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AQUAE:O67450

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Species (Taxon ID) Aquifex aeolicus (strain VF5). (224324)
Gene Name(s) dnaB (ECO:0000313 with EMBL:AAC07414.1)
Protein Name(s) Replicative DNA helicase (ECO:0000256 with RuleBase:RU362085)
External Links
UniProt O67450
EMBL AE000657
PIR H70427
RefSeq NP_214015.1
WP_010880953.1
PDB 4NMN
PDBsum 4NMN
ProteinModelPortal O67450
STRING 224324.aq_1472
EnsemblBacteria AAC07414
GeneID 1192981
KEGG aae:aq_1472
PATRIC 20960068
eggNOG ENOG4105CDU
COG0305
HOGENOM HOG000113196
InParanoid O67450
KO K02314
OMA WHESFID
OrthoDB EOG6T4RW5
BioCyc AAEO224324:GJBH-1056-MONOMER
Proteomes UP000000798
GO GO:0005829
GO:1990077
GO:0005524
GO:0003677
GO:0003678
GO:0046872
GO:0006269
GO:0006268
Gene3D 1.10.860.10
3.40.50.300
InterPro IPR003593
IPR007692
IPR007694
IPR007693
IPR016136
IPR027417
Pfam PF00772
PF03796
SMART SM00382
SUPFAM SSF48024
SSF52540
TIGRFAMs TIGR00665
PROSITE PS51199

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0032508

DNA duplex unwinding

PMID:24373746[1]

ECO:0000315

P

"When the dilated and constricted mutants were tested in a single-turnover, fork-unwinding assay with DnaC, the dilated mutant was able to produce ∼20% more unwound product as the wild-type helicase and did so at a slightly faster rate (Figure 5B). By contrast, while the constricted mutant could generate an amount of ssDNA comparable to that of wild-type DnaB, it took longer to do so (Figure 5B)."

complete
CACAO 11910

involved_in

GO:0006268

DNA unwinding involved in DNA replication

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10236
PANTHER:PTN001248911

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10236
PANTHER:PTN001248911
UniProtKB:P9WMR3

C

Seeded From UniProt

complete

enables

GO:0003678

DNA helicase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10236
PANTHER:PTN001248911

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692

F

Seeded From UniProt

complete

enables

GO:0003678

DNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:1990077

primosome complex

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0639

C

Seeded From UniProt

complete

involved_in

GO:0006269

DNA replication, synthesis of RNA primer

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0639

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0235

P

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

part_of

GO:1990077

primosome complex

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000171759

C

Seeded From UniProt

complete

involved_in

GO:0006269

DNA replication, synthesis of RNA primer

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000171759

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000171759

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000171759

F

Seeded From UniProt

complete

enables

GO:0003678

DNA helicase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000171759

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Strycharska, MS et al. (2013) Nucleotide and partner-protein control of bacterial replicative helicase structure and function. Mol. Cell 52 844-54 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page