ID A0A1I0XL70_9BACT Unreviewed; 839 AA.
AC A0A1I0XL70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=SAMN04489723_103250 {ECO:0000313|EMBL:SFB01634.1};
OS Algoriphagus aquimarinus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB01634.1, ECO:0000313|Proteomes:UP000198790};
RN [1] {ECO:0000313|EMBL:SFB01634.1, ECO:0000313|Proteomes:UP000198790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB01634.1,
RC ECO:0000313|Proteomes:UP000198790};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOKK01000003; SFB01634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XL70; -.
DR STRING; 237018.SAMN04489723_103250; -.
DR Proteomes; UP000198790; Unassembled WGS sequence.
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 CDD; cd18804; SF2_C_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 InterPro; IPR040498; PriA_CRR.
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 Pfam; PF18319; PriA_CRR; 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.
DR PROSITE; PS51194; HELICASE_CTER; 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 Reference proteome {ECO:0000313|Proteomes:UP000198790};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 314..481
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 518..734
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 544..556
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 571..587
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 839 AA; 95372 MW; 61F57973E42D17A4 CRC64;
MENLFGDQDL YPPESGNNFA DIILPVPIPR MFTYSIPHTM QPEINLGARV IVPFGKKKVL
TGIIGKVHNK PPQAYQAKPI LEVLDDTPSV NPLQIRFWVW MAEYYFCHIG EVMHAALPSG
LRLSSESKVQ LNPNYDRETS KFPLDDREIM ILDALDSKPE LSYEDCEKVL SIKSIHPILK
SLVKKEAILI FERLQEKYTP KVETRVRLTP PIAESKSALQ EVFEALAGKA KQESILLKYL
RDVPFLQKPK SNEKGLDKAT LLEEGDSESS LKTLIKNGIF ESFKVVVNRL AEEEAESEPA
VLSTSQQSAF EEIKHQFESK QSVLLHGVTG SGKTEIYIQM IMEVLESGSQ VLLLLPEIAL
TTQIVTRLKK VFGSKMGVYH SKYSDNERVE VWNGVLSGRF SFVVGVRSSI FLPFDSLGLI
IVDEEHESSY KQFDPAPRFQ ARDSAIMLAY FHQARTLLGS ATPSFESYFN ATQGKFGYVE
LTNRFGNASM PQFHLADLAA DKRKNLLKLD TTRILRERIQ EALAKQEQVL IFQNRRGYSP
YIQCEDCGWT GQCVQCDVSL TYHQFSEELR CHYCGYKEKT PSACPACGST HLTTMGMGTE
RIEESLSLLF PEARIGRMDL DTTRNKHGYQ RLLDEFGSGN LDILVGTQMI TKGLDFGRVT
VVGIWDGDRI LNFPDFRAGE RAFQQITQVA GRAGRREVQG QVIVQTRDPE TQIYAQVIKG
DYFEFFNHEI HDRKKFYYPP FVKLVKITTR HTDFKVAEKA ALNLHHGMAE IPIKKIVLGP
EKGIIARIKN QYQFESLIKL DRSGNTPVIF KEHLWKITEE LKSRPEFRSV RFVVDVDPS
//
