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Database: UniProt
Entry: A0A254SR33_9BACT
LinkDB: A0A254SR33_9BACT
Original site: A0A254SR33_9BACT 
ID   A0A254SR33_9BACT        Unreviewed;       719 AA.
AC   A0A254SR33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-NOV-2019, entry version 9.
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=B7982_09075 {ECO:0000313|EMBL:OWV22369.1};
OS   Fibrobacter sp. UWB2.
OC   Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter; unclassified Fibrobacter.
OX   NCBI_TaxID=1964358 {ECO:0000313|EMBL:OWV22369.1, ECO:0000313|Proteomes:UP000197741};
RN   [1] {ECO:0000313|EMBL:OWV22369.1, ECO:0000313|Proteomes:UP000197741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWB2 {ECO:0000313|EMBL:OWV22369.1,
RC   ECO:0000313|Proteomes:UP000197741};
RA   Neumann A.P., Suen G.;
RT   "Draft genomes of novel Fibrobacter strains.";
RL   Submitted (FEB-2017) 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:OWV22369.1}.
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DR   EMBL; MWQK01000004; OWV22369.1; -; Genomic_DNA.
DR   Proteomes; UP000197741; 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; 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:UP000197741};
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      263    344       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      40     64       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      640    719       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    640    657       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    658    676       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    696    719       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   719 AA;  79890 MW;  A31BC4936EFD4967 CRC64;
     MPFYSDEIIQ ELKNQADIAL VIQQFLPLKK SGVNKYVGVC PFHDDHSPSM SVNSTLGIYK
     CFACGAGGDV FKFIQEHEKL DFKGAVEWVA NFVGFALPNL GNNVNTEVLE ERTMVRKLNE
     LACEWFEQQL TLSPKALEYL NKRHVSPETR KQFHIGYAPT GREGLIGYAA RNGFSPRDCV
     KAGLAVEKEN GGIADKFRDR LMIAIQNLSG VVVAFGGRDL SDPASHNGIK LAKYMNSPET
     ALYSKRDILF GLNHSRNAIL QEKAVIIVEG YFDLISLYQS GVQNVVAASG TALTENHASI
     LARYAKTAYL VFDGDAAGQN ATRRSLEIVL PKGLSPKVFA LSRPDGTKID PDNFVNEQGP
     DAFRRALRTA EDWLSYLGRT MPNNSPEDRA AFITQAKTLI KSIENPELRN QYLKLVSERY
     STTRSLAGIK VAHPKREKLP AAAEQPAAPQ VSVPWELLSP IEVRFANLLF RNPTLLDRAA
     EYFDMDFAAS GIQIFDSPLI DEFIQSILAQ YAETGSFSPR TLYESLSPQL QLFLEQLPDE
     TWKTPNEILE FYDTVAVLTL NLCDRYKKLI PLDSEAGMRL RMQLNKFTQG IQIVAKKRKI
     SAITPDVFAE QIIQSKTPLI ELYTEINELA MNGGNGAQFN NAPTFAQPAV QPSSPQFAAP
     AAQPPVQPNE KPPEMEAPPP FESDEQFASS EPPEDVPYDP NEDEPYVPDD DFGAMDDFG
//
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