ID B4WSC2_SYNS7 Unreviewed; 784 AA.
AC B4WSC2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=S7335_3281 {ECO:0000313|EMBL:EDX85580.1};
OS Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX85580.1, ECO:0000313|Proteomes:UP000005766};
RN [1] {ECO:0000313|EMBL:EDX85580.1, ECO:0000313|Proteomes:UP000005766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034618,
CC ECO:0000256|RuleBase:RU364053};
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. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
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DR EMBL; DS989904; EDX85580.1; -; Genomic_DNA.
DR RefSeq; WP_006455328.1; NZ_DS989904.1.
DR AlphaFoldDB; B4WSC2; -.
DR STRING; 91464.S7335_3281; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_3; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000005766; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000005766}.
FT DOMAIN 9..341
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 342..617
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 784 AA; 89284 MW; B9D8746976FC591A CRC64;
MVTTVDFLNQ LNPAQRQSVE HFCGPLLVVA GAGSGKTRAL TYRIANLILN HRVDPENILA
VTFTNKAARE MKERIEKLFA EQESLARHGK PFHMLPEREQ IQLRSYIYKT FIKGLWVGTF
HALCARILRY DIEKYQSADG QRWTKSFSIF DESDAQSLVK SIVISGLNLD DRKFNPRSVR
FAISNAKNQG FTPDQYEQEN PHFKGRTIAE VYRLYQKGLS ANNALDFDDL IRMPVQLFRQ
NEQVLDYWHR RFRHILVDEY QDTNRTQYDL IQLLATNGKG KGFDDWNNRS VFVVGDADQS
IYSFRAADFT ILMGFQTEFG DGLTDDETQT LVKLEENYRS TSNILDVANH LIENNTERID
KILRATRGEG DSILCHRADN EAMEAEYVVG QIRNLELKNP ELQWQDFAIL YRTNAQSRAM
EEVLTRFGIP YRVVGGLRFY DRREIKDMLA YMRLAVNPAD SVSLKRIINT PRRGIGKTTL
DNLDKAASEL GVSLWEIIQD ETSVKTLAGR AGKKVTGFAE MIKGWQERVD SVGPAELVQD
VLEQTGYIDS LKSKGTEEDE TRIENIQELY NAVVQFEEEN EDATLLTFLA NASLSTDRDD
SDEGNQVTLM TLHASKGLEF PVVFLVGLEQ GLFPSFRSLE DAAAIEEERR LCYVGITRAQ
DRLFISHARE RRTYGHMREV STPSIFLSEL PRDYILTTVP SALPERWTTT TRQAKLKNPQ
PNLNKPGTHE NDWNVGASVN HKAFGKGKVT HIFGAGNKIC LAIHFPGIGK KIIDPRTTTI
ERLG
//
