ID A0A3L8S464_CHLGU Unreviewed; 1777 AA.
AC A0A3L8S464;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE Flags: Fragment;
GN ORFNames=DV515_00012214 {ECO:0000313|EMBL:RLV97009.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV97009.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV97009.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV97009.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV97009.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV97009.1}.
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DR EMBL; QUSF01000064; RLV97009.1; -; Genomic_DNA.
DR STRING; 44316.ENSEGOP00005020666; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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 CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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; 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; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 264..354
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 464..634
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 763..914
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RLV97009.1"
SQ SEQUENCE 1777 AA; 204829 MW; E607C7CADFCAE8D2 CRC64;
QGIEDLSIPF FLSRSDDDSG SASASGSGSS SGSSSDGSSS QSGSSDSDSG SESGTQSESE
SDTSREKKQI QSKPPKVDGS EFWKSSPSIL AVQRSAVLKK QQQQKTASSD SVSEEDSSSS
EDSADDSSSE TKKKTHKDED WQMSGSGSMS GTGSDSESEE DREKSSCEEN ESDYEPKNKV
KSRKPPIRIK PKSGKKSAGP KKRQLDSSDD DEEEDDDDYD KRGSRRQATV NISYKEAEET
KTDSDDLLEV CGEDVPQPEE DEFETIEKFM DSRVGRKGGA ATTIYAVEAD GDPNAGFEKS
KEPAEVQYLI KWKGWSHIHN TWETEETLKQ QNVKGMKKLD NYKKKDQETK RWLKNASPED
VEYYNCQQEL TDDLHKQYQI LIQIRNQLLV IQTTIVSGKV CLILNVVGKM ELSLPKSFRH
ALMSTSVLKQ RPRFVALKKQ PSYIGGHESL ELRDYQLNGL NWLAHSWCKG NSCILADEMG
LGKTIQTISF LNYLFHEHQL YGPFLLVVPL STLTSWQREI QTWAPQMNAV VYLGDITSRN
MIRTHEWMHP QTKRLKFNIL LTTYEILLKD KSFLGGLNWA FIGVDEAHRL KNDDSLLYKT
LIDFKSNHRL LITGTPLQNS LKELWSLLHF IMPEKFSSWE DFEEEHGKGR EYGYASLHKE
LEPFLLRRVK KDVEKSLPAK VEQILRMEMS ALQKQYYKWI LTRNYKALSK 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
IQRRRIEEEE 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 EDKRELKEKR ENKVKESTQK EKEVKEEKVN EIKSENKEKS
KKIPLLDTPV HITASSEPIP ISEESEELDQ KTFSVCKERM RPVKAALKQL DRPEKGLSER
EQLEHTRQCL IKIGDHITEC LKEYTNPEQI KQWRKNLWIF VSKFTEFDAR KLHKLYKHAI
KKRQESQQHS DQNISGHVNT HVIRNPDVER LKENTNHDDS SRDSYSSDRH LSQYHDHHKD
RHQGDAYKKN DSRKRPYSAF SNGKDHRDWD HYKQDSRYYS DSKHRKLDDY RNRDHRSSLE
GSLKDSRVHL DHRSHSDHRI HSDHRSSSEY SHHKSPRDYR YHSDWQMDHR ASGSGPRSPL
DQRSPYGSRS PLGHRSPFEH SSDHKSTPEH TWSSRKT
//
