(data stored in SCRATCH zone)

SWISSPROT: Q13DP7_RHOPS

ID   Q13DP7_RHOPS            Unreviewed;       735 AA.
AC   Q13DP7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
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=RPD_0554 {ECO:0000313|EMBL:ABE37792.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37792.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37792.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37792.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37792.1; -; Genomic_DNA.
DR   RefSeq; WP_011500979.1; NC_007958.1.
DR   STRING; 316057.RPD_0554; -.
DR   EnsemblBacteria; ABE37792; ABE37792; RPD_0554.
DR   KEGG; rpd:RPD_0554; -.
DR   eggNOG; ENOG4105C25; Bacteria.
DR   eggNOG; COG1198; LUCA.
DR   HOGENOM; HOG000037413; -.
DR   KO; K04066; -.
DR   OMA; FQNRRGY; -.
DR   OrthoDB; 1132322at2; -.
DR   BioCyc; RPAL316057:RPD_RS02840-MONOMER; -.
DR   Proteomes; UP000001818; 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; 1.
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; Q13DP7.
DR   SWISS-2DPAGE; Q13DP7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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   ECO:0000313|EMBL:ABE37792.1};
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      216    382       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      480    638       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   ZN_FING     443    455       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00983}.
FT   ZN_FING     470    486       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00983}.
SQ   SEQUENCE   735 AA;  81136 MW;  07D4BD37B780F3BC CRC64;
     MDDSRTSPTS NASTRVVDVQ VPVAVDQAYS YRVPRGLDLK PGDVVAVPLG PREVLGVVWA
     ENPNPDPRLH NRLKDVAEKL DVPPLREELR RLVDWVANYT LSPRGQVLRM TLRMGELGPE
     RQRMGVRLVG PPPQRMTPAR RRLIEILSDG LLHGKSDVAK EAGVSPGVID GLVDEGTLHV
     EAMPREPAAP TPDPDFAPAD FSPEQARAAE TMRELVKPGG GFQAALLDGV TGSGKTEVYF
     EAVAEVVRQG RQCLILMPEI ALTGQFLDRF ALRFGVRPLE WHSELTPRTR ARNWAAIAAG
     EAQVVVGARS ALFLPYADLG LIIVDEEHDQ AYKQEDGAHY HARDMAVVRA SIARIPIVLA
     SATPSVETEV NARKGRYRRI PLPSRFGGQH MPQIEAIDLR REPPMRGRFI SPRLAEQVGH
     AIERREQALL FLNRRGYAPL TLCRACGHRF ACTICDAWLV DHRFRQRLVC HHCGFSMPRP
     LQCPHCAAEQ SLVAVGPGVE RLQEEASSLF PDARTMVLSS DLITSIEAMR SELNDIAEGR
     VDIIIGTQLV AKGHNFPRLN LVGVVDADLG LSNGDPRAAE RTFQLLNQVI GRAGRDQGRG
     VGFLQTHQPE HPVMKALVAC DREAFYASEI EARERTLYPP FGRLASLIIS AGDRPTAEGF
     ARQLASSAPV DERVQVLGPA EAPLAVIKGR YRFRLLVKSV RSFDLSNYLR QWLAQGPKTK
     GNLKLEVDVD PQSFL
//

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