ID D4JUP3_9FIRM Unreviewed; 949 AA.
AC D4JUP3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=EUS_17220 {ECO:0000313|EMBL:CBK96812.1};
OS [Eubacterium] siraeum 70/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK96812.1, ECO:0000313|Proteomes:UP000008803};
RN [1] {ECO:0000313|EMBL:CBK96812.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK96812.1,
RC ECO:0000313|Proteomes:UP000008803};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum 70/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK96812.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK96812.1,
RC ECO:0000313|Proteomes:UP000008803};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929044; CBK96812.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JUP3; -.
DR KEGG; esu:EUS_17220; -.
DR PATRIC; fig|657319.3.peg.2031; -.
DR HOGENOM; CLU_004585_6_0_9; -.
DR BioCyc; ESIR657319:G136K-1460-MONOMER; -.
DR Proteomes; UP000008803; 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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 3: Inferred from homology;
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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}.
FT DOMAIN 5..302
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 949 AA; 111231 MW; 9B24BBD30D0BF966 CRC64;
MFDFGIANER QKEAVTCTEG PLLIIAGPGT GKTFTLVKRI AYLVFEKGVK PSEIMAITFT
EKAAHQLVTR ISDEFLRYSG CENINIDEMY IGTFHSVCLR LMKEYSELLP FDADKRIIDS
FEQQYMVYNN LERFRSVKGY CRSNFNNMSK WEQAKAICKY TSTMSEELLS RDKLLDDKDA
DILVIAKVWD EYDKLLTENN ATDFSTIQAD AWRMMQNSDI FASVREKIRY VMVDEYQDTN
HIQEQLILAI GGKHGNICVV GDDDQGLYRF RGATIRNIFE FPKHFGENEC RVIKLEENYR
SEKGIIDLYN NWMTNPEYKR KFDWGKYRYP KQIYTSKNET YSSVYTCKGT YDEPARVKLA
EMIKRMKQNG TVTDYNQIVF LFKSVRNDEA KKTAEFLEES GIPVYTPRSK LYFERAEVKQ
IIGCLICCFR TFTCFLKQQK DADKPSKISR YYISDCMPLS SGLLKENKEL YRCISEIAND
IAGCKDKTEY TLLSIFYRII AFEPFRSYIE NPDGSNARQA RNLAEMSNII SKFCYIHDMH
LIGADNRDTL SEEFFERYLR LLKDEGVGEY EDEAEYAPEG CVSFMTIHQA KGLEFPVVIV
GSLPLKKESE SKDSFFYSVE SRFCRKPFEA PDMIPYFDMW RKYYVAFSRA KNLLVLTEKD
GSRTKPFTSV ITENIPDISE YNDNRVFDRV KKEHIRKTYS FTSHISVYDE CPSRYLYFKE
YKFAPCEILH TSVGTLIHAT LEDLNRFAIA SRYDEITEVL IKKWFALNYA KMQESTGLML
SEERRKSALG QVLNYFDKRK EHIRKVWKAE EKVELVLPEY ILQGVIDLIE DDDGKIEIVD
YKTGRKPDSP EKSAQVEHYR KQLEIYAYLI SERYKKNVSR MHLYYTNEAE GNPLVTFEYS
KNCVDKEIED VSQTVRKIEG KRFDAKAEND YSCRYCDMKY MCKKVKNYD
//
