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Database: UniProt
Entry: A0A1Z4JEI4_LEPBY
LinkDB: A0A1Z4JEI4_LEPBY
Original site: A0A1Z4JEI4_LEPBY 
ID   A0A1Z4JEI4_LEPBY        Unreviewed;       634 AA.
AC   A0A1Z4JEI4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   05-DEC-2018, entry version 10.
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=NIES2135_19910 {ECO:0000313|EMBL:BAY55169.1};
OS   Leptolyngbya boryana NIES-2135.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY55169.1, ECO:0000313|Proteomes:UP000217895};
RN   [1] {ECO:0000313|EMBL:BAY55169.1, ECO:0000313|Proteomes:UP000217895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY55169.1,
RC   ECO:0000313|Proteomes:UP000217895};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-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|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}.
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DR   EMBL; AP018203; BAY55169.1; -; Genomic_DNA.
DR   RefSeq; WP_017286720.1; NZ_AP018203.1.
DR   Proteomes; UP000217895; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000217895};
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:UP000217895};
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      265    350       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      41     65       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   634 AA;  72763 MW;  C8BA3D3B873F9F7F CRC64;
     MNVPRLHPDT IEQVKQRADI VDVVSEHVVL KKQGKDFVGL CPFHDDKSPS FTVSPSKQFY
     YCFSCGAGGN TIKFLMELGK RNFSEVVLDL ARKYQVPVQT LQAEDRQELQ RQLSVREQLY
     EILAITAKFY EHALQQPQGA DALAYLRRDR KLSVETIQQF QLGYAPAGWD ILCKYLVEQK
     KYPIVLLEKA GLLVPRKTGD GYYDRFRNRL MVPIQDSQGR VIGFGGRTLT DEQPKYLNSP
     ETELFDKGRT LFGLDKAKSA IAKQDQAVVV EGYFDVIALH AAGVTNAVAS LGTALSIAQV
     KQLLRYTESK RVVFNFDADR AGVQAAERAI GEVATLAYQG EVQLRVLNLP DGKDPDDFLK
     NHSAKAYQDL LDHAPLWLDW QINQAISNQD LKQSDQFQQA VMAIVALLGN LPNPSLRTHY
     IHHCSELLSQ GNSRLTQQIE ENLRLQVRGQ RWHGRSQKWQ TPGDRNLLEE CEAQLLRLYL
     HAPEYRVELR NAISAQDLEF SLSHHRFLWR QITDIEHDSL EVDLLEQLRD RTHNFPREMS
     QVYSLFELDE KTQRDILRAP LVIRSATAGI ERVMCEKRYR HFLDLWQKTD LSTTPDLGQF
     YQQKAYVEKQ RITELDRLRQ VSFVDLVQAP IAVD
//
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