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Database: UniProt
Entry: G5BDL1_HETGA
LinkDB: G5BDL1_HETGA
Original site: G5BDL1_HETGA 
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
//
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