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Database: UniProt
Entry: Q97VY9
LinkDB: Q97VY9
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ID   HELS_SACS2              Reviewed;         708 AA.
AC   Q97VY9;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442};
DE            EC=5.6.2.4 {ECO:0000255|HAMAP-Rule:MF_00442};
DE   AltName: Full=DNA 3'-5' helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442};
GN   Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; OrderedLocusNames=SSO2462;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC       involved in repair of stalled replication forks. {ECO:0000255|HAMAP-
CC       Rule:MF_00442}.
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:0000255|HAMAP-Rule:MF_00442};
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=5.6.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00442};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00442}.
CC   -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00442}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK42601.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006641; AAK42601.1; ALT_INIT; Genomic_DNA.
DR   PIR; B90418; B90418.
DR   RefSeq; WP_010923869.1; NC_002754.1.
DR   AlphaFoldDB; Q97VY9; -.
DR   SMR; Q97VY9; -.
DR   STRING; 273057.SSO2462; -.
DR   PaxDb; 273057-SSO2462; -.
DR   EnsemblBacteria; AAK42601; AAK42601; SSO2462.
DR   GeneID; 7806244; -.
DR   KEGG; sso:SSO2462; -.
DR   PATRIC; fig|273057.12.peg.2540; -.
DR   eggNOG; arCOG00553; Archaea.
DR   HOGENOM; CLU_006553_3_0_2; -.
DR   InParanoid; Q97VY9; -.
DR   PhylomeDB; Q97VY9; -.
DR   EvolutionaryTrace; Q97VY9; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd18028; DEXHc_archSki2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00442; Helicase_Hel308; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048772; Hel308-like_dom4.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR022965; Helicase_Hel308.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; NF040935; helicase_Hel308; 1.
DR   PANTHER; PTHR47961:SF10; ATP-DEPENDENT DNA HELICASE HEL308; 1.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21280; Helicase_dom4_arc; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Isomerase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..708
FT                   /note="ATP-dependent DNA helicase Hel308"
FT                   /id="PRO_0000102112"
FT   DOMAIN          33..196
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   DOMAIN          229..435
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT   MOTIF           145..148
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   BINDING         28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
SQ   SEQUENCE   708 AA;  80500 MW;  D52C24C89541C780 CRC64;
     MSIDDLKLPS NVIDIIKNRG IKKLNPPQTE AVKKGLLDGN RLLLTSPTGS GKTLIAEMGI
     ISFLLKNGGK AIYVTPLRAL TNEKYLTFKD WESIGFKVAM TSGDYDTDDA WLKNYDIIIT
     TYEKLDSLWR HRPDWLNEAN YFVLDELHYL NDPERGPVVE SVTIRAKRRN LLALSATISN
     YKQIAKWLGA EPVATNWRPV PLMEGVMYPE RKKKEYTILF RDNTARKVHG DDAIIAYTLD
     SLSKNGQVLV FRNSRKMAES TALKIANYMN FVSLDEKAIS EILKQLDDIE EGGSDEKELL
     KSLISKGVAY HHAGLSKALR DIIEESFRKR KIKVIVATPT LAAGVNLPAR TVIIGDIYRF
     NRKIVGYYDE IPVMEYKQMS GRAGRPGFDQ IGESIIVVRD KEDVDRVFKK YILSDVEPIE
     SKLGSERAFY TFLLGILSAE GSLSEKQLEA FAYESLLAKS VVDVYFDRAI RWLSEHSFIR
     EENNTFTLTN FGKRVADLYI NPFTADIIRK GLEGYKASCE IAYLHLLAFT PDGPLVSVGR
     NEEEELIELL EDLECELLVE EPYEEDEYSL YLNALKVALI MKDWIDEVDE DTILGKYNIG
     SGDLRNIVET MDWLTYSAYH LSKELRLDDH SDKLRILNLR VTDGVKEELL ELVQIGGVGR
     KRARLLYNNG IKGLGDVVMN PDRVRNLLGQ KLGERVVQEA ARLLNRFH
//
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