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Database: UniProt
Entry: F4KK57_PORAD
LinkDB: F4KK57_PORAD
Original site: F4KK57_PORAD 
ID   F4KK57_PORAD            Unreviewed;       676 AA.
AC   F4KK57;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   31-JUL-2019, entry version 56.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   OrderedLocusNames=Poras_0839 {ECO:0000313|EMBL:AEE12782.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC
OS   10618 / JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides
OS   asaccharolyticus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12782.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Pagani I., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL   Submitted (APR-2011) 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|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};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974};
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|SAAS:SAAS00709351}.
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DR   EMBL; CP002689; AEE12782.1; -; Genomic_DNA.
DR   RefSeq; WP_004331178.1; NC_015501.1.
DR   STRING; 879243.Poras_0839; -.
DR   EnsemblBacteria; AEE12782; AEE12782; Poras_0839.
DR   KEGG; pah:Poras_0839; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   KO; K02316; -.
DR   OMA; PVKQIWK; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; PASA879243:G1GX8-872-MONOMER; -.
DR   Proteomes; UP000006545; 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   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:UP000006545};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   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|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006545};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      261    344       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      446    466       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      619    639       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   676 AA;  76805 MW;  51FF36DB2DBFB571 CRC64;
     MIDEQTKQLI IDTARIEDVV SDFVQLRRKG SGFVGLCPFH KDRHPSFIVT PSKNICKCFA
     CGAGGTPISF IMKIQNCSFV EALRYLAQKY NIPMPEREMT EEEQQRKNER EALYLANEVA
     AKFFTEQLLS SEEGLDIALP YFTQRGVRSE AIQAFGLGYS PSDRRALAKY VEEHGYDMES
     FVATGLLYAP SEGRPSGDRY HERVIFPIYN VGGRVVGFGG RTMRKADKIA KYINSPESII
     YDKSRELYGL YQAKQAIGRL DRSIIVEGYL DVIAMHQVGI ENVVATSGTA LTESQIQLLR
     RFSRNVLVLF DGDEAGVKAA LRSIDMLLAE GMQIKLLVLP DGEDPDEFVA KRSRTEVEEY
     FAAHEQDFLT FKSQLYAPQM ASDPQLKTQL MRDILQSIAT IPDSLERIVY IQQMSQMYGV
     AEDLLLQQIK QERFSRGRVY QYAPPAAATP EERAPEETPQ EVSPLDAPMS NEALDLVRLV
     VRYGERKLKI SVQDEEAGEG AEPMVIQVAV ANFVYQELKQ DDIVIEHPLV KRILNDSNKM
     MLEELSDSED GESKHRCGSF LCNSEVPQVA ALAVDLYATP YRLSRKAREE LQMPDDDDEK
     VPDEWVRDMT FKVLYTYKLA YAEEHCQQIS QQIQALQQEH PEADYESYQP LLQELSTWQE
     IRKAFAQFSG QRVVIS
//
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