ID A2C0D7_PROM1 Unreviewed; 805 AA.
AC A2C0D7;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 96.
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:ABM74947.1};
GN OrderedLocusNames=NATL1_03831 {ECO:0000313|EMBL:ABM74947.1};
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167555 {ECO:0000313|EMBL:ABM74947.1, ECO:0000313|Proteomes:UP000002592};
RN [1] {ECO:0000313|Proteomes:UP000002592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A {ECO:0000313|Proteomes:UP000002592};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM74947.1; -; Genomic_DNA.
DR RefSeq; WP_011823145.1; NC_008819.1.
DR AlphaFoldDB; A2C0D7; -.
DR KEGG; pme:NATL1_03831; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_3; -.
DR OMA; YQDTNRT; -.
DR Proteomes; UP000002592; 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:UniProtKB-KW.
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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:ABM74947.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 10..344
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 345..621
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 727..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 562..589
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 805 AA; 91221 MW; 1326A64F43C56F29 CRC64;
MKQSNSIFLN GLNEAQSHAV DHFHGPLLVV AGAGSGKTRA LTHRIAHLIT EYKVDPSSIL
AVTFTNKAAR EMKDRLELLL AKRLSSLTHG KPWTALQVAE QREIRNRIHR EISRELWIGT
FHALFSRLLR FDIDKFKDPE GLTWTKQFSI YDETDAQSLI KEIVTQDLQL DPKRFEPKKV
RWAISNAKNQ CLLPDDLSNN QEGQRGKLVA ETYRLYRKAL AANNALDFDD LLLIPVQLLQ
QNEKIRTYWH SRFKHVLVDE YQDTNWTQYE LIKQLVTNGK DPSSFQDWNN RSVFVVGDAD
QSIYSFRAAD FRILMGFQED FGKKSLDNTY DSTLVKLEEN YRSTSTILEA ANSLISNNKE
RIDKVLRATR GEGEPIRLTR CDDEIAEAEA VIHRLRILDA SNPELNWGDM AILYRTNAQS
RAIEDSLVRW SIPYIVVGGL RFYDRREIKD LLAYLRLLIN PSDSVSLLRV LNVPKRGIGK
TTVQRLSDAA SQLKIPLWEV VNDPEAVRSL AGRSAKGLLI FSELINELQS HLLSSSPAEL
VQLVLEKSGY LSELIATGTD EAEERRRNLQ ELVNAALQYQ EESEDANLEG FLSTAALSSD
ADNKDTASNR VTLMTLHSSK GLEFPVVCLV GMEQGLFPSY RSLDDPSSLE EERRLCYVGL
TRAKEKLFLF HASERRMWGG MREPAIASIF LSEIPEELVK GDIPLSGGAT LRREKNLDRL
TRIDRQSNKK SFPREAENAV RKTYSGPSPG KRWSVNDRVE HSSFGEGIIT HVFGSGEKIS
LAIKFSGMGP KILDPRLAPL KLIDE
//