ID A0A221R421_9MICC Unreviewed; 1109 AA.
AC A0A221R421;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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=CGQ25_04525 {ECO:0000313|EMBL:ASN51431.1};
OS Sinomonas sp. R1AF57.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN51431.1, ECO:0000313|Proteomes:UP000199767};
RN [1] {ECO:0000313|EMBL:ASN51431.1, ECO:0000313|Proteomes:UP000199767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1AF57 {ECO:0000313|EMBL:ASN51431.1,
RC ECO:0000313|Proteomes:UP000199767};
RA Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT Soils with Potential for Applications in Biocatalysis.";
RL Submitted (JUL-2017) 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; CP022463; ASN51431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221R421; -.
DR Proteomes; UP000199767; Chromosome.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000199767}.
FT DOMAIN 21..453
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 454..753
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1109 AA; 119678 MW; ED5C275003CE6E70 CRC64;
MSAVGTESMA PGVGNHGLGD HGVVDRDVLN RDILGNVAMI SASAGTGKTY TLTEKIVDHI
RAGVRPDQIM ATTFTKKAAG ELRERIAARL LDEGDSALGT ASQELGASLV GTVNSVCGQL
LSEYAIDAGL SPALEVIGED QLDAMFRLAT DEVLADHAET LSPVAWRMGT HPDQEAEYGT
EPWSTTVQRV VTYARTNLLD ADAVRACAER SWTEFREGLL DPASADNRTD WLRELHALRV
EMELTVARGE HSDGTKAKVS TKAFEEQYPK ALAKIAKAQA VETTPWEVWR GFVGSNPAAP
LKKVFWDLRE RIHAELLSNP AFHRDIEGYI RGVLTCAADC LDAYEEFKRD NALMDFVDQE
AKVLELARHN AAFRESFAGR IRVLVVDEFQ DTSPLQLALF LELSSLVGQA VWVGDPKQAI
YEFRGTDPEL MEAVMAAVPD ASRRQLSETW RSRQAPVDLS NAVFERVFAA HGMTTKSVHL
ELPPSKAAEY AGSVGSVEAW TRNQGKAEDR LRATAAGVAG LLALRPDLRP CDIAVLARSN
DEVKKLSAAL DELGLRASRN PRALGAAREV QLARAAMAYV ADGWDTVALA ELVALHPDHP
SHGTWQRELL AAVVPRPASP DALQEGAHDG GAAPEPVGAR AVHAAWRQAP VVAALDALRE
QAAAATPTEV FEAVTGVVGL PQLVAGWSAP ERRLRNLDAF RGAIELYYER CRALRSPATL
RGFLDFFASD DHDSAENAGP DVVNVLTYHK AKGLEWPVVV MESLDKESKL RPFGAGVEST
RALDLADPLA GRWIRLWPSP FPYGGSPLDT AAKASDAAAR FLERDQRSQA RLMYVGMTRA
AETTVLTSKT GSPGVLNDLG LGERFVSWKD GAVSIGGDTS VPARIEALEP AAAPASDGEW
LGRFVDAPVT TSAVARKPAR LKASESLAGG LDADIREVAV LGGRLAEHGS DDWGAVGSAV
HAYLGTEFRA LDDAGRLRLA ERLVARWDVG TTVDAALLTT AGERFEAWLD AEFPGWARHR
EAAIGWRPDG QTMEGWIDLL LEGPDGFVLV DHKTYPGTDP EGHIRAHYLG QMAAYRKAIE
AATGRPVLRV LMHLPALGRV FEVSGMSGA
//
