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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Haemophilus somnus (strain 129Pt) (Histophilus somni)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Biological processProtein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:HS_0040
OrganismiHaemophilus somnus (strain 129Pt) (Histophilus somni)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000001970 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000200751 – 317Methionyl-tRNA formyltransferaseAdd BLAST317

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_0040.

Structurei

3D structure databases

ProteinModelPortaliQ0I182.
SMRiQ0I182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 115Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.
OrthoDBiPOG091H01YM.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiView protein in PROSITE
PS00373. GART. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0I182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPLNIIFAG TPDFAAQHLQ ALLQSQHNVL AVYTQPDKPA GRGQTLRASA
60 70 80 90 100
VKILAEKHHI PVYQPKSLRK VEVQENLSKL NADVMVVVAY GLILPLAVLQ
110 120 130 140 150
TFPLGCLNVH GSLLPRWRGA APIQRAIWAG DKKTGVTIMQ MNEGLDTGDM
160 170 180 190 200
LHKVCCDITP TETSTSLYTK LANIAPKALL EVLDGLEQSL FKAEVQDESL
210 220 230 240 250
SNYAEKLSKE EAKLDWSLSA EQLERCIRAF NPWPMSYFVT QDSQGTLQTL
260 270 280 290 300
KVYQASVLPH QDKPCGTILA ADKRGIQVAT ANGVLNLEQL QPAGKKPMSA
310
RDLLNSRADW FKIGQVL
Length:317
Mass (Da):34,886
Last modified:October 3, 2006 - v1
Checksum:i296CAEC0C7A88FB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI24321.1.
RefSeqiWP_011608199.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI24321; ABI24321; HS_0040.
KEGGihso:HS_0040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI24321.1.
RefSeqiWP_011608199.1. NC_008309.1.

3D structure databases

ProteinModelPortaliQ0I182.
SMRiQ0I182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205914.HS_0040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI24321; ABI24321; HS_0040.
KEGGihso:HS_0040.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.
OrthoDBiPOG091H01YM.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiView protein in PROSITE
PS00373. GART. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_HAES1
AccessioniPrimary (citable) accession number: Q0I182
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: June 7, 2017
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.