expression of the sex chromosome genes
RT CHD1Z and CHD1W in zebra finches.";
RL Mol. Biol. Evol. 21:384-396(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AY217131; AAO61783.1; -; mRNA.
DR RefSeq; NP_001071647.1; NM_001078179.1.
DR GeneID; 778444; -.
DR KEGG; tgu:778444; -.
DR CTD; 1105; -.
DR OrthoDB; 5482994at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
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; IPR040793; CDH1_2_SANT_HL1.
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.
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:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 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; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:AAO61783.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AAO61783.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 273..365
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 390..453
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 494..664
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 793..944
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1345
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1806 AA; 208047 MW; 6BC935637185FAC0 CRC64;
MNGHSDEESV GNSSRESSRS DDDSGSASAS GSGSSSGSSS DGSSSQSGSS DSDCGSGSGT
QSESESDTSR EKKQIQSKPP KVDGSEFWKS SPSILAVQRS AVLKKQQQQK AASSDSVSEE
DSSSSEDSAD DSSSETKKKT HKDEDWQMSG SGSMSGTGSD SESEEDREKS SCEENESDYE
PKNKVKSRKP PIRIKPKSGK KSAGPKKRQL DSSEDDDDDE EEEEDDDYDK RGSRRQATVN
ISYKEAEETK TDSDDLLEVC GEDVPQPEED EFETIEKFMD SRVGRKGATG AATTIYAVEA
DGDPNAGFEK SKEPAEVQYL IKWKGWSHIH NTWETEETLK QQNVKGMKKL DNYKKKDQET
KRWLKNASPE DVEYYNCQQE LTDDLHKQYQ IVERIIAHSN QKSAAGYPDY YCKWQGLPYS
ECSWEDGALI AKKFQARIDE YFSRNQSKTT PFKDCKVLKQ RPRFVALKKQ PSYIGGHESL
GLRDYQLNGL NWLAHSWCKG NSCILADEMG LGKTIQTISF LNYLFHEHQL YGPFLLVVPL
STLTSWQREI QTRAPQMNAV VYLGDITSRN MIRTHEWMHP QTKRLKFNIL LTTYEILLKD
KSFLGGLNWA FIGVDEAHRL KNDDSLLYKT LIDFKSNHRL LITGTPLQNS LKELWSLLHF
IMPEKFSSWE DFEEEHGKGR EYGYASLHKE LEPFLLRRVK KDVEKSLPAK VEQILRMEMS
ALQKQYYKWI LTGNYKALSK GSKGSTSGFL NIMMELKKCC NHCYLIKPPD DNEFYNKQEA
LQHLIRSSGK LILLDKLLIR LRERGNRVLI FSQMVRMLDI LAEYLKYRQF PFQRLDGSIK
GELRKQALDH FNAEGSEDFC FLLSTRAGGL GINLASADTV VIFDSDWNPQ NDLQAQARAH
RIGQKKQVNI YRLVTKGSVE EDILERAKKK MVLDHLVIQR MDTTGKTVLH TGSTPSSSTP
FNKEELSAIL KFGAEELFKE PEGEEQEPQE MDIDEILKRA ETRENEPGPL TVGDELLSQF
KVANFSNMDE DDIELEPERN SRNWEEIIPE VQRRRIEEEE RQKELEEIYM LPRMRNCAKQ
ISFNGSEGRR SRSRRYSGSD SDSISERKRP KKRGRPRTIP RENIKGFSDA EIRRFIKSYK
KFGGPLERLD AVARDAELVD KSETDLRRLG ELVHNGCIKA LKDNSSGQER AGGRLGKVKG
PTFRISGVQV NAKLVISHEE ELAPLHKSIP SDPEERKRYV IPCHTKAAHF DIDWGKEDDS
NLLIGIYEYG YGSWEMIKMD PDLSLTQKIL PDDPDKKPQA KQLQTRADYL IKLLNKDLAR
KEAQRLAGAG NSKRRKTRTK KNKVLKAAKL KEEIKSDSSP QPSEKSDEDD DENNKDEIVS
VKHLHKKFKA EKENEEKPEP DTGIKKEAEE KRETKEKENK RDLKREKKEK EDKKELKEKR
ENKVKESTQK EKEVKEEKVN EIKSENKEKT KKIPLLDTPV HITASSEPIP ISEESEELDQ
KTFSVCKERM RPVKAALKQL DRPEKGLSER EQLEHTRQCL IKIGDHITEC LKEYTNPEQI
KQWRKNLWIF VSKFTEFDAR KLHKLYKHAI KKRQESQQHN DQNISGHVNT HVIRNPDVER
LKENTNHDDS SRDSYSSDRH LSQYHDHHKD RHQGDAYKKN DSRKRPYSAF SNGKDHRDWD
HYKQDRYYSD SKHRKLDDYR NRDHRSSLEG SIKDSRVHLD HRSHSDHRIH SDHRSSSEYS
HHKSPRDYRY HSDWQMDHRA SGSGPRSPLD QRSPYGSRSP LGHRSPFEHS SDHKSTPEHT
WSSRKT
//
