ID Q6YPU8_ONYPE Unreviewed; 604 AA. AC Q6YPU8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-OCT-2013, entry version 78. DE RecName: Full=DNA primase; DE EC=2.7.7.-; GN Name=dnaG; OrderedLocusNames=PAM_627; OS Onion yellows phytoplasma (strain OY-M). OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Candidatus Phytoplasma; OC Candidatus Phytoplasma asteris. OX NCBI_TaxID=262768; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OY-M; RX PubMed=14661021; DOI=10.1038/ng1277; RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S., RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.; RT "Reductive evolution suggested from the complete genome sequence of a RT plant-pathogenic phytoplasma."; RL Nat. Genet. 36:27-29(2004). CC -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA CC primers for the Okazaki fragments on both template strands at CC replication forks during chromosomal DNA synthesis (By CC similarity). CC -!- COFACTOR: Binds 1 zinc ion per monomer (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the DNA primase family. CC -!- SIMILARITY: Contains Toprim domain. 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; AP006628; BAD04712.1; -; Genomic_DNA. DR RefSeq; NP_950879.1; NC_005303.2. DR ProteinModelPortal; Q6YPU8; -. DR EnsemblBacteria; BAD04712; BAD04712; PAM_627. DR GeneID; 2673232; -. DR KEGG; poy:PAM_627; -. DR HOGENOM; HOG000053082; -. DR KO; K02316; -. DR OMA; DEYIKTE; -. DR ProtClustDB; CLSK343817; -. DR BioCyc; MORG262768:GHF5-655-MONOMER; -. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003896; F:DNA primase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.90.580.10; -; 1. DR Gene3D; 3.90.980.10; -; 1. DR InterPro; IPR013264; DNA_primase_core_N. DR InterPro; IPR006295; DNA_primase_DnaG. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR002694; Znf_CHC2. DR Pfam; PF13662; Toprim_4; 1. DR Pfam; PF08275; Toprim_N; 1. DR Pfam; PF01807; zf-CHC2; 1. DR PIRSF; PIRSF002811; DnaG; 1. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR01391; dnaG; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed RNA polymerase; KW Metal-binding; Nucleotidyltransferase; Primosome; Transcription; KW Transferase; Zinc; Zinc-finger. FT ZN_FING 38 62 CHC2-type (By similarity). SQ SEQUENCE 604 AA; 70660 MW; 77D4DA70E62CDFAD CRC64; MQDNKQLIDQ INEKMPILDL VQEFVQLKKS GKNYMGLCPF HDEKTPSFSV SPERNIGVCM SCKKGGNPVF FYKSIKNIPL NQAIFELATR LGIATSLPQQ GTHQYQKFYN IMQEAADFYS HQLKHNKQVL NYLEKRGFDN DIIKHFKLGY APKASHLSRY LMEGTKFDPD DLKKLSLINQ DDKTGNFYDF FKNRLIFPIT NKSGQIVAFS SRSLDDQMPK YLNSPETIIF KKGETLYQYY ETQAEIRKKQ KVILHEGFFD VMASFKAQFK NVVATMGTNL TLDHAKLLKK ITDKIIIAYD GDKAGKTATL EIGTFLQKNH FKVQIVDFPN NLDPDEYIKT EGPEKYQHLL TDNLKDFLAL KVDLICQQMD SYNKAQTKKE LQELFQSSSF EIKMLYQEYL QKTYQLTVNL NSQVSINKAP KPPYIAHTKQ QLNLTKFDIK IEIIIELLLN ADFFKTQNPK TFATIKKTPG FDDLQCSCLL NYIKNYYKKN PKQTCIPWEE IKNTTFKENI DDLLTSIEKH HFFKMEKRPL LQDKEGKIFN NYIKELEIRD KIEQKQQKIN ELNDKLLPID NTEKNKLQKK KDKLKKERRQ LQKQLSELVN DIFC //