ID W0GQ59_9MOLU Unreviewed; 734 AA.
AC W0GQ59;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=P344_01855 {ECO:0000313|EMBL:AHI57719.1};
OS Spiroplasma mirum ATCC 29335.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=838561 {ECO:0000313|EMBL:AHI57719.1, ECO:0000313|Proteomes:UP000019260};
RN [1] {ECO:0000313|EMBL:AHI57719.1, ECO:0000313|Proteomes:UP000019260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMCA {ECO:0000313|EMBL:AHI57719.1,
RC ECO:0000313|Proteomes:UP000019260};
RA Landry C.A., Bastian F.O., Thune R.L.;
RT "Complete genome sequence of Spiroplasma mirum suckling mouse cataract
RT agent.";
RL Submitted (SEP-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006720; AHI57719.1; -; Genomic_DNA.
DR RefSeq; WP_025317125.1; NZ_CP006720.1.
DR AlphaFoldDB; W0GQ59; -.
DR STRING; 838561.P344_01855; -.
DR KEGG; smia:P344_01855; -.
DR KEGG; smir:SMM_0308; -.
DR PATRIC; fig|838561.3.peg.353; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_14; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000019260; 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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000019260}.
FT DOMAIN 7..287
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 288..561
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 734 AA; 84443 MW; B1A998EB7460658F CRC64;
MLNEFIKDLN PNQREAVLAI NGPVRVIAGA GSGKTRVIIN KIAYLVRYGN HKPWRICALT
FTNKAANEMK NRIVNLIGQE GRKTWISTYH ALCVRILRED IETLGYPRSF KIIDTTDQDQ
IIRAIYKSAN LKYDAQESWM VKSQISSWKN DFYSPSQVID GAYENSDKKR WGYVYKEYEK
RLKELNSLDF NDLILFTHRL FSYHKDILAK WQDRFDYLLV DEFQDTNDLQ FDIIKWLSET
KKNITVVGDP DQTIYSWRGA KIRLILNFEH YFKETQTIIL DENYRSSQNI LSLANDLIVN
NANRIKKELF TSKELGVKPI LYHASSSLDE SDFVASKINQ LVKKENYHYQ DILILYRANY
LSRDIEGSLA DYGISYRIYG AFKFYERKEI KDALALLKLV VNNEELSLDR VLLFTPKIGP
KAVEQVKAIL KEHQLSFNQL LLDHFDLLPN SLKNNLTALS EAIFDANSLL QDTQSVKIVI
ETLLEKSGYL KRLQDNLETE RVENIKELID GIAKFDFQNS DLQGLELVNE YLQLISLQTD
HDNDEINDDS VSLMTIHNAK GLEKKVVFIV GLNEGIFPSI QAIKSGESEL EEERRTLYVA
ITRAKELLFI SYADGYSYVT GNERFPSRFV KELNPDFLEI IESDLLGTTV KYKSNYSLDS
EWENSLNNFS NKALNTRSQS AQENWSIDDG VSHEIFGIGV VVKKIGSNIQ VIFPSPIGSK
IISADSKAIK KVKN
//