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Database: UniProt
Entry: Q92N97_RHIME
LinkDB: Q92N97_RHIME
Original site: Q92N97_RHIME 
ID   Q92N97_RHIME            Unreviewed;       667 AA.
AC   Q92N97;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   31-JUL-2019, entry version 129.
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:CAC46897.1};
GN   ORFNames=SMc01567 {ECO:0000313|EMBL:CAC46897.1};
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC46897.1, ECO:0000313|Proteomes:UP000001976};
RN   [1] {ECO:0000313|EMBL:CAC46897.1, ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|EMBL:CAC46897.1,
RC   ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2] {ECO:0000313|Proteomes:UP000001976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F.,
RA   Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA   Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA   Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA   Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA   Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA   Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591688; CAC46897.1; -; Genomic_DNA.
DR   RefSeq; NP_386424.1; NC_003047.1.
DR   RefSeq; WP_010969855.1; NC_003047.1.
DR   STRING; 266834.SMc01567; -.
DR   EnsemblBacteria; CAC46897; CAC46897; SMc01567.
DR   GeneID; 1233985; -.
DR   KEGG; sme:SMc01567; -.
DR   PATRIC; fig|266834.11.peg.3797; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014484; -.
DR   KO; K02316; -.
DR   OMA; DEPILCF; -.
DR   Proteomes; UP000001976; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001976};
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:CAC46897.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001976};
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:CAC46897.1};
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   DOMAIN      265    347       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      43     67       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION      436    462       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      608    628       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   667 AA;  74010 MW;  66856D630AF056E2 CRC64;
     MRFSPSFLDE IRDRVPISDV IGKRVTWDRR KTNVSRGDYW ACCPFHGEKS PSFHCEDRKG
     RYHCFGCGVS GDHFRFLTEL EGLSFPEAVQ QIADLAGVPM PQPDPQAEQR ERERTSLLDV
     MELATQFFQD QLQTANGAKA RAYLRERGLT GRTIETFRLG FAPDSRNALK EFLAGKGIGK
     EQIEACGLVV HGDGIPVSYD RFRDRIMFPI PSAREKVIAF GGRAMSPDAP AKYLNSNETE
     LFHKGNVLFN FARARRASQG ADGAGTIIAV EGYMDVIALH QAGIENAVAP LGTALTENQL
     DLLWKMTTQP VLCFDGDGAG VRAAHRAVDL ALPHLKPGRS VRFALLPEGK DPDDVVRHDG
     REPFDKVLAN ARSLADMVWQ REVQGGDFDT PEKRAELEAR LRQVTSVIAD ESVRRHYGQD
     MRDRLNAFLQ GSAPFRGERR PFERGGRQAG RQGGRGWSPA PNPVMGAAVE AGTAGSSKLN
     QMLKAGGSLR PPVLRESVLA LTIVNHPQLL FDEYDEIATI EFDHRDLQRC WAAVLNAAAA
     NGLRLTRETL MEQLEAEGFS ALIGALDQQV RYARLWTATA AAAPEDAREG YLQALTLHRR
     TKALLWQKRE LEREIAEATA SEDVEQGQRL VRAMEEVQLE LHRMDKLEAI IEGFGVLSGR
     VKGPAAR
//
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