ID B2ULA1_AKKM8 Unreviewed; 738 AA. AC B2ULA1; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 03-AUG-2022, 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=Amuc_0043 {ECO:0000313|EMBL:ACD03890.1}; OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC OS 81048 / CCUG 64013 / CIP 107961 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD03890.1, ECO:0000313|Proteomes:UP000001031}; RN [1] {ECO:0000313|Proteomes:UP000001031} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031}; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001071; ACD03890.1; -; Genomic_DNA. DR RefSeq; WP_012419105.1; NC_010655.1. DR STRING; 349741.Amuc_0043; -. DR EnsemblBacteria; ACD03890; ACD03890; Amuc_0043. DR KEGG; amu:Amuc_0043; -. DR eggNOG; COG1198; Bacteria. DR HOGENOM; CLU_013353_3_1_0; -. DR OMA; RCHYCGY; -. DR OrthoDB; 1132322at2; -. DR BioCyc; AMUC349741:G1GBX-50-MON; -. DR Proteomes; UP000001031; 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: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 Gene3D; 3.40.1440.60; -; 1. DR Gene3D; 3.40.50.300; -; 2. 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; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00983}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW 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:UP000001031}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}. FT DOMAIN 214..383 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 459..635 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT ZN_FING 446..458 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983" FT ZN_FING 473..489 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983" SQ SEQUENCE 738 AA; 81646 MW; AA466ADC5D8B8908 CRC64; MQAARILVDG QSDLVLDYGI PPEAGDVKPG CRVQVPLRNR TATGTVLTLS EPAPAWKDRL KPILKLIDPE PLISPVMMNL ASWAADYYSV ALDQMIRCLL PETVRQENTA EKMRKMVYLE KTPAREELDA LYRKAPRQAQ MLDYFSSAKQ QSAPLAAFGA GALNVARSLE AKGFISLKEE AVHRDPSTGE QFVPTQPMKL NSQQQKALEE ITAMCAAERK KPVLLQGVTG SGKTEVYLQA VSQIVKSGKS ALIMVPEISL TPQTVQRFKS RFAELPSSVA VLHSLLSDGE RFDEWHAIRS GKARIVIGPR SAVFAPLQNL GLVIVDEEHD ASYKQESSPR YHGRDLAVLR AHLENCAVLL GSATPSLESI HNALIGKYSL VKLTERADGQ QLPLIRILDM KTEGRNKSGP NVISERLRMS IDRRLDKGEQ VILLLNRRGF ARSIQCPDCG HVVTCLHCSL PLTYHRTEDR LMCHLCGFKA LPPRSCPECR SANILLQGYG TQKVEELLRR TFPAARITRV DADVARRKNA VRTILNQFRA HKIDILLGTQ MIAKGLDFPN VTLVGVLNAD LGLHIPDPRA GERTFQLLTQ VAGRAGRGDL SGEVIIQTFT PQSPSLQYAR HHDTDGFAAQ ELEMRRTFDL PPFTHIAVLT IRSQHESMAE FATQTLAARL RGMLPPPATM TDPMPAPIPR AHGQFRFQIT VKGPSARILS RTLRKLVQEA GLGEDLTAVI DVDAMSFM //