(data stored in SCRATCH zone)

SWISSPROT: Q3KJB2_PSEPF

ID   Q3KJB2_PSEPF            Unreviewed;       744 AA.
AC   Q3KJB2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983};
DE   AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
GN   Name=priA {ECO:0000256|HAMAP-Rule:MF_00983};
GN   OrderedLocusNames=Pfl01_0400 {ECO:0000313|EMBL:ABA72144.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72144.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72144.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72144.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Involved in the restart of stalled replication forks.
CC       Recognizes and binds the arrested nascent DNA chain at stalled
CC       replication forks. It can open the DNA duplex, via its helicase
CC       activity, and promote assembly of the primosome and loading of the
CC       major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00983}.
CC   -!- SUBUNIT: Component of the primosome. {ECO:0000256|HAMAP-
CC       Rule:MF_00983}.
CC   -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00983}.
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DR   EMBL; CP000094; ABA72144.1; -; Genomic_DNA.
DR   STRING; 205922.Pfl01_0400; -.
DR   EnsemblBacteria; ABA72144; ABA72144; Pfl01_0400.
DR   KEGG; pfo:Pfl01_0400; -.
DR   eggNOG; ENOG4105C25; Bacteria.
DR   eggNOG; COG1198; LUCA.
DR   HOGENOM; HOG000037413; -.
DR   KO; K04066; -.
DR   OMA; FQNRRGY; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.630; -; 1.
DR   HAMAP; MF_00983; PriA; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005259; PriA.
DR   InterPro; IPR041222; PriA_3primeBD.
DR   InterPro; IPR042115; PriA_3primeBD_sf.
DR   InterPro; IPR041236; PriA_C.
DR   InterPro; IPR040498; PriA_CRR.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF17764; PriA_3primeBD; 1.
DR   Pfam; PF18074; PriA_C; 1.
DR   Pfam; PF18319; PriA_CRR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00595; priA; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJB2.
DR   SWISS-2DPAGE; Q3KJB2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN      220    386       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      462    637       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   ZN_FING     445    457       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00983}.
FT   ZN_FING     472    488       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00983}.
SQ   SEQUENCE   744 AA;  82699 MW;  12BCC5B09ED8F787 CRC64;
     MRIPRVPDAI LRLALPSPLR RLFDYRAPAG VLRSQLQPGM RLRVPFGRRE MIGILVEVTD
     TSEVPVEKLK PALALLDVTA PLPPALFKLC LWTSQYYQHS LGDTLSWALP VLLRQGELAE
     VRQERFWSAA PGASLDDPRI ARAPRQREAL ATLAQHPHGV AHQLLSKLML SKDSLDLLLA
     KDLVQVEVRR HAPGARHEHW LAQPELPLNS EQRAAYEAIR AGFDSYHAFL LAGVTGSGKT
     EVYLQLIRET LEAGKQALVL IPEINLGPQT LARFEQRFNA RIALLHSAVN DRDRLDAWLA
     ARDGEADIII GTRSALFTPM KNPGLIIIDE EHDGSYKQQE GLRYHARDLA LVRARQENIP
     IVLGSATPSL ESLHNAYTGR YGLLRLNERA GGAKQPRFLR LDVKSRPLDS GISGPMQQAI
     GQTLAAGQQV LVFLNRRGFA PTLLCHDCGW MSECQRCDAR MTVHQRYGEL RCHHCGYVER
     VPRQCPKCNK VDLRPVGAGT ERAEERLAIL FPDYPVLRVD RDSTSRKDAM NQLFATIQKG
     QPCILVGTQM LAKGHHFPRV TLVSILDADG GLFSGDFRAS ERMAQLIVQV AGRAGRAEEP
     GKVIIQTHLA DHPLLVQLTE QGYFAFAEQA LSERRAAGLP PFAHLALLRA EAHKPGQAEG
     FLDEACSEAE RLLAEQNLSG IELLGPVPAP MERRAGRFRA QLLLQATARA PLHRLLASWL
     LVLEQMPSGR AVRWSLDVDP VDLY
//

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