ID A5UJE0_METS3 Unreviewed; 819 AA.
AC A5UJE0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, 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 OrderedLocusNames=Msm_0113 {ECO:0000313|EMBL:ABQ86318.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86318.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86318.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86318.1; -; Genomic_DNA.
DR RefSeq; WP_011953690.1; NZ_CP117965.1.
DR AlphaFoldDB; A5UJE0; -.
DR STRING; 420247.Msm_0113; -.
DR EnsemblBacteria; ABQ86318; ABQ86318; Msm_0113.
DR GeneID; 78816738; -.
DR KEGG; msi:Msm_0113; -.
DR PATRIC; fig|420247.28.peg.117; -.
DR eggNOG; arCOG00798; Archaea.
DR HOGENOM; CLU_004585_6_3_2; -.
DR BioCyc; MSMI420247:GHWZ-114-MONOMER; -.
DR Proteomes; UP000001992; Chromosome.
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 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.
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 20..352
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 819 AA; 94640 MW; 1252703AD899BB47 CRC64;
MISYEEFEDI VVNTLKRNIS SNEDQKKAIS SHANESLFIV AGPGSGKTTV IVLKILKYIF
VDDIAPDEIL ATTFTRKAAN ELHSRILSWG DQIKNYLLDN IVEDDPVKEM ELMDFIEKKI
DLNKINIGTT DSVAEDLLRI HREPGTNQPL VIEDFVTKSA MTNILLKDNI YLNENLKEYL
KSFTPKEKLE EPSKMAEIIL NMKNRMYYDQ VNFDEIYDKF EEGSGAKLTL NCIKDYEDEL
KKRNIIDFPM LEFKFLNKLK NHKLDIFLDN IKIILIDEYQ DTNLIQEDIY FTIAEYGLKN
NGSITVVGDD DQSLYRFRGA TVDLFTNFKK RAHDRLGINV EEINLKTNYR SSENIINHCN
HFVELDKEYQ KARVDEKPKI IAPDFDKDKM PVLGMFRNNP QMLARDLTLL INNLINNGEA
SLKIRRILNK DYYDTLNGNS NLQSINKQKQ NNAKKSKNLE KITLKLDEEY GSASDIAILS
YSPKEMKGSN PTFNFYLRKN LKKLKKPIEV FNPKGRDLQD VKQVEIFCGL ILECIDPQGI
IQKSDKQIQN LADRNMNRWR YRAIDHIKSK PEPNEPVSLS EFVISWQNRH PKNRDKWPES
ASLMELAYKL ITWIEELQDD VEGIVYLEAI TRSIKQTGFF NKYSGNIVFT NSKTERESVL
EAIWNIFIPI ATGGVGIDED LLETLPDDRI NIMSIHQSKG LEFPLVIVDV GSRFKKNTVN
TQNLRFPKLE PKNRSIEDSV RCFSSLGESE RSEKDRSFDD LTRLYFVAFS RAENVLLLIG
LLPSLDGYAV NNNLKQIPNV ALGWNRDEQL VGFDEIYLI
//
