GenomeNet

Database: UniProt
Entry: A0A2A4WVY2_9BACT
LinkDB: A0A2A4WVY2_9BACT
Original site: A0A2A4WVY2_9BACT 
ID   A0A2A4WVY2_9BACT        Unreviewed;       582 AA.
AC   A0A2A4WVY2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   10-APR-2019, entry version 6.
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   ECO:0000313|EMBL:PCI73967.1};
GN   ORFNames=COB28_03035 {ECO:0000313|EMBL:PCI73967.1};
OS   Candidatus Dependentiae bacterium.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=2030827 {ECO:0000313|EMBL:PCI73967.1};
RN   [1] {ECO:0000313|EMBL:PCI73967.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NORP98 {ECO:0000313|EMBL:PCI73967.1};
RX   PubMed=29099490; DOI=10.1038/ismej.2017.187;
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy
RT   inhabits the cold, oxic subseafloor aquifer.";
RL   ISME J. 12:1-16(2018).
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:PCI73967.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; NVUD01000006; PCI73967.1; -; Genomic_DNA.
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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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   DOMAIN      256    337       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      34     58       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   COILED      540    560       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   582 AA;  66318 MW;  0D0EEA1C522EDC8C CRC64;
     MTIFDHVKTS LSILEVVGSY VSLKRMGGYY KGPCPLHSEK DASFTVSPDR NIFYCFGCQV
     GGDVISFIAR IERLTQGQAV RHLIEQHNLV IPESLQKEMS QHTETYVKES LSSVAKACAK
     WAHQHFLNDE YAQKYLASRG MSEQMMKYFE IGLVAGGIKG MQRFIKGMQA ENILLDDLKS
     VGFVMDGKTH PYSPFEDRIL FPIKDSIGRY IAFSGRVFLP EDDRARYYNS KESEMFSKRQ
     TLFGFDMARK KAQQTNTIFL VEGGMDVVAM VQSGYENSVA TLGTACSADH LQMLRRFVHT
     LVVVYDGDRA GQNAIEKVAE LCWDIAITLK VVSLPTGEDP ASLLQKGIPL NTFIEKQEDI
     FSFLIKKTSK NFFNQSMPEK LRLCAQVVQM VKHATHGLKR HLLXQQISTA LQIPVAMLQK
     VSXQELRKPT YELKEKEQQP TLSVQVAVLT GIEEKVTSFF FTADRQSSEY LKVYICMDEY
     WNSPVQKIVE KWFQSPIADM HCFLDSLPES DRQLILSIVM KYGEGISYEV VETLMNELKK
     RKWKAEVNRL KQDLDSARHE GDTARVHALI SNFLILKQKI QN
//
DBGET integrated database retrieval system