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C0ZRD0 (C0ZRD0_RHOE4) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 31. 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 length311 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP By similarity. SAAS SAAS015518

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

Ontologies

Keywords
   Biological processProtein biosynthesis SAAS SAAS015518
   Molecular functionTransferase SAAS SAAS015518 EMBL BAH31680.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhydroxymethyl-, formyl- and related transferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
C0ZRD0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: AAFB5A9CFDB95DB7

FASTA31134,484
        10         20         30         40         50         60 
MRVATLGYQT WGHRTLQALI DSDHEVVLAI THPKSEHVYE QMWADSVADL AAENGVPVHV 

        70         80         90        100        110        120 
ANKPDDAFKA ALAEAAPDII VANNWRTWLP AEVFDAPKYG TLNIHDSLLP KYTGFSPLIW 

       130        140        150        160        170        180 
ALINGEEEVG LTAHLMDEEL DAGDIVLQRS TTVGPTDTVT DLFHRTIDMI GPITLDALDL 

       190        200        210        220        230        240 
IASGRTDWTP QDRSQATFFH KRAPQDSHVD WSWPAEVIER FVRAQSDPYP NAFAEFKGRR 

       250        260        270        280        290        300 
IRILKASVSR GHYGGTPGRV FIQEDDGMVI VAGPDAWSGK NKGLRIERVR LDDGSEYTAA 

       310 
EFFPHGGGYL T 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH31680.1.
RefSeqYP_002764419.1. NC_012490.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_09720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH31680; BAH31680; RER_09720.
GeneID7712883.
KEGGrer:RER_09720.
PATRIC23188250. VBIRhoEry66701_1428.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAFTGFSPV.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycRERY234621:GHDE-989-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
InterProIPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC0ZRD0_RHOE4
AccessionPrimary (citable) accession number: C0ZRD0
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)