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Database: UniProt
Entry: E1L3P3_9ACTN
LinkDB: E1L3P3_9ACTN
Original site: E1L3P3_9ACTN 
ID   E1L3P3_9ACTN            Unreviewed;       637 AA.
AC   E1L3P3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   11-DEC-2019, entry version 60.
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:EFL43565.1};
GN   ORFNames=HMPREF9248_0727 {ECO:0000313|EMBL:EFL43565.1};
OS   Atopobium vaginae PB189-T1-4.
OC   Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Atopobium.
OX   NCBI_TaxID=866774 {ECO:0000313|EMBL:EFL43565.1, ECO:0000313|Proteomes:UP000004431};
RN   [1] {ECO:0000313|EMBL:EFL43565.1, ECO:0000313|Proteomes:UP000004431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB189-T1-4 {ECO:0000313|EMBL:EFL43565.1,
RC   ECO:0000313|Proteomes:UP000004431};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFL43565.1}.
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DR   EMBL; AEDQ01000033; EFL43565.1; -; Genomic_DNA.
DR   RefSeq; WP_006304687.1; NZ_AEDQ01000033.1.
DR   STRING; 866774.HMPREF9248_0727; -.
DR   EnsemblBacteria; EFL43565; EFL43565; HMPREF9248_0727.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; GCF_000179715-HMP:HMPREF9248_RS05850-MONOMER; -.
DR   Proteomes; UP000004431; 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; 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   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:EFL43565.1};
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   ECO:0000313|EMBL:EFL43565.1};
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          252..345
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         36..60
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
FT   REGION          425..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          612..632
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        425..448
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..480
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  70430 MW;  2A0E9396906EF61C CRC64;
     MVDDDREKIR QVVNFEQLVG EHVQLTRKGS DLWGCCPFHH EKSASFHINP QTGLWKCFGC
     GAGGDMFAYV MRAENLNFAG AMQYLADKYG IELSHTPHAR DGIRRNRLFA CLAAAEQHFM
     RTLFTCPQED VSAARSYLHN RGLTSDICKA WSIGYAKGDD NLIAALTRSG FSRKELLACD
     VAHAGAYGLR SRFFNRVMFA IHDEQSKCIG FGGRVINDGK PKYLNTKETP LFHKGKHLYA
     IDKAKDGIIQ TGEVIVCEGY TDVIAMHTHG FTNTVAALGT ALTLNHIRLI ERFARTRIIC
     MFDGDAAGQK AAERAIQFID QTSLALMCVV LPNNQDPCEF LMSHPKEELA SYLSQAEPLM
     NFVLRHTLAR FDMRVPGQRI EALKSAARIL SAVKHSLLID DFATQLADML ALDVTRVKEQ
     IMKTQPMTHP SFSDEPVPSA SAPSTATPAA AMQAAPFQHG AQSADKQATP QGASASQAAH
     MQLLSSDAKR QYKAEEELLC LLVRTPGAYA RYAQPLAAIP WIDDDHKRIA QFICQHASQM
     DIPQLIDTIC AQLPSAAYIL ASGRIPSTTT LSQDDAISFL LTSIQIVSST MRMQEIKSYL
     KRNSQTLSFE ESQALLKQAT ALQKNVNNLK KSLSNDV
//
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