ID A5WCY7_PSYWF Unreviewed; 774 AA.
AC A5WCY7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=PsycPRwf_0573 {ECO:0000313|EMBL:ABQ93528.1};
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93528.1};
RN [1] {ECO:0000313|EMBL:ABQ93528.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93528.1};
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., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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-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; CP000713; ABQ93528.1; -; Genomic_DNA.
DR AlphaFoldDB; A5WCY7; -.
DR STRING; 349106.PsycPRwf_0573; -.
DR KEGG; prw:PsycPRwf_0573; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_6; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 CDD; cd17929; DEXHc_priA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.1440.60; PriA, 3(prime) DNA-binding domain; 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 NCBIfam; TIGR00595; priA; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00983}; DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00983};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, 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 223..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 470..482
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 503..519
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 774 AA; 86415 MW; 31AE4F14B15E0EF2 CRC64;
MLIRVALPVP LYREFDYLPP IPASSNPAHC AKTAPPMPPI GSRVQVSFGR QTLIGIVVAH
IDRQSSDIPL NKLKPIKQCL DETPILDAAM LSLARWLASY YHYPLGDVIS VMLPTLIRQG
KPLDLLVTHW RIRPNVSDAN FNSNAHKQKQ QFAMLKLHGT HGASEETLLL EGMERPFLKR
LEENGLIEHY LQPQADPAPV SLAKMPLDLN EQQKLAVNAI IHTANTNTYC GYLLNGVTGS
GKTEVYLQAM QSVLEAGKQV LVLVPEIGLT PQTRARFAER FSANILLLHS NLNNTQRMHG
WEDCRQGRAQ IVIGTRSSVL HPFANLGLIV VDESHDQSYK QQDTLRYHAA DVALYRGYQL
GIPVVLGTAT PSLEHLKLVQ EGKLTELMLT ERAGHAKAAS LHLVDARDTP TKYSDMPVED
KQRQLLPNLE RSQNTGLTDD TIAAIRSTLE AGEQVLVFLN RRGYAPILLC DACGWQADCV
RCEAHMTLHH SQLNSQQPSY LKCHHCDWQA SIPLACPECH SPNLNAVGMG TTRLTESLHA
LFSNPQTSKI TYPIIQIDRD TTRRKDSWEE IYQRINTGKP AILVGTQMVA KGHHFPNVTL
VCLPNADRGF LSPDFRSPEH TAQLIVQVAG RSGRGSKPGK VLIQTVQPEN PLLRKLVRDG
YQPFALELLK ERKMIGLPPY TYAALIRCEA KTLQRATQVL KDAVVILPPH NLSILGPVDA
PMKLKNSRYH TQLLLLSKQR APLHQVLNLW WPQVLQLPSA KYLKLTLDID PIGW
//
