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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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

Enzyme and pathway databases

BioCyciCBUR227377:GJ7S-1970-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:CBU_1997
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000002671 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Methionyl-tRNA formyltransferasePRO_0000082955Add
BLAST

Proteomic databases

PRIDEiQ83AA8.

Interactioni

Protein-protein interaction databases

STRINGi227377.CBU_1997.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi24 – 329Combined sources
Helixi49 – 568Combined sources
Beta strandi67 – 693Combined sources
Helixi70 – 778Combined sources
Beta strandi82 – 887Combined sources
Helixi95 – 984Combined sources
Beta strandi105 – 1117Combined sources
Turni113 – 1164Combined sources
Beta strandi117 – 1193Combined sources
Helixi121 – 1288Combined sources
Beta strandi131 – 1399Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi149 – 1568Combined sources
Helixi163 – 18725Combined sources
Helixi197 – 1993Combined sources
Helixi208 – 2114Combined sources
Helixi219 – 22810Combined sources
Turni229 – 2335Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi242 – 25211Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi276 – 28611Combined sources
Helixi295 – 3028Combined sources
Helixi303 – 3053Combined sources
Turni308 – 3103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TQQX-ray2.00A1-314[»]
ProteinModelPortaliQ83AA8.
SMRiQ83AA8. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1144Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiDTGAMIS.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERiPTHR11138. PTHR11138. 1 hit.
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.

Q83AA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKIVFAGT PQFAVPTLRA LIDSSHRVLA VYTQPDRPSG RGQKIMESPV
60 70 80 90 100
KEIARQNEIP IIQPFSLRDE VEQEKLIAMN ADVMVVVAYG LILPKKALNA
110 120 130 140 150
FRLGCVNVHA SLLPRWRGAA PIQRAILAGD RETGISIMQM NEGLDTGDVL
160 170 180 190 200
AKSACVISSE DTAADLHDRL SLIGADLLLE SLAKLEKGDI KLEKQDEASA
210 220 230 240 250
TYASKIQKQE ALIDWRKSAV EIARQVRAFN PTPIAFTYFE GQPMRIWRAT
260 270 280 290 300
VVDEKTDFEP GVLVDADKKG ISIAAGSGIL RLHQLQLPGK RVCSAGDFIN
310
AHGDKLIPGK TVFG
Length:314
Mass (Da):34,288
Last modified:June 1, 2003 - v1
Checksum:i11A4B3CCB9ED0AD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91486.1.
RefSeqiNP_820972.1. NC_002971.3.
WP_010958586.1. NZ_CCYB01000066.1.

Genome annotation databases

EnsemblBacteriaiAAO91486; AAO91486; CBU_1997.
GeneIDi1209910.
KEGGicbu:CBU_1997.
PATRICi17932735. VBICoxBur82552_1984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91486.1.
RefSeqiNP_820972.1. NC_002971.3.
WP_010958586.1. NZ_CCYB01000066.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TQQX-ray2.00A1-314[»]
ProteinModelPortaliQ83AA8.
SMRiQ83AA8. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_1997.

Proteomic databases

PRIDEiQ83AA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91486; AAO91486; CBU_1997.
GeneIDi1209910.
KEGGicbu:CBU_1997.
PATRICi17932735. VBICoxBur82552_1984.

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiDTGAMIS.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciCBUR227377:GJ7S-1970-MONOMER.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERiPTHR11138. PTHR11138. 1 hit.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RSA 493 / Nine Mile phase I.

Entry informationi

Entry nameiFMT_COXBU
AccessioniPrimary (citable) accession number: Q83AA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.