GenomeNet

Database: UniProt
Entry: A0A3A9ZSA3_9ACTN
LinkDB: A0A3A9ZSA3_9ACTN
Original site: A0A3A9ZSA3_9ACTN 
ID   A0A3A9ZSA3_9ACTN        Unreviewed;       631 AA.
AC   A0A3A9ZSA3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=D7223_05125 {ECO:0000313|EMBL:RKN51099.1};
OS   Micromonospora endolithica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN51099.1, ECO:0000313|Proteomes:UP000281726};
RN   [1] {ECO:0000313|EMBL:RKN51099.1, ECO:0000313|Proteomes:UP000281726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN51099.1,
RC   ECO:0000313|Proteomes:UP000281726};
RX   PubMed=15046305; DOI=10.1078/072320204322881781;
RA   Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT   "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT   Micromonospora endolithica sp. nov. and two isolates related to
RT   Micromonospora coerulea Jensen 1932.";
RL   Syst. Appl. Microbiol. 27:166-174(2004).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00974,
CC         ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKN51099.1}.
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; RBAK01000001; RKN51099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9ZSA3; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000281726; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR019475; DNA_primase_DnaB-bd.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR030846; DnaG_bac.
DR   InterPro; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00766; DnaG_DnaB_bind; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281726};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          273..359
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         49..73
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
FT   REGION          453..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  68534 MW;  43158750456A0BE6 CRC64;
     MYAEGVATMA GRIRDEDIAL VRERTSIAEV ISDTVTLKSA GGGNLKGLCP FHDEKSPSFN
     VSPARNVWYC FGCGAGGDAI KFLMDADHLS FVESVERLAA RAGIQLRYLE SDHTTPRARP
     QQGQRQRLVA AHAAAVEFYR AQLTTAGARP AREFLARRGF DRAAAERYGC GFAPDGWDLL
     TKHLRQQGFS HDELVTAGLS RPARSGSLID RFRRRLLWPI RDLTGDVIGF GARKLFDDDD
     GPKYLNTPET PIYKKSHVLY GVDQAKREIA KQGKVVVVEG YTDVMACHLA GVPTAVATCG
     TAFGADHIGV LRRLLMDTDA VAGEIIFTFD GDAAGQKAAL RAFDDDQRFV GRTFIAVSPD
     NMDPCDLRLA KGDLAVRDLV ARREPLVDFA LRHVIGRYDL DTVDGRVEAM RRAAPLVAKI
     KDREKRPEYV RKLAGDLGME IEPVQRAVLA AGNAPPTGRG TDAPARPAPA EPAVDSPRSM
     VEREALKLAL QEPVLAGPMF DAVEASEYRH PVHAAVREAV AAAGGAAAAS GGAVWIESVR
     DACADLAAQA LVGELAVEPL RIDGEPDPRY VSVTMARLQW GSVTSRIRDL KSRIQRINPV
     NNKDEYFAAF GELLSLEQHA RALREQAAGG L
//
DBGET integrated database retrieval system