ID F9D4Z5_PREDD Unreviewed; 857 AA.
AC F9D4Z5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=uvrD {ECO:0000313|EMBL:EGQ13416.1};
GN OrderedLocusNames=Prede_1741 {ECO:0000313|EMBL:AGB29040.1};
GN ORFNames=HMPREF9136_1923 {ECO:0000313|EMBL:EGQ13416.1};
OS Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043
OS / ES 2772) (Mitsuokella dentalis).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=908937 {ECO:0000313|EMBL:EGQ13416.1, ECO:0000313|Proteomes:UP000007820};
RN [1] {ECO:0000313|EMBL:EGQ13416.1, ECO:0000313|Proteomes:UP000007820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3688 {ECO:0000313|EMBL:EGQ13416.1,
RC ECO:0000313|Proteomes:UP000007820};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000010862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772
RC {ECO:0000313|Proteomes:UP000010862};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome 2 of Prevotella dentalis DSM 3688.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGB29040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3688 {ECO:0000313|EMBL:AGB29040.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome 2 of Prevotella dentalis DSM 3688.";
RL Submitted (FEB-2012) 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; CP003369; AGB29040.1; -; Genomic_DNA.
DR EMBL; AFPW01000028; EGQ13416.1; -; Genomic_DNA.
DR RefSeq; WP_005846553.1; NZ_GL982489.1.
DR AlphaFoldDB; F9D4Z5; -.
DR STRING; 908937.Prede_1741; -.
DR KEGG; pdt:Prede_1741; -.
DR PATRIC; fig|908937.9.peg.1842; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_8_10; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000007820; Unassembled WGS sequence.
DR Proteomes; UP000010862; Chromosome 2.
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; PF21196; PcrA_UvrD_tudor; 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:UP000010862}.
FT DOMAIN 9..295
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 296..582
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 664..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 857 AA; 96894 MW; 669C8FD510E27EB8 CRC64;
MQSEEQLLEQ LNESQRAAVT YCDGPQLVIA GAGSGKTRVL TYKIAWLLAH YDMKPWNVLA
LTFTNKAARE MQSRIAQLVG GERARYLQMG TFHSVFSRIL RVEADSIGYR SDFTIYDESD
SRSLIKNIVK SMGLEDKTYK PASVHAAISA AKNRLCMPEQ YAEDGDLLAR DRHHNMPETF
KIYASYQQRL RQANAMDFDD LLVNTFQMLR DHEPLRQKYA ERFQYVFVDE YQDTNYVQQQ
IVTKLTRDHG RICVVGDDYQ SIYAFRGAKI DNILNFNRIY PDARMFKLEQ NYRSTQLIVA
AANSLMKHNS RQIPKEVYSR KEEGDKVTIL ETISDKREAA MVCREIRRIK NQEGCRWSDF
AILYRTNAQS RTFEEEMRKP EVGMGSHYRI YGGLSFYQRK EVKDVIAYFR LTVNPNDEEA
FRRIINYPAR GIGDTTVQKI VRAAEQHEVS LWETIARPAA YGLDVNRGTL GKLAAFHALM
SGFMAKAQTT DALTLGDEIM VESGIKADLA ADKTVEGDSR RQNIDALISG MADFVQAQRE
DDHADEARLQ DYLATVSLMT DQDSDDGSDD KVTLMTIHAA KGLEFPTVFV VGMEENIFPS
TLSVSTPREL EEERRLLYVA ITRAEKHCYL TWAHSRWLYG KMDSFVNPSR FINDIDPEFV
TVQTEGGRVG GNPFGEDRPR RRPWDEDKPA RRRPWDDDYE TDQPYTGARV WGGEYRRMSG
RMQNSRPVAG QFMADPKPKE TAPHRPEQAV NPFSSSFEAK LRQSGKWQSV SRAMTGGGRA
EPGSASPVSA GAGSAPSASA GTGAGLHAGQ VIEHQRFGRG TVVGVEGTGE NRKATVDFDT
TGRKQLLLKF AKFTIVG
//
