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Database: UniProt
Entry: A0A1Z9LDT0_9CYAN
LinkDB: A0A1Z9LDT0_9CYAN
Original site: A0A1Z9LDT0_9CYAN 
ID   A0A1Z9LDT0_9CYAN        Unreviewed;       693 AA.
AC   A0A1Z9LDT0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 7.
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=CBD48_06550 {ECO:0000313|EMBL:OUW53370.1};
OS   Cyanobacteria bacterium TMED188.
OC   Bacteria; Cyanobacteria.
OX   NCBI_TaxID=1986678 {ECO:0000313|EMBL:OUW53370.1};
RN   [1] {ECO:0000313|EMBL:OUW53370.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED188 {ECO:0000313|EMBL:OUW53370.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a
RT   resource for marine microbiology.";
RL   Submitted (MAY-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:OUW53370.1}.
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DR   EMBL; NHIL01000051; OUW53370.1; -; 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; 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   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      265    350       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      41     65       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      448    467       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   693 AA;  77978 MW;  F4845AA57EAF5723 CRC64;
     MVNARLHPRT IEAVKERADI VDVVGEHVVL KKKGREFVGI CPFHDDSKPS MTVSPAKQFY
     YCFSCGAGGN SIKFLMEFQR QSFSDVVLDL ARRYQLPIET VEGPQQERLR QQLSRRDKLQ
     RALALAAGWF RSQLLAPTGQ EALAYLNXKR GLSATTQETF QLGYAPDQWD GLLNHLQQVE
     GLPPELLEAA GLVVPRKGGN GFYDRFRHRV MVPIHDRQGR VIGFGGRSLD GSEPKYLNSP
     ETELFEKGKH LFGLDKASNA IRKDDRAVVV EGYFDVIALH AAGITNAVAS LGTALSSQQI
     TQLCRVSDSK RIVLNFDADG AGVRAANRAI GEVEQLALQG QLELRVLHLP SGKDPDEFLK
     DHGSGDYRAL LDQAPLWLDW QIDQALEDRD LSRADQFQQA VSNLVALLGK LPQSAVRTHY
     LQRVAERLSG GQGRLALQLE EDLRQQVKGQ RWHGRSSRHE QPGETGQRER CEADLLRLYL
     HCPRHRAVIR QELRQRELED FAIPHHRHLW ASITDLEETN LGVGRLEAIS RREDEGEGLD
     AMDLPRLLTD QLLLESSALL SRLTPLLEPG ELQRLALADP LVQLRGTAAL LERQKSLKRC
     RHLLEAWGGQ RLQTLESCIA VLIDPEQTLN QEGEDMEVRI QTLFDDLNRD ALRYQELYYT
     ERKHIHHLDQ QRCAGYSVAD PADPSSDAVL PAA
//
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