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Database: UniProt
Entry: J9HGI3_9ACTN
LinkDB: J9HGI3_9ACTN
Original site: J9HGI3_9ACTN 
ID   J9HGI3_9ACTN            Unreviewed;       602 AA.
AC   J9HGI3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   11-DEC-2019, entry version 43.
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=A27L6_002700000350 {ECO:0000313|EMBL:EJX36062.1};
OS   actinobacterium SCGC AAA027-L06.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=913338 {ECO:0000313|EMBL:EJX36062.1, ECO:0000313|Proteomes:UP000006343};
RN   [1] {ECO:0000313|EMBL:EJX36062.1, ECO:0000313|Proteomes:UP000006343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AAA027-L06 {ECO:0000313|EMBL:EJX36062.1,
RC   ECO:0000313|Proteomes:UP000006343};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Huntemann M.,
RA   Wei C.-L., Han J., Chen A., Kyrpides N., Mavrommatis K., Markowitz V.,
RA   Szeto E., Pagani I., Pati A., Garcia S.L., McMahon T., Srivastava A.,
RA   Grossart H.-P., Martinez M., Stepanauskas R., Sczyrba A., Warnecke F.,
RA   Woyke T.J.;
RT   "The standard draft genome of actinobacterium SCGC AAA027-L06.";
RL   Submitted (AUG-2012) 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 replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       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|HAMAP-Rule:MF_00974,
CC         ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJX36062.1}.
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DR   EMBL; AJWB01000056; EJX36062.1; -; Genomic_DNA.
DR   EnsemblBacteria; EJX36062; EJX36062; A27L6_002700000350.
DR   PATRIC; fig|913338.3.peg.735; -.
DR   Proteomes; UP000006343; Unassembled WGS sequence.
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; 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; 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   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   Primosome {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|SAAS:SAAS00709304};
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|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   DOMAIN          262..348
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         41..65
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   602 AA;  66747 MW;  299C3FBBB40AE4A7 CRC64;
     MAGRIKDEDV TYIRDHSPID DVVADYVQLK NAGGGQKKGL CPFHDEKSPS FHVTPSKGYF
     HCFGCQVGGD VIAFIMKLEH LTFTETVERL ADRIGYTLRY ESGGSTTTPS INRSRLVAAN
     TAASIFYQEQ LQLPAAQIGR DFLTKRGFDR DAAKQFNVGY APDEWDGLYK HLKGKGFTDE
     ELNLAGLVKE GTKGMIDRYR NRLIWPVKDI SGDVVGFGAR KLASDEVDTG PKYLNSPETP
     VYKKNQILYG LDMAKKEISK NRQVVIVEGY TDVMAAHIAG VSTAVATCGT AFGDEHIRII
     RRLLMDADAF RGEVIFTFDG DAAGQKAALR AFEDDQKFVA QTFVAVEPNG MDPCELRQAH
     GDDAVRNLIA RRVPLFEFAI KSVIANYDIT AAEGRVNALN QVAPLIGKIR DASLRPEYVR
     LLAGWLGMEV DIVSTAVKRS GGSSAAPSER KVNLTDPILV LEREVLKVKL QLPQLAHSWV
     DLEPTAFSFA LYDQLRKLID AQEVFNIQEL IESSDTDELK SLVTELTVEP IRTDGEVSDR
     YITSIFARLR EVALSRSIAE IKSTLQRLNP VENDAQYQEI FGELVGMEAA RRVQKELALG
     QS
//
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