ID A0A0S8FZ97_9BACT Unreviewed; 966 AA.
AC A0A0S8FZ97;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AMS21_03430 {ECO:0000313|EMBL:KPK65957.1};
OS Gemmatimonas sp. SG8_38_2.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703358 {ECO:0000313|EMBL:KPK65957.1, ECO:0000313|Proteomes:UP000051763};
RN [1] {ECO:0000313|EMBL:KPK65957.1, ECO:0000313|Proteomes:UP000051763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_38_2 {ECO:0000313|EMBL:KPK65957.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK65957.1}.
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DR EMBL; LJTP01000023; KPK65957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FZ97; -.
DR PATRIC; fig|1703358.3.peg.2202; -.
DR Proteomes; UP000051763; 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 GO; GO:0004527; F:exonuclease activity; IEA:UniProt.
DR CDD; cd06127; DEDDh; 1.
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; 3.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; PF00929; RNase_T; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-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};
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 3..266
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 267..528
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 966 AA; 109674 MW; 323B86A5D6D35DC6 CRC64;
MDFEPFPKQR EAIESPLGPT LVLAGPGAGK TFCLIRRVEH LIDSRGFAPQ RICAVTFTNK
AAEEVTARLH RRMGARADGI TLGTLHALCL AILREYPQQV GLRRGFGVAD EDYQQLLLRR
LNVFPEQRRR GLLTLFGRHR LQGYQLTDND DAVFDNYISL LREKNLADFD DIIALTEVLF
RQHDEVADEV ATRWDYLLVD EFQDLDAAQY SILKRLAQDH RNFFAVGDDE QSIFSWRGSD
PRILWRFQND FEIEDAIILD KNLRCSRQIY HAARQLLREN PELFQKQIEA ERDSEFEVEA
RGFKDEEVEA GWVIDHLLTD KRASGLDWGE YALLYRKHDV GDYLENRLVA ADVPCRLARG
RSLLDDPVIA YVVASLRAVA APDDPVAVES FAQRMLPEHM VAEVRTLASS RSDDFMSALR
IYARQHPRDH PDTQKAWRFV YHVDNLRALH ESQDTLAGLV DELLSQRVKP YENRLEEHYD
ELQDPEEFPG ARDLADRLLS TLSAGGSVFL EGDSGKEIAL RGMLAAVNLP TAVHYLTSAA
EPRPHDLILA REKYPGRPLT TTLFKALQLI HSRDFGDILR DYVAFDIETT DLDTASCEII
ELGAAKVRAG EVVDTFHSLV RCEGPIDAGA SDVHGYTEED LRDAAPLSEV WRRFEAFAED
NVLVAHNGHR FDVPVIRRSV ADFADTSKLI FFDTLPLARS LFRESARLTD LAERFGVAPG
RAHHALDDSV TLARVFSGLN RQKRLRARKA ALVNLLDHVG LGLALEAKSR LDDEDRLLLK
IAAPYALGRF SDCLEFYATE RDRERTDAPE LDFAIRRLGG RAMMERIRAE RTPAERYPAA
MARLHSLIES RQGDSLEEAM QRFLERVALS TSEGVEADPH RVNLLTLHST KGLEFSRVYV
IGVEDYQLPG YYPVVNKRKE EIEEARRLLY VGMTRAKDRL VLTRVDRRRG KDAGGSIFLG
EIGLTL
//
