(data stored in SCRATCH3701 zone)

SWISSPROT: PRIA_RICTY

ID   PRIA_RICTY              Reviewed;         648 AA.
AC   Q68WJ4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 94.
DE   RecName: Full=Primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983};
DE   AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983};
GN   Name=priA {ECO:0000255|HAMAP-Rule:MF_00983}; OrderedLocusNames=RT0529;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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:0000255|HAMAP-
CC       Rule:MF_00983}.
CC   -!- SUBUNIT: Component of the primosome. {ECO:0000255|HAMAP-Rule:MF_00983}.
CC   -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00983}.
DR   EMBL; AE017197; AAU03998.1; -; Genomic_DNA.
DR   RefSeq; WP_011190979.1; NC_006142.1.
DR   SMR; Q68WJ4; -.
DR   STRING; 257363.RT0529; -.
DR   PRIDE; Q68WJ4; -.
DR   EnsemblBacteria; AAU03998; AAU03998; RT0529.
DR   KEGG; rty:RT0529; -.
DR   eggNOG; ENOG4105C25; Bacteria.
DR   eggNOG; COG1198; LUCA.
DR   HOGENOM; HOG000037414; -.
DR   KO; K04066; -.
DR   OMA; RCHYCGY; -.
DR   OrthoDB; 1132322at2; -.
DR   BioCyc; RTYP257363:G1G0L-535-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; 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; PF00271; Helicase_C; 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; Q68WJ4.
DR   SWISS-2DPAGE; Q68WJ4.
KW   ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Primosome; Zinc; Zinc-finger.
FT   CHAIN           1..648
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102133"
FT   DOMAIN          131..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   DOMAIN          393..548
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   NP_BIND         144..151
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         358..370
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         385..401
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   MOTIF           240..243
FT                   /note="DEAH box"
SQ   SEQUENCE   648 AA;  73424 MW;  FBBE56456EF8B337 CRC64;
     MRIAKILLPV SKLFPLDYLI TEDLELNIGD LVVVHFRNQE LTGIVWELAT NSEAKKIKTI
     KAKVPLNLNI SLEVLALIKW MSSYYMSELG SIAKLVLPIN IAEKPIKIKE QQVKNYFVLP
     QLSEEQKQAV TIFNESNKPT LIKGVTGSGK TEIYFHIIAD HLMKGQQVLI MLPEIALSRQ
     IINRFIDRFG FEPIIWNSSV TKAQKKMILR GILSDKVKVV IGARSSLFLP FHNLGLIVID
     EEHDDSYKQD DNILYNARDT AIVRGVFDKA KIVLCSATPS LETIYNIKTH KYQLVTLVNR
     YKNIDLPNIE IIDMTKEKLP KNSYLSKILI DAIKGNLENK KQVLLFLNRR GYAPLMLCKA
     CGHRFTCRFC SAWMVLHKAT KTLECHHCGY QSKIFSSCPE CLEDETLTIC GPGIERIEEE
     AMLLFPKSKI AVISKDHAKT PAKIAQLLHQ MENLEIDILI GTQIITKGYH FPNLTLVGVI
     DADLGSNNAE LRASERTFQL LHQVGGRAGR GDSKGVVYLQ SYYPDNIIFS YVKVGDEDSF
     FTNELEIRKA ANMPPFSKTA SLILSGFSES KILDIAKNIV QIAPKANVKI LGPARALMSK
     LAGKYRYRIL IIADKKFNLQ QYLKFWLSLI KIPSYCQIKI DIDPKTFY
//

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