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Database: UniProt
Entry: A0A101HT06_9FIRM
LinkDB: A0A101HT06_9FIRM
Original site: A0A101HT06_9FIRM 
ID   A0A101HT06_9FIRM        Unreviewed;       645 AA.
AC   A0A101HT06;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE   Flags: Fragment;
GN   ORFNames=XD97_0383 {ECO:0000313|EMBL:KUK82641.1};
OS   Pelotomaculum thermopropionicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=110500 {ECO:0000313|EMBL:KUK82641.1, ECO:0000313|Proteomes:UP000054705};
RN   [1] {ECO:0000313|Proteomes:UP000054705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUK82641.1}.
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DR   EMBL; LGGS01000077; KUK82641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101HT06; -.
DR   Proteomes; UP000054705; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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}.
FT   DOMAIN          5..284
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          285..560
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   NON_TER         645
FT                   /evidence="ECO:0000313|EMBL:KUK82641.1"
SQ   SEQUENCE   645 AA;  73305 MW;  78CBDAB7F03BB34C CRC64;
     MTVLERLNPD QIKAVTYGDG PLLVLAGAGS GKTSVLTRRV AYLLKERRIS PYNILAITFT
     NKAAREMRER VEALVPEEVR ALWICTFHAA GLRILRRQTT FYGRDRNFIV YDAGDQLTVV
     KDCLKELEID EKKYPPRAVA WAVSQAKNRL LDATGFQRDA DDHFSRTVAE VYRLYQDRLQ
     RNNAVDFDDL IFLVVRLFQE YPQVLSYYRD RFRHILVDEY QDTNHAQYVL VNLLAGAHRN
     LFAVGDPDQG IYGWRGADIG NIMKFEKDYS EACVVKLEQN YRSTGTILDA ANYIIKNNYN
     RKEKRLWTAA DPGTPLVKHY CENEHDEAGF VAGSILRLKE IENRPYRDFA VLYRTHAQSR
     VIEETFVRGG VPYTIIGGLK FYERKEIKDI IAYLRLILNH SDALSLSRIA NVPRRGIGNA
     SLKKIFAFAG ERGISPVESL ARAVEIPGLT AKVRAGGAAL GTMLIEFSEA AVHSGVTSLT
     RTVLEQTGYL QELLAEKTVE ARTRIENLEE FLSVTGDFDR QAEEKGLRSF LENIALVTDL
     DQYDGDTDQV ALMTLHSAKG LEFPVVFLTG MEEGVFPHAR SLTEPGELEE ERRLCYVGVT
     RAKERVYLTN CWRRTLYGNQ RYNPPSRFLE EIPPHLVING DLVEG
//
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