ID   A0A095C5V6_SCHHA        Unreviewed;       910 AA.
AC   A0A095C5V6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JUL-2024, entry version 37.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=MS3_05688 {ECO:0000313|EMBL:KGB37353.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB37353.1};
RN   [1] {ECO:0000313|EMBL:KGB37353.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22246508; DOI=10.1038/ng.1065;
RA   Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA   Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA   Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA   Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA   Wang J., Gasser R.B.;
RT   "Whole-genome sequence of Schistosoma haematobium.";
RL   Nat. Genet. 44:221-225(2012).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; KL250874; KGB37353.1; -; Genomic_DNA.
DR   RefSeq; XP_012797115.1; XM_012941661.1.
DR   AlphaFoldDB; A0A095C5V6; -.
DR   STRING; 6185.A0A095C5V6; -.
DR   GO; GO:0005694; C:chromosome; IEA:TreeGrafter.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:TreeGrafter.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:TreeGrafter.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:TreeGrafter.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KGB37353.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          37..200
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          235..403
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          669..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..703
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   910 AA;  103313 MW;  575F32173238F01E CRC64;
     MARPSQDGVY TALSDIFKLK NFKSKLQEQA THSVFEGSGK SLCFQLPSVM HSGVALVVSP
     LLALISDQLT HLKKLHIQAE TINSRTADTQ RRKLFHQLMS TPLGSKSYPK LLYITPEQLQ
     TPFSSSLISQ LYEKSCLSYF VVDEAHCVSE WGHDFRPAYL ALGRIRRKLF PAVPCIALTA
     TATPRVREDI IKCLGLGELS NYSPISSLGF AGNLEEFKCS IFRPNLYYDV VFGDLLDDVY
     ADVLQFAAES IGWDKSRKCD WTKLGCGIVY CRTRTDCEGL AEKLTSLGLS SRAYHAGLSK
     SEREDVQTGW SSGFYPIVVA TISFGMGVDK PNVRFVLHWT LPKSLAAYYQ ESGRAGRDGL
     QASCRIYYFK KERDTVVFLS NQQPNSGSQK SLNNTQCRKI DINTMVKYVE TAKHQQMGIY
     FKDEQAPCGN HCDVCVNASR VCMNLALFRA LEFTDQQREE YDKLERQKLI TSEFNKRRRD
     TDKLIQSSWV SAPDTTEVIS PDNRNVTGIT GWCRDQTLQL LTSAMKKLFP EHEALLNKLC
     ADAEYVLFKE SKVAAMYRTR MARLITFVRR PNVTKESVWN AVKSKADILL TRTNEKIKST
     DNSIENDNRK SALAEKGIIS SKHFHHKIKR SCSPETNKSN VQYSTPAVGK KLKLESEFAN
     FKSQCKSETI SPIKKSSSPD LSDDDDDDNN GKEIKRHPQL DPVMKGNEEL SNYEVTRDHV
     RIVRSDEVKH DINDNDNIDY KSKSYHTIPQ TGSIPELLIE PEKRLVYFWE QEDITNIPVD
     KQIHHKHRLV NPRAIVSIPT KTRHTEPNKE INSASTEMNS STAELAKQVV ASLSRHFAKG
     LFKNKDAFKS VAKKLTRKLL THHEVDIFTK SRLDQLIDQL LIHFVETKTQ IQVADDIDWS
     RLAGIFLRLP
//