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D5VP75 (D5VP75_CAUST) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. 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 length308 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. HAMAP-Rule MF_00182 SAAS SAAS005794

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182 SAAS SAAS005794

Sequence similarities

Belongs to the fmt family. HAMAP-Rule MF_00182

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region109 – 1124Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
D5VP75 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 4803CA0FC99DF3F0

FASTA30832,638
        10         20         30         40         50         60 
MRIAFLGTPD FAVTCLAELV ASGHEIVAVY SQPPAPRGRG QELKPSPVHA FAEGLGLPVR 

        70         80         90        100        110        120 
TPVSMKTPEE IEAFKALDLD AAVVVAFGQI LVKDVLEAPR HGCFNLHASL LPRWRGAAPI 

       130        140        150        160        170        180 
QRAIMAGDPV TGVQVMRMSE GLDEGPILMS EQVAIAADDT AATLHDKLAT VGARLLPVAL 

       190        200        210        220        230        240 
AAIEREVVRE TPQSEDGVTY AKKIKSAEAR IDWTRPAAEV DRHIRGLSPF PGAWFEAPSE 

       250        260        270        280        290        300 
KGPVRVKALL SRVEAASGVA GTALDDALLI ACGEASIRLL KAQREGKGVQ DAETFTRGFP 


IPAGTVLA 

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References

[1]"Genome sequences of eight morphologically diverse alphaproteobacteria."
US DOE Joint Genome Institute
Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.
J. Bacteriol. 193:4567-4568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / TK0059.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002008 Genomic DNA. Translation: ADG12298.1.
RefSeqYP_003594916.1. NC_014100.1.

3D structure databases

ProteinModelPortalD5VP75.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG12298; ADG12298; Cseg_3878.
GeneID9105404.
KEGGcse:Cseg_3878.
PATRIC37207954. VBICauSeg118057_3957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.

Enzyme and pathway databases

BioCycCSEG509190:GHVG-3931-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. 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. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD5VP75_CAUST
AccessionPrimary (citable) accession number: D5VP75
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)