rnhA:Gene Product(s): Difference between revisions

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[[rpsT:Gene_Product(s)|rpsT]]
[[rpsT:Gene_Product(s)|rpsT]]
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PMID:19402753
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LCMS(ID Probability):99.6
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Protein
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[[rpsN:Gene_Product(s)|rpsN]]
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Revision as of 19:32, 17 June 2011

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

RnhA

Synonyms

ribonuclease HI, degrades RNA of DNA-RNA hybrids[1], B0214[2][1], Sin[2][1], Cer[2][1], Rnh[2][1], SdrA[2][1], HerA[2][1], DasF[2][1], RnhA[2][1]

Product description

RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication[2][3]

RNase HI; participates in DNA replication[4]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0000287

magnesium ion binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00042

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc (v14.0)

complete

GO:0003676

nucleic acid binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002156

F

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

P

Seeded from Riley et al 2006 [1].

Missing: evidence

GO:0003676

nucleic acid binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012337

F

Seeded from EcoCyc (v14.0)

complete

GO:0004518

nuclease activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0540

F

Seeded from EcoCyc (v14.0)

complete

GO:0004519

endonuclease activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0255

F

Seeded from EcoCyc (v14.0)

complete

GO:0004523

ribonuclease H activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00042

F

Seeded from EcoCyc (v14.0)

complete

GO:0004523

ribonuclease H activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002156

F

Seeded from EcoCyc (v14.0)

complete

GO:0004523

ribonuclease H activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:3.1.26.4

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00042

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0006401

RNA catabolic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00042

P

Seeded from EcoCyc (v14.0)

complete

GO:0016787

hydrolase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

GO:0004523

ribonuclease H activity

PMID:4572736[5]

IDA: Inferred from Direct Assay

F

complete

GO:0003676

nucleic acid binding

PMID:4572736[5]

IDA: Inferred from Direct Assay

F

complete

GO:0004519

endonuclease activity

PMID:4572736[5]

IDA: Inferred from Direct Assay

F

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

ssb

PMID:15690043[6]

Experiment(s):EBI-881230, EBI-888507

Protein

aceE

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

aceF

PMID:15690043[6]

Experiment(s):EBI-881230, EBI-888507

Protein

lpdA

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

malP

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

priA

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

recQ

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

rplB

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

rpsC

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

sbcB

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

topA

PMID:15690043[6]

Experiment(s):EBI-881230, EBI-888507

Protein

topB

PMID:15690043[6]

Experiment(s):EBI-881230

Protein

hupA

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpmB

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpsE

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpsI

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpsN

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpsT

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

yhbY

PMID:15690043[6]

Experiment(s):EBI-888507

Protein

rpsI

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

rpsC

PMID:19402753[7] 

MALDI(Z-score):22.098379

Protein

rpsT

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

rpsN

PMID:19402753[7]

LCMS(ID Probability):99.6

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Source Notes
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Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK
EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW
VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV
Length

155

Mol. Wt

17.596 kDa

pI

8.4 (calculated)

Extinction coefficient

40,450 - 40,825 (calc based on 5 Y, 6 W, and 3 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

2..142

PF00075 RNase H

PMID:19920124[8]

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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=rnhA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:EG10860-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A7Y4

PFAM (EcoliWiki Page)

Pfam:P0A7Y4

RefSeq (EcoliWiki Page)

RefSeq:NP_414750


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Notes

Links

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References

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

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 Miller, HI et al. (1973) Ribonuclease H (hybrid) in Escherichia coli. Identification and characterization. J. Biol. Chem. 248 2621-4 PubMed
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  7. ↑ 7.0 7.1 7.2 7.3 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  8. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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