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ECOLI:RNH

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) rnhA (synonyms: dasF, herA, rnh, sdrA)
Protein Name(s) Ribonuclease HI

RNase HI Ribonuclease H RNase H

External Links
UniProt P0A7Y4
EMBL K00985
V00337
X04027
U70214
U00096
AP009048
PIR A92401
RefSeq NP_414750.1
YP_488511.1
PDB 1F21
1G15
1GOA
1GOB
1GOC
1JL1
1JL2
1JXB
1KVA
1KVB
1KVC
1LAV
1LAW
1RBR
1RBS
1RBT
1RBU
1RBV
1RCH
1RDA
1RDB
1RDC
1RDD
1RNH
1WSE
1WSF
1WSG
1WSH
1WSI
1WSJ
2RN2
2YV0
2Z1G
2Z1H
2Z1I
2Z1J
3AA2
3AA3
3AA4
3AA5
3HYF
3QIN
3QIO
PDBsum 1F21
1G15
1GOA
1GOB
1GOC
1JL1
1JL2
1JXB
1KVA
1KVB
1KVC
1LAV
1LAW
1RBR
1RBS
1RBT
1RBU
1RBV
1RCH
1RDA
1RDB
1RDC
1RDD
1RNH
1WSE
1WSF
1WSG
1WSH
1WSI
1WSJ
2RN2
2YV0
2Z1G
2Z1H
2Z1I
2Z1J
3AA2
3AA3
3AA4
3AA5
3HYF
3QIN
3QIO
ProteinModelPortal P0A7Y4
SMR P0A7Y4
DIP DIP-47864N
IntAct P0A7Y4
MINT MINT-1224022
STRING 511145.b0214
BindingDB P0A7Y4
ChEMBL CHEMBL1770039
PaxDb P0A7Y4
PRIDE P0A7Y4
EnsemblBacteria AAC73319
BAA77885
GeneID 12934461
946955
KEGG ecj:Y75_p0205
eco:b0214
PATRIC 32115541
EchoBASE EB0853
EcoGene EG10860
eggNOG COG0328
HOGENOM HOG000040465
InParanoid P0A7Y4
KO K03469
OMA ITSWIHN
OrthoDB EOG696BTR
PhylomeDB P0A7Y4
BioCyc EcoCyc:EG10860-MONOMER
ECOL316407:JW0204-MONOMER
MetaCyc:EG10860-MONOMER
EvolutionaryTrace P0A7Y4
PRO PR:P0A7Y4
Proteomes UP000000318
UP000000625
Genevestigator P0A7Y4
GO GO:0005737
GO:0004519
GO:0000287
GO:0003676
GO:0004523
GO:0043137
GO:0090305
GO:0090502
Gene3D 3.30.420.10
HAMAP MF_00042
InterPro IPR022892
IPR012337
IPR002156
Pfam PF00075
SUPFAM SSF53098
PROSITE PS50879

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004523

ribonuclease H activity

PMID:4572736[1]

ECO:0000314

F

See Fig 2

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000068227
WB:WBGene00004382
WB:WBGene00022888

P

Seeded From UniProt

complete

involved_in

GO:0043137

DNA replication, removal of RNA primer

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10860
PANTHER:PTN000068227

P

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10860
FB:FBgn0023171
MGI:MGI:1335073
PANTHER:PTN000068227
PomBase:SPBC336.06c
SGD:S000004847
UniProtKB:O60930
WB:WBGene00004382
WB:WBGene00022888

F

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

PMID:4572736[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

PMID:4572736[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

PMID:4572736[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043137

DNA replication, removal of RNA primer

PMID:6319961[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

PMID:4572736[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

PMID:25903123[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002156
InterPro:IPR036397

F

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002156
InterPro:IPR022892

F

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.26.4

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075854

F

Seeded From UniProt

complete

enables

GO:0004523

RNA-DNA hybrid ribonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075854

F

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075854

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000075854

C

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Miller, HI et al. (1973) Ribonuclease H (hybrid) in Escherichia coli. Identification and characterization. J. Biol. Chem. 248 2621-4 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
  3. Ogawa, T & Okazaki, T (1984) Function of RNase H in DNA replication revealed by RNase H defective mutants of Escherichia coli. Mol. Gen. Genet. 193 231-7 PubMed GONUTS page
  4. Petzold, C et al. (2015) Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity. J. Biol. Chem. 290 14626-36 PubMed GONUTS page