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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Staphylococcus aureus (strain USA300 / TCH1516)
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

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein 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:USA300HOU_1153
OrganismiStaphylococcus aureus (strain USA300 / TCH1516)
Taxonomic identifieri451516 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000773271 – 311Methionyl-tRNA formyltransferaseAdd BLAST311

Structurei

3D structure databases

ProteinModelPortaliA8Z3Q2.
SMRiA8Z3Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni109 – 112Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8Z3Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKIIFMGTP DFSTTVLEML IAEHDVIAVV TQPDRPVGRK RVMTPPPVKK
60 70 80 90 100
VAMKYDLPVY QPEKLSGSEE LEQLLQLDVD LIVTAAFGQL LPESLLALPN
110 120 130 140 150
LGAINVHASL LPKYRGGAPI HQAIIDGEQE TGITIMYMVK KLDAGNIISQ
160 170 180 190 200
QAIKIEENDN VGTMHDKLSV LGADLLKETL PSIIEGTNES VPQDDTQATF
210 220 230 240 250
ASNIRREDER ISWNKPGRQV FNQIRGLSPW PVAYTTMDDT NLKIYDAELV
260 270 280 290 300
ETNKINEPGT IIETTKKAII VATNDNEAVA IKDMQLAGKK RMLAANYLSG
310
AQNTLVGKKL I
Length:311
Mass (Da):34,211
Last modified:January 15, 2008 - v1
Checksum:iFC45A768EA61D5CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000730 Genomic DNA. Translation: ABX29168.1.
RefSeqiWP_000161299.1. NC_010079.1.

Genome annotation databases

EnsemblBacteriaiABX29168; ABX29168; USA300HOU_1153.
GeneIDi28381227.
KEGGisax:USA300HOU_1153.
PATRICi19597410. VBIStaAur36919_1224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000730 Genomic DNA. Translation: ABX29168.1.
RefSeqiWP_000161299.1. NC_010079.1.

3D structure databases

ProteinModelPortaliA8Z3Q2.
SMRiA8Z3Q2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX29168; ABX29168; USA300HOU_1153.
GeneIDi28381227.
KEGGisax:USA300HOU_1153.
PATRICi19597410. VBIStaAur36919_1224.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_STAAT
AccessioniPrimary (citable) accession number: A8Z3Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: November 2, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.