HELS_SULTO
ID HELS_SULTO Reviewed; 704 AA.
AC Q974S1; F9VN44;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00442};
DE AltName: Full=ATP-dependent Holliday junction unwindase Hjm;
DE Short=StoHjm;
GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; OrderedLocusNames=STK_05900;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP ACTIVITY REGULATION.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=18782564; DOI=10.1016/j.bbrc.2008.08.150;
RA Lu S., Li Z., Wang Z., Ma X., Sheng D., Ni J., Shen Y.;
RT "Spatial subunit distribution and in vitro functions of the novel trimeric
RT PCNA complex from Sulfolobus tokodaii.";
RL Biochem. Biophys. Res. Commun. 376:369-374(2008).
RN [3]
RP FUNCTION AS AN ATPASE, FUNCTION AS A HELICASE, COFACTOR, ACTIVITY
RP REGULATION, INTERACTION WITH HJC, SUBUNIT, AND DNA-BINDING.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=18296528; DOI=10.1128/jb.01662-07;
RA Li Z., Lu S., Hou G., Ma X., Sheng D., Ni J., Shen Y.;
RT "Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication
RT fork regression and interacts with Hjc endonuclease in vitro.";
RL J. Bacteriol. 190:3006-3017(2008).
RN [4]
RP FUNCTION, INTERACTION WITH HJC, DOMAIN, AND DNA-BINDING.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=22062475; DOI=10.1016/j.dnarep.2011.10.009;
RA Hong Y., Chu M., Li Y., Ni J., Sheng D., Hou G., She Q., Shen Y.;
RT "Dissection of the functional domains of an archaeal Holliday junction
RT helicase.";
RL DNA Repair 11:102-111(2012).
CC -!- FUNCTION: An ATP, Mg(2+)-dependent DNA 3'-5' and 5'-3' helicase that
CC may be involved in repair of stalled replication forks. Stimulated by
CC both ss and dsDNA. Unwinds both leading and lagging strands in
CC replication fork structures, unlike orthologs in P. furiosus and M.
CC thermautotrophicus which only unwind the lagging strand and only have
CC 3'-5' helicase activity. Preferentially binds dsDNA with overhangs or
CC branched DNA. Able to anneal DNA substrates that could form a
CC replication fork-like structure, has replication fork reversal activity
CC (at least in vitro). {ECO:0000269|PubMed:18296528,
CC ECO:0000269|PubMed:22062475}.
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:0000255|HAMAP-Rule:MF_00442};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18296528};
CC -!- ACTIVITY REGULATION: Helicase activity is inhibited by Hjc
CC (PubMed:18296528) and by PCNA123 and PCNA323 (PubMed:18782564).
CC {ECO:0000269|PubMed:18296528, ECO:0000269|PubMed:18782564}.
CC -!- SUBUNIT: Monomer; forms a 1:2 complex with Hjc, which may form a
CC complex with Holliday junction DNA. {ECO:0000255|HAMAP-Rule:MF_00442,
CC ECO:0000269|PubMed:18296528}.
CC -!- DOMAIN: DNA-binding occurs via the first 2 N-terminal domains, which
CC are also responsible for ATPase. {ECO:0000269|PubMed:22062475}.
CC -!- DOMAIN: The central region (432-645) which is structurally composed of
CC 2 domains (432-500 and 501-645) is necessary for helicase activity.
CC {ECO:0000269|PubMed:22062475}.
CC -!- DOMAIN: The C-terminal region (646-704) inhibits ATPase and helicase
CC activity. {ECO:0000269|PubMed:22062475}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00442}.
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DR EMBL; BA000023; BAK54341.1; -; Genomic_DNA.
DR RefSeq; WP_010978569.1; NC_003106.2.
DR AlphaFoldDB; Q974S1; -.
DR SMR; Q974S1; -.
DR STRING; 273063.STK_05900; -.
DR EnsemblBacteria; BAK54341; BAK54341; STK_05900.
DR GeneID; 1458536; -.
DR KEGG; sto:STK_05900; -.
DR PATRIC; fig|273063.9.peg.671; -.
DR eggNOG; arCOG00553; Archaea.
DR OMA; MFLNANI; -.
DR OrthoDB; 9752at2157; -.
DR BRENDA; 3.6.4.12; 15396.
DR Proteomes; UP000001015; 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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00442; Helicase_Hel308; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..704
FT /note="ATP-dependent DNA helicase Hel308"
FT /id="PRO_0000102113"
FT DOMAIN 36..200
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 235..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT REGION 366..645
FT /note="Binds Hjc"
FT REGION 432..644
FT /note="Required for helicase activity"
FT REGION 646..704
FT /note="Inhibits intrinsic ATPase, and helicase"
FT MOTIF 148..151
FT /note="DEAH box"
FT BINDING 31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
SQ SEQUENCE 704 AA; 79719 MW; 74B5737F218AC524 CRC64;
METISIDDLP LDIKIIDILK RRGIRTLNPP QSEAIRKGLL DGKRLLVTSP TASGKTLIAE
LGMINYLLSK GGKAIYITPL RALTNEKYNT FKDWETLGIK TGMTSGDYDT DDAWLENYDI
IVTTYEKLDS LWRHKAKWLN EVSYFVLDEF HYLNDPERGP TVESVAIRAK KRGIVLGLSA
TISNGKEIAN WLNAELVATN WRPVPLKEGI IYPEKKGFVV VYKDNTSRKV YGDDAIIAYT
LDIVSKGGQV LVFRSSRKLA ENTARKIVQY MNFVKLEDKK LLEIARKIKE VEDAGSNEKE
DLYNLVLRGV AYHHAGLSKG LRDIIESSFR DRILKVIVAT PTLAAGVNLP ARAVVIGDIY
RYNRKVVGYM DLIPVMDYKQ MSGRAGRPGF DENGEAVVVV RNKREAEKVY ERYLMSDVEP
IESKLGSESA FYSFLISIIA SEGEKTTEEL MEYVKETLLP KELAKKYFRS GLDWLLQHDI
FAEISDKITL TRFGRRISDL YINPFTAVTI REALEKNEKG CEIAYLHLLA YTPDGPSIGV
SRAEEDALID ELNCELFVDE PEDEYEFSNY ISALKVAYIV YDWVNEIDED TILGKYGIGS
GDLRAIIDTM DWLTYSGYHV ASVLELKDHK DILEELHARV KDGVKPELIE LVKIPGIGRV
RARLLYQHDI KKPEDIVLNP EKVKQLLGPN LGEKIVREAA RTIA
