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Database: UniProt
Entry: A0A1I5GFA5_PARPN
LinkDB: A0A1I5GFA5_PARPN
Original site: A0A1I5GFA5_PARPN 
ID   A0A1I5GFA5_PARPN        Unreviewed;       647 AA.
AC   A0A1I5GFA5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-2019, entry version 16.
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   ORFNames=EB844_11680 {ECO:0000313|EMBL:RNI17115.1};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=82367 {ECO:0000313|EMBL:RNI17115.1, ECO:0000313|Proteomes:UP000278340};
RN   [1] {ECO:0000313|EMBL:RNI17115.1, ECO:0000313|Proteomes:UP000278340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJUST38 {ECO:0000313|EMBL:RNI17115.1,
RC   ECO:0000313|Proteomes:UP000278340};
RA   Wang J.;
RT   "Substantial enhancement of N-methylpyrrolidone bio-mineralization by
RT   Paracoccus pantotrophus under anoxic condition: metabolite mechanism
RT   and genomic characterization.";
RL   Submitted (NOV-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RNI17115.1}.
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DR   EMBL; RIAQ01000019; RNI17115.1; -; Genomic_DNA.
DR   RefSeq; WP_024844484.1; NZ_RIAQ01000019.1.
DR   Proteomes; UP000278340; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000278340};
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   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   ZN_FING      43     67       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
SQ   SEQUENCE   647 AA;  71093 MW;  521FC2E151447727 CRC64;
     MSLPPQFLDE IRARVPLSRV IGRKVVWDLR RSNQAKGDWW APCPFHGEKT ASFHVDDQKG
     FYYCFGCHAK GDALTFLREA EGLGFIEAVE LLAAEAGLPM PERDPRQVQR ADRRTELVEV
     MEQAVRWFRM QLGMGPAEAA RAYLARRGLD EAACEAFGIG FAPDQRQGLF NALRAKGIAE
     ALIVEAGLAA KPDEGGAPFD RFRGRITFPI RDGRGRCIAF GGRAMDPNAR AKYLNSPETP
     LFDKGRNLYN IGPARAAVAK GRPLVVAEGY MDVIALVRAG FEGAVAPLGT AITEDQLRLM
     WRISPEPVIA LDGDEAGLRA AMRLIDLALP MTGPGQALRF AFLPQGLDPD DLIRARGAGA
     MGAVLDEARP LVDLLWRRET EGRVFDSPER RAALDKALAE AVAKIPDKDT RDHYHAVLRN
     LKWELFGNRR RADAPAPARP AREWQGREWQ GGRGARFQPV APTAPTRASR LSSPDLNEHE
     AEALVEAMVL AICATHPGLI APVESRLERL EPQDADRAAL VHDLLSGTQS QAGQRALESI
     MADPHVRAAP AILRPHDRDA AAGILANALD RIEARRAARE EIARAEAEIE GLADEGLTWR
     MAQSARARQQ ADHPSLADLS DLGEDSDAYR AILDAALKNE IWRKPRR
//
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