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Database: UniProt
Entry: F9ZCK2_ODOSD
LinkDB: F9ZCK2_ODOSD
Original site: F9ZCK2_ODOSD 
ID   F9ZCK2_ODOSD            Unreviewed;       645 AA.
AC   F9ZCK2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-NOV-2019, entry version 62.
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   OrderedLocusNames=Odosp_2532 {ECO:0000313|EMBL:ADY33515.1};
OS   Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 /
OS   JCM 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY33515.1, ECO:0000313|Proteomes:UP000006657};
RN   [1] {ECO:0000313|EMBL:ADY33515.1, ECO:0000313|Proteomes:UP000006657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC   {ECO:0000313|Proteomes:UP000006657};
RX   PubMed=21677857; DOI=10.4056/sigs.1714269;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A.,
RA   Hammon N., Deshpande S., Cheng J.F., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A.,
RA   Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brambilla E.M., Rohde M., Detter J.C.,
RA   Woyke T., Bristow J., Markowitz V., Hugenholtz P., Eisen J.A.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Odoribacter splanchnicus type strain
RT   (1651/6).";
RL   Stand. Genomic Sci. 4:200-209(2011).
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; CP002544; ADY33515.1; -; Genomic_DNA.
DR   RefSeq; WP_013612708.1; NC_015160.1.
DR   STRING; 709991.Odosp_2532; -.
DR   EnsemblBacteria; ADY33515; ADY33515; Odosp_2532.
DR   GeneID; 41367331; -.
DR   KEGG; osp:Odosp_2532; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   KO; K02316; -.
DR   OMA; PVKQIWK; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; OSPL709991:G1GRN-2583-MONOMER; -.
DR   Proteomes; UP000006657; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006657};
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,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006657};
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      259    340       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   COILED      505    525       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   645 AA;  73957 MW;  2BC214515480FFCF CRC64;
     MIDQATIQKI FDAADIYEVI SDFVSLKKRG VNYVGCCPFH NEKTGSFTVS PSKGIYKCFG
     CGKGGNAVNF IMEHEQLSYV EALRWLAAKY NIIIEEKELS EHEKQEKSER ESMLIVTNYA
     EEFFVQQLLH TDEGKSVGLG YFRRRGLDDR TIEKFGLGYC PEAWDGFTKA ALEKGYKKEF
     LVKTGLTIES ERGLFDRFRA RVMFPIRDLA GKIIAFGGRI MTNDKKSAKY LNSPESEIYH
     KSRTLYGIYF AKKSIVQHNR CYLVEGYLDV ISFHQKGIEN TVASSGTSLT IEQIRLIRRL
     TPNVTIIYDG DAAGIKASLR GIDLVLEEGL NVRVVSLPDG EDPDSYAQAH TAEEVLEYIS
     GHETDFIHFK TKLLLTQAGS DPIERAKLIT DIVRSISLIP DTITRSVYVQ ETANQMKVEE
     KLLYNEIARI RKEKVGDPTP LPYKSPTQQP PRVTLTPAKT VQVTPCDTEE MVLVRYLLLF
     GGQELYEEER DGMPYSVTVG EYIIHELAED ELEMLNPRLR EIQNEYRKNY RNPGFIPSKY
     FIGNPDVSIC ELVADILSEP YELSKLWTLK DSSMRTEEMM LDELLPKIVD NYKMRRVEIL
     CREADEKILE FQNAGDMERL VEWIKKKNAM IKVRSRINEK LKRTI
//
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