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PRIA_CHLTR
ID   PRIA_CHLTR              Reviewed;         753 AA.
AC   O84783;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=CT_778;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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}.
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DR   EMBL; AE001273; AAC68373.1; -; Genomic_DNA.
DR   PIR; B71472; B71472.
DR   RefSeq; NP_220297.1; NC_000117.1.
DR   RefSeq; WP_010725341.1; NC_000117.1.
DR   AlphaFoldDB; O84783; -.
DR   SMR; O84783; -.
DR   STRING; 813.O172_04335; -.
DR   PRIDE; O84783; -.
DR   EnsemblBacteria; AAC68373; AAC68373; CT_778.
DR   GeneID; 884574; -.
DR   KEGG; ctr:CT_778; -.
DR   PATRIC; fig|272561.5.peg.854; -.
DR   HOGENOM; CLU_013353_3_1_0; -.
DR   InParanoid; O84783; -.
DR   OMA; RCHYCGY; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   Gene3D; 3.40.1440.60; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00983; PriA; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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; PF17764; PriA_3primeBD; 1.
DR   Pfam; PF18074; PriA_C; 1.
DR   Pfam; PF18319; PriA_CRR; 1.
DR   Pfam; PF04851; ResIII; 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;
KW   ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Primosome; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..753
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102122"
FT   DOMAIN          228..395
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   DOMAIN          491..646
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         458..470
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         485..502
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   MOTIF           337..340
FT                   /note="DEAH box"
FT   BINDING         241..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   753 AA;  84832 MW;  C91861B4385C5E35 CRC64;
     MDPTHQPFRL YAEVIVNANI NKILDYGIPA ELENLVTVGS VVKVPLQRKL TNDKYKIAIV
     LKIKSSSDFV HVIQPILDIS YEGITLPQDL IDLIFWISQY YFCPLGSAVS LFLPTVYAQT
     HSTKHQNNVF LGQNAERTQE ILKTLDNPQQ IAVLRKLLKT TKPLTPPELM RKTEVSAKTL
     DALVKQKFIR IVDSADLEIQ DEQLHYFLPD PPTLNQEQLD AVNTISQSLV AEQFQTCLLF
     GVTGSGKTEV YLQVIRKARA LGKSVILLVP EVALTIQTLS FFKMHFGSEV GVLHYKLSDS
     ERTQTWYKAS RGLINIIIGP RSAIFCPIQN LGLIIVDEEH DSAYKQSDLP PFYQARDVAV
     MRGKMTNATV ILGSATPSLE SYTNALSKKY TLSVLSKRAS TSTPTKVFLI DMNLEMEKTR
     KKPFFSQTVI RSIEQRLEVG EQTIIFFNRR GFHTNVSCSS CKYTLKCPHC DMILTFHKTE
     RILLCHLCNT RLSKPITSCP QCLGTMTLQY RGAGTEKIET LLREFFPTAR TIRLDSDTTR
     FRGSHDALVK QFATGKADIL IGTQMIAKGM HFPAVTLSVV LSGDSGLYIP DFRAAEQVFQ
     LITQVTGRSG RSHLPGEVLI QTFLPQNSTI SHALAQDFPA FYKEEILGRK VCNYPPFTRL
     IRCIFLGKCS DYTLKETQRV HTLIKQNLDS QASLMEISPC GHFKVKDLFH YQFLIKTRNI
     LVANKQIQEA LAAAKLSSKV RCIVDVDPVT TFF
 
 
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