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Protein

Ribonuclease HI

Gene

rnhA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer.

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit in the absence of substrate. Requires millimolar levels of Mg2+ for maximal activity. Has low activity at micromolar concentrations of Mn2+ and is inhibited at higher Mn2+ levels. Can bind a second metal ion at a regulatory site, or after substrate binding.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Magnesium 11 Publication
Metal bindingi10 – 101Magnesium 21 Publication
Metal bindingi48 – 481Magnesium 11 Publication
Metal bindingi70 – 701Magnesium 11 Publication
Metal bindingi134 – 1341Magnesium 21 Publication

GO - Molecular functioni

  • endonuclease activity Source: EcoliWiki
  • magnesium ion binding Source: UniProtKB-HAMAP
  • nucleic acid binding Source: EcoliWiki
  • RNA-DNA hybrid ribonuclease activity Source: EcoCyc

GO - Biological processi

  • DNA replication, removal of RNA primer Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10860-MONOMER.
ECOL316407:JW0204-MONOMER.
MetaCyc:EG10860-MONOMER.
BRENDAi3.1.26.4. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease HI (EC:3.1.26.4)
Short name:
RNase HI
Alternative name(s):
Ribonuclease H
Short name:
RNase H
Gene namesi
Name:rnhA
Synonyms:dasF, herA, rnh, sdrA
Ordered Locus Names:b0214, JW0204
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10860. rnhA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → N: Loss of activity. 1 Publication
Mutagenesisi48 – 481E → Q: Loss of activity. 1 Publication
Mutagenesisi70 – 701D → N: Loss of activity. 1 Publication
Mutagenesisi124 – 1241H → A: Reduces activity. 3 Publications
Mutagenesisi130 – 1301N → A: Reduces activity. 1 Publication
Mutagenesisi134 – 1341D → A: Loss of activity. 3 Publications
Mutagenesisi134 – 1341D → H or N: Slight decrease of activity. 3 Publications

Chemistry

ChEMBLiCHEMBL1770039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Ribonuclease HIPRO_0000195372Add
BLAST

Proteomic databases

PaxDbiP0A7Y4.
PRIDEiP0A7Y4.

Interactioni

Subunit structurei

Monomer.4 Publications

Protein-protein interaction databases

BioGridi4263455. 204 interactions.
DIPiDIP-47864N.
IntActiP0A7Y4. 21 interactions.
MINTiMINT-1224022.
STRINGi511145.b0214.

Chemistry

BindingDBiP0A7Y4.

Structurei

Secondary structure

1
155
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Beta strandi5 – 1511Combined sources
Beta strandi18 – 2811Combined sources
Beta strandi31 – 4212Combined sources
Helixi44 – 5714Combined sources
Beta strandi64 – 696Combined sources
Helixi72 – 798Combined sources
Helixi82 – 876Combined sources
Turni88 – 903Combined sources
Beta strandi95 – 973Combined sources
Helixi101 – 11010Combined sources
Turni111 – 1133Combined sources
Beta strandi115 – 1206Combined sources
Helixi123 – 1253Combined sources
Helixi128 – 14215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F21X-ray1.40A1-155[»]
1G15X-ray1.90A1-155[»]
1GOAX-ray1.90A1-155[»]
1GOBX-ray2.00A1-155[»]
1GOCX-ray2.00A1-155[»]
1JL1X-ray1.30A1-155[»]
1JL2X-ray1.76A/B/C/D1-155[»]
1JXBX-ray1.60A1-155[»]
1KVAX-ray1.80A1-155[»]
1KVBX-ray1.90A1-155[»]
1KVCX-ray1.90A1-155[»]
1LAVX-ray1.80A1-155[»]
1LAWX-ray1.80A1-155[»]
1RBRX-ray1.80A1-155[»]
1RBSX-ray1.80A1-155[»]
1RBTX-ray1.80A1-155[»]
1RBUX-ray1.80A1-155[»]
1RBVX-ray1.80A1-155[»]
1RCHNMR-A1-155[»]
1RDAX-ray2.15A1-155[»]
1RDBX-ray1.90A1-155[»]
1RDCX-ray2.30A1-155[»]
1RDDX-ray2.80A1-155[»]
1RNHX-ray2.00A1-155[»]
1WSEX-ray2.30A/B1-155[»]
1WSFX-ray2.30A/B/C/D1-155[»]
1WSGX-ray2.20A/B/C/D1-155[»]
1WSHX-ray1.90A/B/C/D1-155[»]
1WSIX-ray2.00A/B/C/D1-155[»]
1WSJX-ray2.00A/B/C/D/E/F/G/H1-155[»]
2RN2X-ray1.48A1-155[»]
2YV0X-ray1.40X1-155[»]
2Z1GX-ray2.10A1-155[»]
2Z1HX-ray2.60A1-155[»]
2Z1IX-ray2.00A/B1-155[»]
2Z1JX-ray2.38A1-155[»]
3AA2X-ray1.90A1-155[»]
3AA3X-ray2.20A1-155[»]
3AA4X-ray1.79A1-155[»]
3AA5X-ray2.10X1-155[»]
3HYFX-ray1.70A79-102[»]
3QINX-ray1.70A79-102[»]
3QIOX-ray1.40A79-102[»]
4Z0UX-ray2.00A/B1-155[»]
ProteinModelPortaliP0A7Y4.
SMRiP0A7Y4. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Y4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 142142RNase HAdd
BLAST

Sequence similaritiesi

Belongs to the RNase H family.Curated
Contains 1 RNase H domain.Curated

Phylogenomic databases

eggNOGiENOG4108UMW. Bacteria.
COG0328. LUCA.
HOGENOMiHOG000040465.
InParanoidiP0A7Y4.
KOiK03469.
OMAiLVTDSQY.
OrthoDBiEOG696BTR.
PhylomeDBiP0A7Y4.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00042. RNase_H.
InterProiIPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7Y4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM
60 70 80 90 100
AAIVALEALK EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN
110 120 130 140 150
VDLWQRLDAA LGQHQIKWEW VKGHAGHPEN ERCDELARAA AMNPTLEDTG

YQVEV
Length:155
Mass (Da):17,597
Last modified:July 21, 1986 - v1
Checksum:iB8EF81EEB2F94CBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00985 Genomic DNA. Translation: AAA24565.1.
V00337 Genomic DNA. Translation: CAA23620.1.
X04027 Genomic DNA. Translation: CAA27660.1.
U70214 Genomic DNA. Translation: AAB08636.1.
U00096 Genomic DNA. Translation: AAC73319.1.
AP009048 Genomic DNA. Translation: BAA77885.1.
PIRiA92401. NRECH.
RefSeqiNP_414750.1. NC_000913.3.
WP_000917883.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73319; AAC73319; b0214.
BAA77885; BAA77885; BAA77885.
GeneIDi946955.
KEGGiecj:JW0204.
eco:b0214.
PATRICi32115541. VBIEscCol129921_0216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00985 Genomic DNA. Translation: AAA24565.1.
V00337 Genomic DNA. Translation: CAA23620.1.
X04027 Genomic DNA. Translation: CAA27660.1.
U70214 Genomic DNA. Translation: AAB08636.1.
U00096 Genomic DNA. Translation: AAC73319.1.
AP009048 Genomic DNA. Translation: BAA77885.1.
PIRiA92401. NRECH.
RefSeqiNP_414750.1. NC_000913.3.
WP_000917883.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F21X-ray1.40A1-155[»]
1G15X-ray1.90A1-155[»]
1GOAX-ray1.90A1-155[»]
1GOBX-ray2.00A1-155[»]
1GOCX-ray2.00A1-155[»]
1JL1X-ray1.30A1-155[»]
1JL2X-ray1.76A/B/C/D1-155[»]
1JXBX-ray1.60A1-155[»]
1KVAX-ray1.80A1-155[»]
1KVBX-ray1.90A1-155[»]
1KVCX-ray1.90A1-155[»]
1LAVX-ray1.80A1-155[»]
1LAWX-ray1.80A1-155[»]
1RBRX-ray1.80A1-155[»]
1RBSX-ray1.80A1-155[»]
1RBTX-ray1.80A1-155[»]
1RBUX-ray1.80A1-155[»]
1RBVX-ray1.80A1-155[»]
1RCHNMR-A1-155[»]
1RDAX-ray2.15A1-155[»]
1RDBX-ray1.90A1-155[»]
1RDCX-ray2.30A1-155[»]
1RDDX-ray2.80A1-155[»]
1RNHX-ray2.00A1-155[»]
1WSEX-ray2.30A/B1-155[»]
1WSFX-ray2.30A/B/C/D1-155[»]
1WSGX-ray2.20A/B/C/D1-155[»]
1WSHX-ray1.90A/B/C/D1-155[»]
1WSIX-ray2.00A/B/C/D1-155[»]
1WSJX-ray2.00A/B/C/D/E/F/G/H1-155[»]
2RN2X-ray1.48A1-155[»]
2YV0X-ray1.40X1-155[»]
2Z1GX-ray2.10A1-155[»]
2Z1HX-ray2.60A1-155[»]
2Z1IX-ray2.00A/B1-155[»]
2Z1JX-ray2.38A1-155[»]
3AA2X-ray1.90A1-155[»]
3AA3X-ray2.20A1-155[»]
3AA4X-ray1.79A1-155[»]
3AA5X-ray2.10X1-155[»]
3HYFX-ray1.70A79-102[»]
3QINX-ray1.70A79-102[»]
3QIOX-ray1.40A79-102[»]
4Z0UX-ray2.00A/B1-155[»]
ProteinModelPortaliP0A7Y4.
SMRiP0A7Y4. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263455. 204 interactions.
DIPiDIP-47864N.
IntActiP0A7Y4. 21 interactions.
MINTiMINT-1224022.
STRINGi511145.b0214.

Chemistry

BindingDBiP0A7Y4.
ChEMBLiCHEMBL1770039.

Proteomic databases

PaxDbiP0A7Y4.
PRIDEiP0A7Y4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73319; AAC73319; b0214.
BAA77885; BAA77885; BAA77885.
GeneIDi946955.
KEGGiecj:JW0204.
eco:b0214.
PATRICi32115541. VBIEscCol129921_0216.

Organism-specific databases

EchoBASEiEB0853.
EcoGeneiEG10860. rnhA.

Phylogenomic databases

eggNOGiENOG4108UMW. Bacteria.
COG0328. LUCA.
HOGENOMiHOG000040465.
InParanoidiP0A7Y4.
KOiK03469.
OMAiLVTDSQY.
OrthoDBiEOG696BTR.
PhylomeDBiP0A7Y4.

Enzyme and pathway databases

BioCyciEcoCyc:EG10860-MONOMER.
ECOL316407:JW0204-MONOMER.
MetaCyc:EG10860-MONOMER.
BRENDAi3.1.26.4. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A7Y4.
PROiP0A7Y4.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
HAMAPiMF_00042. RNase_H.
InterProiIPR022892. RNaseH.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the gene coding for Escherichia coli ribonuclease H."
    Kanaya S., Crouch R.J.
    J. Biol. Chem. 258:1276-1281(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promoter regions."
    Maki H., Horiuchi T., Sekiguchi M.
    Proc. Natl. Acad. Sci. U.S.A. 80:7137-7141(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FB2.
  3. "Low levels of RNase H activity in Escherichia coli FB2 rnh result from a single-base change in the structural gene of RNase H."
    Kanaya S., Crouch R.J.
    J. Bacteriol. 154:1021-1026(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene."
    Cox E.C., Horner D.L.
    J. Mol. Biol. 190:113-117(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification."
    Kanaya S., Kimura S., Katsuda C., Ikehara M.
    Biochem. J. 271:59-66(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF CYSTEINE RESIDUES.
  10. "Identification of the amino acid residues involved in an active site of Escherichia coli ribonuclease H by site-directed mutagenesis."
    Kanaya S., Kohara A., Miura Y., Sekiguchi A., Iwai S., Inoue H., Ohtsuka E., Ikehara M.
    J. Biol. Chem. 265:4615-4621(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-10; GLU-48; ASP-70; HIS-124; ASN-130 AND ASP-134.
  11. "Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition."
    Keck J.L., Goedken E.R., Marqusee S.
    J. Biol. Chem. 273:34128-34133(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, MUTAGENESIS OF HIS-124 AND ASP-134.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  13. "Structure of ribonuclease H phased at 2-A resolution by MAD analysis of the selenomethionyl protein."
    Yang W., Hendrickson W.A., Crouch R.J., Satow Y.
    Science 249:1398-1405(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.
  14. "Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy."
    Yamazaki T., Yoshida M., Kanaya S., Nakamura H., Nagayama K.
    Biochemistry 30:6036-6047(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  15. "Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution."
    Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S., Nakamura H., Ikehara M., Matsuzaki T., Morikawa K.
    J. Mol. Biol. 223:1029-1052(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
  16. "Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability."
    Ishikawa K., Kimura S., Kanaya S., Morikawa K., Nakamura H.
    Protein Eng. 6:85-91(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.
  17. "Crystal structures of ribonuclease HI active site mutants from Escherichia coli."
    Katayanagi K., Ishikawa K., Okumura M., Ariyoshi M., Kanaya S., Kawano Y., Suzuki M., Tanaka I., Morikawa K.
    J. Biol. Chem. 268:22092-22099(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ASN-10; GLN-48 AND ASN-70.
  18. "Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study."
    Yamazaki T., Ogasahara K., Yutani K., Oobatake M., Kanaya S.
    Biochemistry 34:16552-16562(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  19. "Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI."
    Kashiwagi T., Jeanteur D., Haruki M., Katayanagi K., Kanaya S., Morikawa K.
    Protein Eng. 9:857-867(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF HIS-124 AND ASP-134.
  20. "Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI."
    Goedken E.R., Keck J.L., Berger J.M., Marqusee S.
    Protein Sci. 9:1914-1921(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
  21. "Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site."
    Goedken E.R., Marqusee S.
    J. Biol. Chem. 276:7266-7271(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
  22. "Identification of single Mn(2+) binding sites required for activation of the mutant proteins of E.coli RNase HI at Glu48 and/or Asp134 by X-ray crystallography."
    Tsunaka Y., Takano K., Matsumura H., Yamagata Y., Kanaya S.
    J. Mol. Biol. 345:1171-1183(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS ALA-48 AND ASN-134 IN COMPLEX WITH MANGANESE IONS.

Entry informationi

Entry nameiRNH_ECOLI
AccessioniPrimary (citable) accession number: P0A7Y4
Secondary accession number(s): P00647, Q8FKY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.