Q46DW1

PR
Gene name
dnaG
Protein name
DNA primase DnaG
Names
Species
Methanosarcina barkeri (strain Fusaro / DSM 804)
KEGG Pathway
mba:Mbar_A0959
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)

350-420 (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 Q46DW1

Entry ID Method Resolution Chain Position Source
AF-Q46DW1-F1 Predicted AlphaFoldDB

No variants for Q46DW1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q46DW1

No associated diseases with Q46DW1

2 regional properties for Q46DW1

Type Name Position InterPro Accession
domain TOPRIM domain 171 - 257 IPR006171
domain Archaeal primase DnaG/twinkle-like, TOPRIM domain 171 - 244 IPR034154

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
MQNTDTTKYI IHSKINADGV IERPDIVGAI FGQTEGLLGA DLDLRDLQKT GRIGRIEVMV
70 80 90 100 110 120
TAKGGKTKGN IFVPSSLDKV ETSILAASLE TIDRVGPCSA KIEVFQVEDV RAVKRKKIIE
130 140 150 160 170 180
RAKLIFTKMF DETVPESQEL ADEVRQSVRV DELTYYGKSR IPCGPNVLNS DAIIILEGRA
190 200 210 220 230 240
DILNLLRYGI KNTICVGGTN IPPEVAELTK KKTVTAFTDG DRGGELIIRE LLQVADIDYV
250 260 270 280 290 300
ARAPDGKCVE DLVQKEVIRA LRRKVPVEQI IEKYGIQERE GEESTRVERG SKRKIRAPEI
310 320 330 340 350 360
APRITEKKLH KRIKIHRVSS KPDLYEEELP EEETKGKASA KAFEKVSVKA AEKVSEMVPA
370 380 390 400 410 420
TAGKVKTRSI VAKPQISARK APAAARVSRE KPAEKVPSAV KVSRGEAVRV SPAPVKTVPV
430 440 450 460 470 480
SPEATRFRPH VEALKGTLTA RILDSQDKVI EEIAVRDLAS RLKTYKENIQ SVVFDGVITQ
490 500 510
RLVDIASSNA IKNLIGVKIG NIAKVPADME VLTASML