ID G5BDL1_HETGA Unreviewed; 1719 AA.
AC G5BDL1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=GW7_18186 {ECO:0000313|EMBL:EHB07372.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB07372.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB07372.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH169665; EHB07372.1; -; Genomic_DNA.
DR STRING; 10181.G5BDL1; -.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; G5BDL1; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EHB07372.1};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000313|EMBL:EHB07372.1};
KW Helicase {ECO:0000313|EMBL:EHB07372.1};
KW Hydrolase {ECO:0000313|EMBL:EHB07372.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EHB07372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 279..371
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 396..459
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 500..670
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..950
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1351
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 197567 MW; 5AF24D35133F30D8 CRC64;
MNGHSDDESV RNSSGESSPS DDDSGSASGS GSGSSTGSSS DGSSSQSGSS DSDSGSESDS
QSESESGTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA MLKKQQQQQQ QQQQQQQQQQ
HPASSNSGSD GDSSSSDDSD DSSSDVKRKK HKDEDWQMSG SGSASQSGSD SESEEERNKS
SCDETESDYE PKNKVKSRKP QNRSKSKNGK KILGQKKRQI DSSEDDDDEE DYDNDKRSSR
RQATVNVSYK EDEEMKTDSD DLLEVCGEDV PQPEEEEFET IERFMDCRIG RKGATGATTT
IYAVEADGDP NAGFEKNKEP GEIQYLIKWK GWSHIHNTWE TEETLKQQNV RGMKKLDNYK
KKDQETKRWL KNASPEDVEY YNCQQELTDD LHKQYQIVER IIAHSNQKSA AGYPDYYCKW
QGLPYSECSW EDGALISKKF QACIDEYFSR NQSKTTPFKD CKVLKQRPRF VALKKQPSYI
GGHEGLELRD YQLNGLNWLA HSWCKGNSCI LADEMGLGKT IQTISFLNYL FHEHQLYGPF
LLVVPLSTLT SWQREIQTWA SQMNAVVYLG DINSRNMIRT HEWMHPQTKR LKFNILLTTY
EILLKDKAFL GGLNWAFIGV DEAHRLKNDD SLLYKTLIDF KSNHRLLITG TPLQNSLKEL
WSLLHFIMPE KFSSWEDFEE EHGKGREYGY ASLHKELEPF LLRRVKKDVE KSLPAKVEQI
LRMEMSALQK QYYKWILTRN YKALSKGSKG STSGFLNIMM ELKKCCNHCY LIKPPDNNEF
YNKQEALQHL IRSSGKLILL DKLLIRLRER GNRVLIFSQM VRMLDILAEY LKYRQFPFQR
LDGSIKGELR KQALDHFNAE GSEDFCFLLS TRAGGLGINL ASADTVVIFD SDWNPQNDLQ
AQARAHRIGQ KKQVNIYRLV TKGSVEEDIL ERAKKKMVLD HLVIQRMDTT GKTVLHTGSA
PSSSTPFNKE ELSAILKFGA EELFKEPEGE EQEPQEMDID EILKRAETHE NEPGPLTVGD
ELLSQFKVAN FSNMDEDDIE LEPERNSKNW EEIIPEDQRR RLEEEERQKE LEEIYMLPRM
RNCAKQISFN GSEGRRSRSR RYSGSDSDSV SEGKRPKKRG RPRTIPRENI KGFSDAEIRR
FIKSYKKFGG PLERLDAIAR DAELVDKSET DLRRLGELVH NGCIKALKDS SSGTERTGGR
LGKVKGPTFR ISGVQVNAKL VISHEEELIP LHKSIPSDPE ERKQYTIPCY TKAAHFDIDW
GKEDDSNLLI GIYEYGYGSW EMIKMDPDLS LTHKILPDDP DKKPQAKQLQ TRADYLIKLL
SRDLAKKEAV RLSGAGGLKR KKGRVKKNKA MKSIKVKEEI KSDSSPLPSE KSDDDDDKLG
ESSSESKERS KKSSVLDAPV HITASGEPVP ISEESEELDQ KTFSICKERM RPVKAALKQL
DRPEKGLSER EQLEHTRQCL IKIGDHITEC LKEYANPEQI KQWRKNLWIF VSKFTEFDAR
KLHKLYKHAI KKRQETQQNS DQNSNLNAHV IRNPDVERLK ENTNHDDSSR DSYSSDRHLS
QYHDHHKDRH QGDSYKKSDS RKRPYSSFSN GKDHRDWDHY KQDSRYYSDR EKHRKLDDHR
SRDHRSNLEG SLKERSHSDH RSHSDHRVHS DHRSSSEYTH HKSSRDYRYH SEWQMDHRAS
SSGPRSPLDQ RSPYGSRSPF EHSIEHKSTP EHTWSNRKT
//