ID F0F7S0_9BACT Unreviewed; 843 AA.
AC F0F7S0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=pcrA {ECO:0000313|EMBL:EGC19763.1};
GN ORFNames=HMPREF9141_1637 {ECO:0000313|EMBL:EGC19763.1};
OS Prevotella multiformis DSM 16608.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=888743 {ECO:0000313|EMBL:EGC19763.1, ECO:0000313|Proteomes:UP000005697};
RN [1] {ECO:0000313|EMBL:EGC19763.1, ECO:0000313|Proteomes:UP000005697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16608 {ECO:0000313|EMBL:EGC19763.1,
RC ECO:0000313|Proteomes:UP000005697};
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 (JAN-2011) 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 -!- 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:EGC19763.1}.
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DR EMBL; AEWX01000024; EGC19763.1; -; Genomic_DNA.
DR RefSeq; WP_007366391.1; NZ_GL872282.1.
DR AlphaFoldDB; F0F7S0; -.
DR STRING; 888743.HMPREF9141_1637; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_8_10; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000005697; 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 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:UP000005697}.
FT DOMAIN 12..297
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 298..580
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 674..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 843 AA; 95953 MW; 1683237B7D78210E CRC64;
MDHQEREEEL LSALNESQRK AVEYCAGPSL VIAGAGSGKT RVLTYKIAYL LEKGLKPWNI
LALTFTNKAA KEMKERIAQI TTAGEARRLY MGTFHSIFAR ILRSEGELIG FGHNFTIYDE
TDSRSLIKSI VKALGLDEKT YKPAAVHNFI SMAKNRLITA SEYAEDRAAL NRDRIVRMPA
VYQIYKAYEA RCRQANAMDF DDILLYTYLL FRDHVDVRKK YGQLFEYILV DEYQDTNFAQ
VSIISQLANT HRRVCVVGDD YQSIYSFRGA NIDNILDFRE KFTDARLFKL ERNYRSTQLI
VQAANSLMKH NERQIPKEVY SEEGEGHKVL YKPCYSDREE AMVVAGELRR IKRDERCDYG
SFAILYRTNA QSRPFEDEFR KQGIPYKIIG GLSFYQRKEI KDIIAYFRLV ANPDDEEAFR
RIINYPARGI GSTTVQKIVD CAQHHAVSLW ETILNPIGYG LNVNKGTLTK LLAFKTLISG
FIKKAALTDA YELGSEIIEE SGIGADIRSG RDPEDLARRE NLEEFMSAMQ DFVDIGREEG
REENVYLTDY LQEVALYTDA DKKDDDTPKV TLMTIHAAKG LEFPTVFVVG LEENVFPSPM
ASGSRREVEE ERRLLYVAIT RAERHCILTN ARNRFRYGTM QVDDPSRFLD DIDASLLQEE
NNGSDVFRTQ RQKMPWDDDP CKRSGGSTRE YEPNRPYTGS RPWGQEYRQM GARWQNANPV
ASQFRADPKP KITERKRPEA AVDPLSERTK RRILCEGGNF KRLSSAMTNG GRTLPASSSS
AADSASASTS GLRVGMTIEH QRFGIGKVLG LEGTGENAKA TVEFRNAGRK QLLLKFARFK
VIG
//
