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Database: UniProt
Entry: A0A0H3JA93_CLOPA
LinkDB: A0A0H3JA93_CLOPA
Original site: A0A0H3JA93_CLOPA 
ID   A0A0H3JA93_CLOPA        Unreviewed;       590 AA.
AC   A0A0H3JA93;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   10-APR-2019, entry version 27.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:AJA52348.1};
GN   ORFNames=CLPA_c22900 {ECO:0000313|EMBL:AJA52348.1};
OS   Clostridium pasteurianum DSM 525 = ATCC 6013.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA52348.1, ECO:0000313|Proteomes:UP000030905};
RN   [1] {ECO:0000313|EMBL:AJA52348.1, ECO:0000313|Proteomes:UP000030905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 525 / ATCC 6013 {ECO:0000313|Proteomes:UP000030905};
RX   PubMed=25700415;
RA   Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT   "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT   Clostridium pasteurianum DSM 525.";
RL   Genome Announc. 3:e01591-14(2015).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC       domain that contains the primase activity, and a C-terminal DnaB-
CC       binding domain. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CP009268; AJA52348.1; -; Genomic_DNA.
DR   RefSeq; WP_003441584.1; NZ_JPGY02000001.1.
DR   STRING; 1262449.CP6013_2218; -.
DR   EnsemblBacteria; AJA52348; AJA52348; CLPA_c22900.
DR   EnsemblBacteria; KRU11642; KRU11642; CP6013_00889.
DR   KEGG; cpae:CPAST_c22900; -.
DR   KEGG; cpat:CLPA_c22900; -.
DR   PATRIC; fig|1262449.3.peg.700; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; GCF_001856645:G1FB7-2257-MONOMER; -.
DR   Proteomes; UP000030905; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   Gene3D; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR013264; DNA_primase_core_N.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR019475; DNA_primase_DnaB-bd.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR030846; DnaG_bac.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030905};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339,
KW   ECO:0000313|EMBL:AJA52348.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030905};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442,
KW   ECO:0000313|EMBL:AJA52348.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   590 AA;  68009 MW;  874145657CBEF202 CRC64;
     MIPEDVIEKI KYENDIVDVI SDTVKLKKSG RNYMGLCPFH NEKSPSFSVS EDKQIYKCFG
     CGEAGNVITF VMKTKSLSFI DAVKLLAERI HLDLDYLEKG NNKKKDTNDK LLKLNVDAAR
     FFFSNLNSNK KAKNYFINRG ILESTIRSFG LGYALDDWHG IMNFLKRKGY SDLDLLNAGL
     IIKNEKGNKY DRFRNRVMFP VFDYKGKVIG FGGRVLDDSK PKYLNSPETA LFKKGINLYG
     LNFVLKNDNK RTIIIVEGYM DCITLHQYGI NNTVASLGTA LTVNQAKLLK RYADNIIISY
     DADTAGQKAT LRGLKILRDV GLNVKVLIVP KGKDPDEFIR NNGKEAFEEL IKNSMNLIDY
     RIKKAGENVN FRNNREIPAY IKKIADILID LDPIEKDVYI KRVSEETGIK EQAIYDLLSE
     ERHKSTNYLQ NMNNIGDYGQ KLYLEPAYIK AERLLLKLMN SNEEAYNYIV KKLDPDNLNL
     ESHKKIFNLI AENKLLDLES RNKIIEIKCD DAKSSSEWIN ICEEKFANND CNIEELIDDY
     IFNIKKFKLE ESKKEIMKKI KYYETNGMIE KSLKMVKELN HIQEEINSLL
//
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