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Database: UniProt
Entry: A0A1L7CZ92_9CORY
LinkDB: A0A1L7CZ92_9CORY
Original site: A0A1L7CZ92_9CORY 
ID   A0A1L7CZ92_9CORY        Unreviewed;       644 AA.
AC   A0A1L7CZ92;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   31-JUL-2019, entry version 12.
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   ORFNames=CSPHI_08530 {ECO:0000313|EMBL:APT91061.1};
OS   Corynebacterium sphenisci DSM 44792.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1437874 {ECO:0000313|EMBL:APT91061.1, ECO:0000313|Proteomes:UP000185469};
RN   [1] {ECO:0000313|EMBL:APT91061.1, ECO:0000313|Proteomes:UP000185469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44792 {ECO:0000313|EMBL:APT91061.1,
RC   ECO:0000313|Proteomes:UP000185469};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium sphenisci CECT 5990(T)
RT   (=DSM 44792(T)), isolated from healthy wild penguins.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer.
CC       {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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DR   EMBL; CP009248; APT91061.1; -; Genomic_DNA.
DR   KEGG; csph:CSPHI_08530; -.
DR   KO; K02316; -.
DR   Proteomes; UP000185469; 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:InterPro.
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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
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; SM00766; DnaG_DnaB_bind; 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:UP000185469};
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|PIRNR:PIRNR002811,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185469};
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   Zinc {ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      264    350       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      464    487       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   644 AA;  70632 MW;  84BB791D65D5564D CRC64;
     MAMARGRIPD SDIAAIRENT PLEEVVGEYV QLKPGGADSL KGLSPFKDER TPSFHVRPNH
     GYYHCFSTGK GGDVFSFLME MEHLSFPEAV EACAERIGYR INYEGGGTGR REEPGTRQRL
     VAANREAQKF YAERLGTPEA AVARDFLADR GFTAEHARAF GCGYAPAGWD TLTRHLQRLG
     FEFAELEKAG LAKMGRKGPI DRFHRRLLWP IRNMAGDVIG FGARKLFDDD QLGKYMNTPE
     TMLYKKSKVL FGLDLAKRAI AESHRAVIVE GYTDVMAMHA AGETTAVAAC GTAFGEEHLQ
     LLRRLMLDDS FFRGELIYTF DGDEAGQKAA LRAFAGEQQF TGQSYVAVAP AGADPCDLRL
     AKGDAALRDL VATRTPMVEF VLRTLLADFD LDTANGRVAA LNRVVPVLAQ VRESALRDEY
     AREVAGWIGW NDEAELVRRV REEARAPRKA DPGERRRRRL AEAAAAEERR RVAAGPPTTP
     RPDPRDPRLH VQREALKLAV QEPAALGPVF SELDPEVFTH PAYRAVFDAV AAAGGIPADG
     GGAGWVADLA AAAADEVVRG LVTELGVEEI HVDPPALAGY AASVLARLQE VWVGQQIAQV
     KGTLQRMRPG DDEAGYRRLF EDLIGLEEYR RELLAEALRG PAAE
//
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