ID G0HHI0_CORVD Unreviewed; 931 AA.
AC G0HHI0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=pcrA1 {ECO:0000313|EMBL:AEK37460.1};
GN OrderedLocusNames=CVAR_2110 {ECO:0000313|EMBL:AEK37460.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK37460.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK37460.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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; CP002917; AEK37460.1; -; Genomic_DNA.
DR AlphaFoldDB; G0HHI0; -.
DR STRING; 858619.CVAR_2110; -.
DR KEGG; cva:CVAR_2110; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_3_1_11; -.
DR Proteomes; UP000006659; 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; 2.
DR Gene3D; 1.10.10.160; -; 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; 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; 2.
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}.
FT DOMAIN 114..399
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 400..732
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 931 AA; 100194 MW; 56928211B9A75797 CRC64;
MNQGMSDNPF DGQIPFPEDA FPDESGQDAG WDAPPEEDLP PDDAGDLLNG FAADFAVSVA
HLAPLPELPP EPHSPDMTSG SAGATSAPQR ATAPASLRTG GGNGLAAREE ELLAGLNPAQ
RAAVVHHGSP LLIVAGAGSG KTSVLTRRVA WLLAHGVAPW QILAITFTNK AAAEMRERVT
DLVGPVAERM WLSTFHSLCV RILRANAQLI EGLNTNFTIY DSDDQKRLIT MVLKDHDCDL
KEFAPRAVLS VISNWKNELQ GPAEALKETQ EDGNRHREQI ALVYRDYQAR LRESNAVDFD
DLIGEVVWML QANPAVADHY RRRFRHVLVD EYQDTNHAQY VLVSTLVGEG PDAGELCVVG
DADQSIYAFR GATIRNIEEF ERDYPHAETI LLEQNYRSTQ NILSAANAVI ARNQGRREKK
LWTDSGDGPL IGGYVADNEH DEARFIAQTI DQLVDDGDAT YGDIAVMYRT NNSSRVVEDV
LVRSGLPYKV VGGTRFYERR EIRDVVAYLK VLDNAEDTMG LRRIINTPRR GIGDRAISQV
SVHAENMDLS FAGGLRAAAA GEVPGLSSRG RNAIAGFLEL MDGLREDLPG HVMEASDGSS
LEIPDLGAVI RDVLDRTGYT TELEKSNDPQ DGSRLDNLHE LVSVGHEFSQ EAANLAAYEA
MPDTAGGTAA QQESGAASDA DAAADAVLSE GEPAPGSLQA FLERVSLVAD ADQIPGEEQE
LITLMTLHTA KGLEFPVVFL TGWEDGQFPH QRALGDPTEL SEERRLAYVG ITRARQRLYL
SRAVTRSSWG TPANNPPSRF LDEIPGELID WIREEPTPSW GGGWGSSTSG GYADGTSFGG
GGFGGGYGGG SGYGSRQSSS PAPRRKAPSS PLSGGKPLEL AVGDRVNHDK YGLGTVKTVD
GSGVRATATI DFGASGTVRL MLIGGVPMEK L
//
