P0ABS5

PR
Gene name
dnaG
Protein name
DNA primase
Names
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b3066
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)

399-478 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

12 structures for P0ABS5

Entry ID Method Resolution Chain Position Source
1DD9 X-ray 160 A A 111-433 PDB
1DDE X-ray 170 A A 111-433 PDB
1EQN X-ray 290 A A/B/C/D/E 111-429 PDB
1T3W X-ray 280 A A/B 434-581 PDB
2HAJ NMR - A 434-581 PDB
3B39 X-ray 235 A A/B 111-429 PDB
6CBR X-ray 150 A A/B 434-581 PDB
6CBS X-ray 185 A A/B 434-581 PDB
6CBT X-ray 210 A A/B 434-581 PDB
7T22 EM 420 A G/H/I 434-581 PDB
7T23 EM 420 A G/H 434-581 PDB
AF-P0ABS5-F1 Predicted AlphaFoldDB

No variants for P0ABS5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0ABS5

No associated diseases with P0ABS5

7 regional properties for P0ABS5

Type Name Position InterPro Accession
domain Zinc finger, CHC2-type 7 - 100 IPR002694
domain TOPRIM domain 259 - 341 IPR006171
domain DNA primase, DnaG 4 - 419 IPR006295
domain DNA primase DnaG, DnaB-binding domain 450 - 575 IPR013173
domain DNA primase, catalytic core, N-terminal 126 - 251 IPR013264
domain DNA primase, DnaB-helicase binding domain 369 - 424 IPR019475
domain Bacterial DnaG primase, TOPRIM domain 259 - 340 IPR034151

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

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
DNA-directed RNA polymerase complex A protein complex that possesses DNA-directed RNA polymerase activity.
DnaB-DnaG complex A protein complex containing homohexameric DnaB helicase, and DnaG (a primase). Facilitates the unwinding of double-stranded DNA and the synthesis of RNA primer sequences during DNA replication and repair in Prokaryotes.
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.
replisome A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.

3 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
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.
zinc ion binding Binding to a zinc ion (Zn).

3 GO annotations of biological process

Name Definition
DNA replication, synthesis of RNA primer The synthesis of a short RNA polymer, usually 4-15 nucleotides long, using one strand of unwound DNA as a template; the RNA then serves as a primer from which DNA polymerases extend synthesis.
DNA unwinding involved in DNA replication The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication.
replication fork processing The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAGRIPRVFI NDLLARTDIV DLIDARVKLK KQGKNFHACC PFHNEKTPSF TVNGEKQFYH
70 80 90 100 110 120
CFGCGAHGNA IDFLMNYDKL EFVETVEELA AMHNLEVPFE AGSGPSQIER HQRQTLYQLM
130 140 150 160 170 180
DGLNTFYQQS LQQPVATSAR QYLEKRGLSH EVIARFAIGF APPGWDNVLK RFGGNPENRQ
190 200 210 220 230 240
SLIDAGMLVT NDQGRSYDRF RERVMFPIRD KRGRVIGFGG RVLGNDTPKY LNSPETDIFH
250 260 270 280 290 300
KGRQLYGLYE AQQDNAEPNR LLVVEGYMDV VALAQYGINY AVASLGTSTT ADHIQLLFRA
310 320 330 340 350 360
TNNVICCYDG DRAGRDAAWR ALETALPYMT DGRQLRFMFL PDGEDPDTLV RKEGKEAFEA
370 380 390 400 410 420
RMEQAMPLSA FLFNSLMPQV DLSTPDGRAR LSTLALPLIS QVPGETLRIY LRQELGNKLG
430 440 450 460 470 480
ILDDSQLERL MPKAAESGVS RPVPQLKRTT MRILIGLLVQ NPELATLVPP LENLDENKLP
490 500 510 520 530 540
GLGLFRELVN TCLSQPGLTT GQLLEHYRGT NNAATLEKLS MWDDIADKNI AEQTFTDSLN
550 560 570 580
HMFDSLLELR QEELIARERT HGLSNEERLE LWTLNQELAK K