Q6LXR3

PR
Gene name
dnaG
Protein name
DNA primase DnaG
Names
Species
Methanococcus maripaludis (strain S2 / LL)
KEGG Pathway
mmp:MMP1286
EC number
2.7.7.101: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

249-396 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q6LXR3

Entry ID Method Resolution Chain Position Source
AF-Q6LXR3-F1 Predicted AlphaFoldDB

No variants for Q6LXR3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6LXR3

No associated diseases with Q6LXR3

3 regional properties for Q6LXR3

Type Name Position InterPro Accession
domain Heat shock protein DnaJ, cysteine-rich domain 136 - 218 IPR001305
domain DnaJ domain 3 - 79 IPR001623
domain Chaperone DnaJ, C-terminal 123 - 340 IPR002939

Functions

Description
EC Number 2.7.7.101 Nucleotidyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
DNA-directed RNA polymerase complex A protein complex that possesses DNA-directed RNA polymerase activity.
exosome (RNase complex) A ribonuclease complex that has 3-prime to 5-prime exoribonuclease activity and possibly endoribonuclease activity, producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.
primosome complex Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart.

3 GO annotations of molecular function

Name Definition
DNA primase activity Catalysis of the synthesis of a short RNA primer on a DNA template, providing a free 3'-OH that can be extended by DNA-directed DNA polymerases.
metal ion binding Binding to a metal ion.
poly(A) binding Binding to a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDLGTTKYII YTELIADGYV EKHDVIGAIF GQTEGLLSNE LDLRDLQKSG RIGRIDVELE
70 80 90 100 110 120
NINGKSFAKI TLPSSLDKVE TSILAATLET IDRVGPCFAT VKITEVEDIR VSKRQYITNR
130 140 150 160 170 180
ARSILRKLMD EMIDTYEITE EIKESLRTEE IMEYGPENLP CGPNIIHSDS IIVVEGRADV
190 200 210 220 230 240
LNLLRCGIKN TVAVEGTSVP KSIMELTKKK TTTAFTDGDR GGELILKELL QTCDIDYVAR
250 260 270 280 290 300
APYGKEVEGT SKKELMKCLR AKVPVEQIVG NNCNGSGVIE SNTPKEIVEP ITPKHFEKVE
310 320 330 340 350 360
TPAVIEPVFK EDAIEEETII VEPVKKAETE IIDVDATNET QSEKKFSGVK EIVDSIKNTG
370 380 390 400 410 420
NVKFVVDGTE KTNTFKEFLT NIHEIKKMDF FAADMPISQK IVDLLYDKTP IIVGKEINVT
430
KKPVNLRLFS FDEIVA