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Database: UniProt
Entry: U2QNS5_9BACT
LinkDB: U2QNS5_9BACT
Original site: U2QNS5_9BACT 
ID   U2QNS5_9BACT            Unreviewed;      1060 AA.
AC   U2QNS5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=HMPREF9135_1308 {ECO:0000313|EMBL:ERK40427.1};
OS   Segatella baroniae F0067.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40427.1, ECO:0000313|Proteomes:UP000016648};
RN   [1] {ECO:0000313|EMBL:ERK40427.1, ECO:0000313|Proteomes:UP000016648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0067 {ECO:0000313|EMBL:ERK40427.1,
RC   ECO:0000313|Proteomes:UP000016648};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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   -!- 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:ERK40427.1}.
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DR   EMBL; AWEY01000004; ERK40427.1; -; Genomic_DNA.
DR   RefSeq; WP_021588464.1; NZ_AWEY01000004.1.
DR   AlphaFoldDB; U2QNS5; -.
DR   PATRIC; fig|1115809.3.peg.89; -.
DR   Proteomes; UP000016648; 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   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000016648}.
FT   DOMAIN          1..469
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          493..743
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1060 AA;  123297 MW;  7F83EDBD666EF440 CRC64;
     MASLTIYRAS AGAGKTFTLA VEYMTLLINN PYDFKRILAV TFTNKATEEM KLRILSQLYA
     LAYLTGAKKN DYLLQIQDKT GLGEGVVRER AKMALHLLLH NFNYFRVETI DKFFQTVLRN
     LARELELNAN LTVALNDIQI EEKAVDEMIE ELDGKSPVLH WIMEYISDSM QDDKSWNVID
     KIKDFGRNIF KDEYKANVAG INERFHEKGF FNAFKKQLKS IEEEGDRHIK EQGDAFFELL
     EQHGLQESDF KKNAVNYFTK LKTGRYVDEG EKNIVYNKSA REAAESADGW VRKADKTAGN
     AAYELAESRL VEFISESETL RKRQLRQILS ARMIRQHIDQ LRLLKYIEEK VRDINNDHNR
     FLLSNTQTLL HDLIGQSDSP FIFEKIGVML EHIMIDEFQD TSNIQWNNFK VLLKECMSHE
     NAFNLIVGDV KQSIYRWRDG NWRLLNKLEQ QFNPQQVESE TLATNYRSDA NIIHFNNKFF
     TFARQEEYDA LVKDTPAEAE ELLKAYSDVA QQIPMGKDEA RGLVEIKLLE SKSNSYVTET
     LEHVGRKVQE LLDAGARESD IAILVRNNST IQDIGDYFME HMPHVRLVSD EAFHLDAALA
     VNMLVMAMRV IADPTDQIAK AALLLNHRKN IKKTEERVTD ILIKGKSVDE QLPAAFIQHL
     EELSVMPVMD MVEKLYHIFD LKDLDKQSAY VCAFFDELGN YLNENVADVV SFLKYWDEDL
     HKKSIQSSEQ KGIRLITIHK SKGLEFDHVI MPFCDWLLEK RNTIWCKPTE APYDQLSLIP
     VDFDKNKMLN SIFAQDYKIE HLQNMVDNLN LLYVGFTRAK RNLFVFGQKG CSDKNRSKLI
     EDFIKGDSYS FGELDIPVEK ERDETKTDNI FEVKPQDVAI QIENYKTIVD FRQSNKSKDF
     VNGEEDDEGT QRQYIKMGNV FHQIFASIRT TADIPTVLAT LEHDGVLFDN YLTYDKVKTM
     LQRRFDNPTV KDWFSDRWDL HNECSILRYD SIAGKLLERR PDRVMTDGQE MIVVDFKFGT
     PKEEHRRQVS EYMQLLREMG HANVKGYLWY VYTNKIDEVK
//
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