ID W6U2T0_ECHGR Unreviewed; 977 AA.
AC W6U2T0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=EGR_09765 {ECO:0000313|EMBL:EUB55388.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB55388.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB55388.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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:EUB55388.1}.
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DR EMBL; APAU02000165; EUB55388.1; -; Genomic_DNA.
DR AlphaFoldDB; W6U2T0; -.
DR STRING; 6210.W6U2T0; -.
DR EnsemblMetazoa; XM_024499014.1; XP_024346584.1; GeneID_36345480.
DR OMA; PNIQRMI; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000019149; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 6.10.250.3140; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF159; ATP-DEPENDENT DNA HELICASE Q5; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 30..213
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 250..414
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 108770 MW; 6CDD07FD358EF0D1 CRC64;
MDNTDRVLGA LRNTFHHDQF KSKLQEDAIR CIVEGSHNAF ISMPTGSGKS LCYQLPAVLQ
DGLSIIISPL IALIYDQLSH LSELKIPAAT LNSKQSAKER ADIMERLLCP SECLGRLTLP
KIKLLYITPE QCETDGFRSL ANKLIELHSV KYFFVDEAHC VSEWGHDFRP AYLKLGNLRS
TLFPTVPCIA LTATANSRVK ADIISTLKLN PEASQEESCL LITKFREFVT GVFRSNLYYD
VMFSDLIKTP YDDLSLFIRQ CLFGEDPVKS PVKNSSGIVY CRTREDCETV AYQLSLRGIP
SRAYHAGLGS KDRTRVQEEW FKGDFLVVVA TISFGMGVDN AHVRCVVHWT VPKSLAAYYQ
ESGRAGRDGL PSHCRIYYAK QERDTVAFLV GQMSERALTQ KKKEHREKGV QDLALMINYV
ESVKCRHAQF AAYFGDDIPS CVNRCDVCTN PTKVSHLLAG YRRVIYGSLV KGVAVDENEE
LDTDLYRIGP RRKGKGWEVY DVDEGRFVAK EGRDFEEEAR NQRTKFVLEE LSRRRKAGEA
AGLGVPWISA AEDSLLIDPE SKLINGLTGK TRDQTLQLLI TAVCGHLTST SDTGSDVDPE
KSHLSKLAAQ LEHQIFKTSK VAGVYRGHMA RRISQARKAA SLSAVYDAFA EWLNVPVTSL
HPVNSNTPSS FSETLTLKPE EVDVRPSPPP PLLSSPPAPL LLPIEAKSAS PHPGSFLPKP
QSLSIGVNTQ DILESTCLPP SLKKSLIGDS SDKPNEENLP TILRSSGEST MTYFWEKSKP
TPSAQKRPQM EDPDDDVSVV KVIKKEGPSK TYFLLQDPAP LPSQSSQPPP LSASSQNVPP
PLGLMTKTGT PVVEPVPPAF TDFSPYDYRS EETRMKTSFI ANVVVRSLSR YYSLGAFKDK
ATFKDVAREL TRRLVKSGIS DDEVQREISR ITNRLVAPHR RLSGDSRTRR PVPISRLDDL
AWTEALSDIR TNRVQSI
//
