ID UVRD_RICCN Reviewed; 653 AA.
AC Q92HZ6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Probable DNA helicase II homolog;
DE EC=5.6.2.4;
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000305};
GN Name=uvrD; OrderedLocusNames=RC0624;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA duplexes
CC with 3' to 5' polarity with respect to the bound strand and initiates
CC unwinding most effectively when a single-stranded region is present.
CC Involved in the post-incision events of nucleotide excision repair and
CC methyl-directed mismatch repair (By similarity). {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AE006914; AAL03162.1; -; Genomic_DNA.
DR PIR; H97777; H97777.
DR RefSeq; WP_010977253.1; NC_003103.1.
DR AlphaFoldDB; Q92HZ6; -.
DR SMR; Q92HZ6; -.
DR GeneID; 928808; -.
DR KEGG; rco:RC0624; -.
DR PATRIC; fig|272944.4.peg.710; -.
DR HOGENOM; CLU_004585_5_10_5; -.
DR Proteomes; UP000000816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; 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; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
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; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Isomerase; Nucleotide-binding.
FT CHAIN 1..653
FT /note="Probable DNA helicase II homolog"
FT /id="PRO_0000286459"
FT DOMAIN 8..288
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 289..559
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 653 AA; 75051 MW; CF533C14DBA33A1C CRC64;
MQNQDFIHTL NPEQQKAVLH TEGPLLLLAG AGTGKTKVLT SRIANIIHQN LASPQNILAV
TFTNKAAKEM AERVNSLINC YGLNIGTFHS MAARILRDQI EHLNLGLNNR FTIISHDDQL
KLVKDIVKLK DIDTKKYAPK LIHIIISRWK DQGLLPTKLS VSDTNLPLQR VAKLVYEEYQ
KNLLISNVLD FGDLLLYNNE LFIKNSEILR YYQEKYRYIL IDEYQDTNVV QYLWARMLAS
LYKNICCVGD DDQSIYGWRG AEVGNILRFE KDFAGATIIK LEQNYRSTLP ILAAASNVIN
NNKNRHGKTL WTDRENGEKI KIISCWSDKE EARYIAGEID KLVRENRYNA GNIAILVRAG
FQTRSFEEAF INSAMPYKII GGLRFYERME IRDVLAYIRI SLNQNDNLAL ERIINVPKRA
IGAASLNKIR GYALERNISN FAAIKEMLEI GEIKAKSYET LKDLVTKIDN WYERFSIDAP
INVVKAILDD SGYLEMLQEE KTEEAFGRIE NINEMLRAIA EFNDVHDFIE HSSLVMENEV
LETNYGGSVT IMTLHAAKGL EFDVVFLPGW EEGVFPSQRS LDEEGEKGLE EERRIAYVGI
TRAKKDLYIT HAESRKIFYE IVRSYPSRFI TEIPDEITIR TSSMKKYNSF YKF
//
