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Database: UniProt
Entry: A0A1H3YMW1_9FIRM
LinkDB: A0A1H3YMW1_9FIRM
Original site: A0A1H3YMW1_9FIRM 
ID   A0A1H3YMW1_9FIRM        Unreviewed;       715 AA.
AC   A0A1H3YMW1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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};
GN   ORFNames=SAMN04515656_10432 {ECO:0000313|EMBL:SEA12906.1};
OS   Eubacterium aggregans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA12906.1, ECO:0000313|Proteomes:UP000199394};
RN   [1] {ECO:0000313|EMBL:SEA12906.1, ECO:0000313|Proteomes:UP000199394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR12 {ECO:0000313|EMBL:SEA12906.1,
RC   ECO:0000313|Proteomes:UP000199394};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- 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}.
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DR   EMBL; FNRK01000004; SEA12906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3YMW1; -.
DR   STRING; 81409.SAMN04515656_10432; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000199394; Unassembled WGS sequence.
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: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; 2.
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:UP000199394}.
FT   DOMAIN          12..287
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          288..547
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   715 AA;  81017 MW;  25A0F42CC69B650C CRC64;
     MDLTQYLERY AITLNAQQLE AMERIQGATL LLAVPGSGKT TVIICRLGYM IRELGISEDQ
     ILTLTFSRAG ARDLGQRYRS ILGGEGAAPR FSTIHSFALS VIRTYERQTG RRAFDVLQDV
     GAVIRALFRQ VFKSYPSDND IADILSAITY TKNLMLNKEE IAALKVGDLD FPRIYTAYEQ
     YKRKAHLMDF DDMLRYAWLL LKKYPALLAH FTERYRYINV DEAQDTSKIQ FELIHLLVAR
     WGNLFMVGDE DQSIYGFRGA YPQGLLDFET QYPQGKVLLM ETNYRSTGAL VASANRFITL
     NQERYPKKMT TPNALGVPAV QEYVKTLEDQ YRFLLNSVQK EGKETAVLYR NNESAIPLVD
     LFERQGVPYR LKEHNPLFFS HFVVRDILDF LALSEDPGDG EIFEKSYYKM NCGISKENMI
     QAIRQKKPGE TVFHALYTLP GIPEWLVERV QTQEAGFQRL KTLPMNRVVD YIEHQLGYGE
     HLAYRVEMGC REEQLTQKME ILKTLAKREE TRDGFRRRLS DLAAILRGET ESKGRGVLLS
     TIHSSKGLEF EKVFIIDAVD GEFPSRAALE PTEEGERLMN EEIRLFYVGV TRAKGELEFI
     SVGQKGRYNP TRPVSRFVEH YLGRRPVAKA AEKPITGGKS PGKRGLSMGT ASVRPEVMPK
     AAVPDHWGVG TIITHGGFGP GEITALEGET ATVRFERAGA KKLNLAICLS KGIIE
//
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