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Database: UniProt
Entry: R6EV50_9BACT
LinkDB: R6EV50_9BACT
Original site: R6EV50_9BACT 
ID   R6EV50_9BACT            Unreviewed;       785 AA.
AC   R6EV50;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=BN691_01390 {ECO:0000313|EMBL:CDB04528.1};
OS   Prevotella sp. CAG:520.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262929 {ECO:0000313|EMBL:CDB04528.1, ECO:0000313|Proteomes:UP000018359};
RN   [1] {ECO:0000313|EMBL:CDB04528.1, ECO:0000313|Proteomes:UP000018359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:520 {ECO:0000313|Proteomes:UP000018359};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CDB04528.1}.
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DR   EMBL; CBCY010000061; CDB04528.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6EV50; -.
DR   STRING; 1262929.BN691_01390; -.
DR   Proteomes; UP000018359; 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   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; 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};
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:UP000018359}.
FT   DOMAIN          1..284
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          285..573
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          659..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   785 AA;  88907 MW;  99DF6BFBBFD5F17C CRC64;
     MNPNQLAAVE YTDGPELIIA GAGSGKTRVL TYKIAYLLQK GLAPWSILAL TFTNKAAREM
     KSRVAELVGE DRARYLNMGT FHSVFLRILR AEAEAVGLQR NFSIYDDGDS RGVVNSIIKE
     MQLDDKQYKA SAILGRIGAA KNSLVTPEVY MSDPHLLERD KVSSMPKLGQ IYAMYAARCK
     AANAVDFDDM LLFTYKLFAE NPQIAKKYAE RFCYVLVDEY QDTNYAQQAI LTLLTKEQRN
     ICVVGDDAQS IYAFRGANID NILKFQSIYE GARLFKLEQN YRSTQTIVKA ANSVIVNNQR
     QIRKEVFSEN GDGEKVHLNI AYSDKEEASV VCNEIRRLHN RYGVAYRDIA VLYRTNAQSR
     LFEEELRRQD TPYRIYGGMS FYQHKEIKDV IAYFRLVANP NDEEALKRVI NYPKRGIGDT
     TISKLIAASR ACNVSLWDVV GNPSMYNASV SAGTEKKVLG FYYLIDEFIR DNRTVDAYGL
     GKEILEKSGL KFELASDKTM EGAERQENIE EFMSGLHDFV DTKREEGYED EVYIANFLQE
     VALLTDSDEE NDNDNDASSN ERVSLMTIHA SKGLEFNSVF VVGLEENIFP SPRACSSVRE
     LEEERRLLYV AITRAEQRCF LSCAKSRYQY GSMMFNEPSR FLKEIDKQYL VIEGNAAGFK
     SQGSQPQPFQ SRPQSRSFQS RPQSQPYHET PQRNPFQSTV PSGFRRVQSV SQRFQTSASI
     QRMQASASSQ RQTIHAGARV EHQRFGLGTV VAVEGVGENE KATIEFQNAG TKTLLMKFAR
     LTVLK
//
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