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B1Y0J9 (B1Y0J9_LEPCP) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates By similarity. HAMAP-Rule MF_00564 SAAS SAAS002381

Catalytic activity

tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate. HAMAP-Rule MF_00564 SAAS SAAS002381

Sequence similarities

Belongs to the RNase PH family. HAMAP-Rule MF_00564

Sequences

Sequence LengthMass (Da)Tools
B1Y0J9 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: C060C982C26AA38A

FASTA24125,268
        10         20         30         40         50         60 
MSSTRPLGRA ADALRPVRIT RSYTKHAEGS VLIEFGDTQV LCTASVEEKV PPHKKGSGEG 

        70         80         90        100        110        120 
WVTAEYGMLP RATHTRSARE AAKGKQSGRT QEIQRLIGRS LRCVFDLAAL GERSILIDCD 

       130        140        150        160        170        180 
VLQADGGTRT ASITGAFVAA HDAVQGLIAQ GKLKRSPIRD FVAAVSVGIL DGVALLDLEY 

       190        200        210        220        230        240 
VEDSACDTDM NIVMTGAGGF VEVQGTAEGV AFSRAEMDQL LALGSAGIAE LVAAQKAALG 


V 

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References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB32980.1.
RefSeqYP_001789745.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y0J9.
SMRB1Y0J9. Positions 5-240.
ModBaseSearch...

Protein-protein interaction databases

STRING395495.Lcho_0705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB32980; ACB32980; Lcho_0705.
GeneID6163753.
KEGGlch:Lcho_0705.
PATRIC22391689. VBILepCho83238_0706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0689.
HOGENOMHOG000229516.
KOK00989.
OMAMLPRATG.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-714-MONOMER.

Family and domain databases

HAMAPMF_00564. RNase_PH.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR002381. RNase_PH_bac-type.
IPR018336. RNase_PH_CS.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF55666. 3_ExoRNase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR01966. RNasePH. 1 hit.
PROSITEPS01277. RIBONUCLEASE_PH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB1Y0J9_LEPCP
AccessionPrimary (citable) accession number: B1Y0J9
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)