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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Anaplasma marginale (strain St. Maries)
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:AM313
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Methionyl-tRNA formyltransferasePRO_0000082906Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi234826.AM313.

Structurei

3D structure databases

ProteinModelPortaliQ5PBC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1124Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiWAEEPIN.
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.
[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.

Sequencei

Sequence statusi: Complete.

Q5PBC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVIFMGSSE FSVPTLEFLI GSQHEVLAVY TKAPKPAGRG HLLTKTPVHA
60 70 80 90 100
YADAHNVPVR SPASLSSDSE RDIIEKYMPD AIIVASYGMI LPRWMLEVPR
110 120 130 140 150
FGCINVHPSL LPRWRGAAPM QHAILSGDAV TGVTIMQLNE RLDAGDIFLQ
160 170 180 190 200
ESTPIGSREN IVALSERLSS MGGRMLLKVL DNLDTMRSVS QDDAGATYAA
210 220 230 240 250
KPSEFCVNFN DAADYICRQV RAFYPRMFFF LDGKRVKLLE ADNYELAGAQ
260 270 280 290 300
IGDVVNDELH IQCGNGTVLA PKIVQPESKK PCDIRSFLRG FRGCVSNVLQ

R
Length:301
Mass (Da):33,230
Last modified:January 4, 2005 - v1
Checksum:iCDC2A754D91976DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000030 Genomic DNA. Translation: AAV86402.1.
RefSeqiWP_010263215.1. NZ_AFMU01000046.1.

Genome annotation databases

EnsemblBacteriaiAAV86402; AAV86402; AM313.
GeneIDi7398237.
KEGGiama:AM313.
PATRICi20946677. VBIAnaMar46146_0267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000030 Genomic DNA. Translation: AAV86402.1.
RefSeqiWP_010263215.1. NZ_AFMU01000046.1.

3D structure databases

ProteinModelPortaliQ5PBC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi234826.AM313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV86402; AAV86402; AM313.
GeneIDi7398237.
KEGGiama:AM313.
PATRICi20946677. VBIAnaMar46146_0267.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiWAEEPIN.
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.
[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.
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
    Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: St. Maries.

Entry informationi

Entry nameiFMT_ANAMM
AccessioniPrimary (citable) accession number: Q5PBC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 4, 2005
Last modified: March 16, 2016
This is version 69 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.