ID A0A1F9VS27_9BACT Unreviewed; 905 AA.
AC A0A1F9VS27;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=A3G41_06180 {ECO:0000313|EMBL:OGS05728.1};
OS Elusimicrobia bacterium RIFCSPLOWO2_12_FULL_59_9.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797952 {ECO:0000313|EMBL:OGS05728.1, ECO:0000313|Proteomes:UP000176685};
RN [1] {ECO:0000313|EMBL:OGS05728.1, ECO:0000313|Proteomes:UP000176685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGS05728.1}.
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DR EMBL; MGUX01000007; OGS05728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9VS27; -.
DR STRING; 1797952.A3G41_06180; -.
DR Proteomes; UP000176685; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 CDD; cd18807; SF1_C_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; 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; 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.
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}; 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 1..268
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 269..549
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 905 AA; 102873 MW; FBB4A6BA0FC31424 CRC64;
MAYRGGHLQV IACAGSGKTE SISRRVAELI NEGNPPESIT AFTFTEKAAA ELKERIYSCV
EAKKGHEFLG RLGPMFVGTI HGYCFRLLQD YVPNFGNYDV LDEHRHSGLL SRAFSDIGLQ
KLKRRNVIKD FLHSADVISN ELLDARHLAG TPLGECYEAY VSTLERYHFL SFGLIIAQAV
EELKNPATYK RVHGPLRHLI VDEYQDINPA QERLIELLAR DPVQLCVVGD DDQAIYQWRG
SDLSNIINFK KRWKGVQKIE LDVNRRSRPE IIRTANEFAK TIPDRFDKAM REKRPGAAHE
VISWCADTDA AEAKKIAETI ARLSTKGVPY GGIAILYRSV RTSSPPIIEA LEQAEIPYQC
AGRTGLFLQP EINLFGEIYA WLTEGEWRDE QYAPKRATAI AHVVADISRL FRLKGTAVKN
FRDYLEDWKS NRLHGKRPVN LVGDFYDLLF RLGAHEFDLS IPRQAARFGA FARFSRILAD
FEHVTRRGRY VVEEGQRVFR GGRDRGPEYH KRLHKYLLYY ARDAYEDFDG EPIFTSDAVS
IITVHQAKGL EWPVVFLPAL TDRRFPSGRA GKEKDWLLPE AIFPKEKRKR YEGGDAEERR
LFYVAMTRAR DALYLSYFEK KKNSFKPSPY LLQAAKMTGG LKRCASLPLP DLTRDAAEEK
PPLLEIGFSD IASYEDCGHR YRLASSLDFQ QKLVIELGYG KAIHHILRHV AEIVRATGKV
PSRREAEKIV ADKFYLPFAD NPTFERMVKA ASKVLGRYLD KHSEDLKRVW AIERPFEIHL
PDAIITGKAD VILDHEQGLP GRLVIVDYKS TEDPERSERY EQQVAVYAAA GRGEGLTVEA
GYLHNLSNGS RQAVDVSAAR TQEAVARLRK AVDGIRKAQF DPKPEEKKCS ACDYGRICRF
SKADR
//
