UniProt: E6MTX4

Database: UniProt
Entry: E6MTX4_NEIMH

LinkDB:  E6MTX4_NEIMH 
Original site:  E6MTX4_NEIMH

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (1)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   E6MTX4_NEIMH            Unreviewed;       590 AA.
AC   E6MTX4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   ECO:0000313|EMBL:EFV64933.1};
GN   ORFNames=NMH_0215 {ECO:0000313|EMBL:EFV64933.1};
OS   Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=909420 {ECO:0000313|EMBL:EFV64933.1, ECO:0000313|Proteomes:UP000032707};
RN   [1] {ECO:0000313|EMBL:EFV64933.1, ECO:0000313|Proteomes:UP000032707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76 {ECO:0000313|EMBL:EFV64933.1,
RC   ECO:0000313|Proteomes:UP000032707};
RX   PubMed=21378179; DOI=10.1128/JB.01331-10;
RA   Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA   van de Beek D., Pannekoek Y., van der Ende A.;
RT   "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL   J. Bacteriol. 193:2371-2372(2011).
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:EFV64933.1}.
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DR   EMBL; AEQZ01000001; EFV64933.1; -; Genomic_DNA.
DR   RefSeq; WP_002225052.1; NZ_AEQZ01000001.1.
DR   AlphaFoldDB; E6MTX4; -.
DR   SMR; E6MTX4; -.
DR   PATRIC; fig|909420.3.peg.928; -.
DR   Proteomes; UP000032707; 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; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
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; PF13155; Toprim_2; 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; SSF117023; DNA primase DnaG, C-terminal domain; 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   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          255..337
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         37..61
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   590 AA;  65915 MW;  36DFCEAD470A1019 CRC64;
     MIPSDFIDEL LAKTDIVDII DEQVPLKKGG ANYMACCPFH KEKTPSFSVS PTKQFYHCFS
     CGAHGSAIGF VMEHQGLSFP EAVQFLADRV GMVVPKVHGQ NDNPEVRAER KKKQQTLEET
     TAAAADFYAQ QLKFNPAAKA YLDKRGLSAE VIAHYGLGYA PDGWQPLTQV FQPYPNTALV
     DTGMVIDNEG RHYDRFRHRI MFPIRNPRGQ VIGFGGRVLD DSKPKYLNSP DTPLFDKGKN
     LYGLYEGRAA VKEAGRILVV EGYMDVVALA QFGVGYGVAA LGTATTAEHV KILMRQADSI
     YFCFDGDSAG RKAAWRALEN ALPQLKDDKS LHFLFLPEEH DPDSYIRAYG KAQFEDALLN
     QSKPLSEYFW EHLSDGIHLN TQEGKAELVK TSSPLLAQIT APALAYLLKQ RLSELVGIDP
     DNLAQLLGQE APKRHVKQKN YKLPPISVKQ PVMLTLVQRQ IRSLLINPDW AAYIDLPDYL
     ALDGDFACLA NLAESIKNHA AVPETAQVLE YMRGSPYEET ITRIFHSTHQ SEEMNSSSEE
     DCENFQIGMK KLLNELKYSQ IETLKQKSLQ SGLNESEKKL LLSLLTAKQN
//

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