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Database: UniProt
Entry: A0A0M2Y361_9SPHI
LinkDB: A0A0M2Y361_9SPHI
Original site: A0A0M2Y361_9SPHI 
ID   A0A0M2Y361_9SPHI        Unreviewed;       667 AA.
AC   A0A0M2Y361;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 24.
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   ORFNames=AAW12_05985 {ECO:0000313|EMBL:KKO92294.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO92294.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO92294.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO92294.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito
RT   Anopheles gambiae.";
RL   Submitted (APR-2015) 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|PIRNR:PIRNR002811, 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, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       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:KKO92294.1}.
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DR   EMBL; LBGU01000028; KKO92294.1; -; Genomic_DNA.
DR   RefSeq; WP_046672700.1; NZ_LBGU01000028.1.
DR   EnsemblBacteria; KKO92294; KKO92294; AAW12_05985.
DR   PATRIC; fig|1643451.3.peg.1767; -.
DR   Proteomes; UP000034524; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000034524};
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   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034524};
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   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      260    341       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION      438    465       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      617    637       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    450    464       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   667 AA;  75533 MW;  3F1AEBBB03261B15 CRC64;
     MIKQEVIDKV LETARIEEVV GDFVDLKKRG TSLIGNCPFH HEKTPSFHVS VSKGIYKCFG
     CGVGGDSLKF VMELEKFSYP EAIRYLADKY SIQIEEVERS PAQLAAQDKR ESLYVLSAWA
     SKFFAEQLWK TEMGQVIGLN YFKERGYRED IIKKFELGYS PEEWTALVDK AQVAGFHPDY
     LAASGLAIER DDKSLYDRFR GRVMFPIHNL TGRVIGFGGR TLKTDKKVAK YVNSPESEIY
     HKSDVLYGLN FAKKAIMEED NCYLVEGYAD VLSVHQAGVE NVVSSSGTSL TTGQIKLISR
     FTKNVTILYD GDEAGIKASL RGTDMLLEEG LNVKVLLFPD GNDPDSYVQK FGATAFKDYV
     KSNQQDFIFY KTNILLRDAN NDPIKRAEVI RDVVESIALI PDEIKVSVFI RECSSLLDIE
     ERILLTELNK IRLNRAKKAD KDAARKPQSP PPNTGMPPFG MDGPPPDFFM TDDERGGLPP
     IESVEQPAQL TSEILQEREI VRILINYGDY LATWEGDGDI PVAGLLLGNI SDIEFKDKAA
     AYILNVYREA AEKYEIPDTK QFYSNSDPAI ADLAINCVAS KYSLSENWND DKRKIYVTQE
     YEHLKQLVVT AIYRIKKRKI EAEMHHIREE MKHEQDVANL EVLIFKYQKL KEAERLLGGF
     LGNTIVK
//
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