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Database: UniProt
Entry: A8F5R7_PSELT
LinkDB: A8F5R7_PSELT
Original site: A8F5R7_PSELT 
ID   A8F5R7_PSELT            Unreviewed;       627 AA.
AC   A8F5R7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=Tlet_0935 {ECO:0000313|EMBL:ABV33501.1};
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33501.1, ECO:0000313|Proteomes:UP000002016};
RN   [1] {ECO:0000313|EMBL:ABV33501.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABV33501.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; CP000812; ABV33501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8F5R7; -.
DR   STRING; 416591.Tlet_0935; -.
DR   KEGG; tle:Tlet_0935; -.
DR   eggNOG; COG0210; Bacteria.
DR   HOGENOM; CLU_004585_5_10_0; -.
DR   Proteomes; UP000002016; 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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   PANTHER; PTHR11070:SF3; ATP-DEPENDENT HELICASE_DEOXYRIBONUCLEASE SUBUNIT B; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 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};
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:UP000002016}.
FT   DOMAIN          6..289
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          290..545
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   627 AA;  72548 MW;  1AB51F9E26F0DD85 CRC64;
     MEDYLQQLDD EQRTAVLKSA GRSIIIAGPG SGKTRVITYK LLHLLKTGIK PSEILLVTFT
     RAAANEMIDR ARMLTGIDLE GITAGTFHHI CNLILRRYAR KVGLFPNFTI LDEEDSKSLI
     KHVRTMVLER TGEIKHFPSH GVLQKIFSYA TNTMSTLHSA LLKINPKYID YEKIIEDIYR
     EYTIEKRNQN CVDYDDLLVF AVQVLQDSDI RLRESRKYKW ILVDEFQDTN ILQLNLIELL
     SSFHKNIVVV ADDSQSIYSF RGARYENVRD FMKIDGTKLF KIQTNYRSVE PIVKLINATI
     PKRSVPKVLR AVKFSDQKPI VIKTSDRQEE AAYVSKQILR LIEQGFDPEE IAVLYRSHSH
     SLELQIELSK QQIDFKILSG IRFTETAHVK DIIAFLRIIQ NPREKISWIR VARLFPGIGA
     KTASNLAEHA YGAALQNDVS SILDGFSQKK GQILEIKKLL SEMQEESTVS DKISFLYESF
     YQQYLQDNYP DYKERQQDIE RLIEVALRYN SLEHFLSDLT VNEDVQNNVS KGQKITLTTV
     HQAKGLEWDV VFVISVNPGD FPSYYALMEN NIDEEERIFY VAITRPRKLL YLVTQQYPSS
     PYMYWAKAVD FLQKIPEELV DIYDTSY
//
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