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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Sphaerobacter thermophilus (strain DSM 20745 / S 6022)
Status
Unreviewed-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
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).SAAS annotation

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotation

Keywords - Biological processi

Protein biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciSTHE479434:GHJN-1202-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotationSAAS annotation (EC:2.1.2.9UniRule annotationSAAS annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:Sthe_1176Imported
OrganismiSphaerobacter thermophilus (strain DSM 20745 / S 6022)Imported
Taxonomic identifieri479434 [NCBI]
Taxonomic lineageiBacteriaChloroflexiSphaerobacteridaeSphaerobacteralesSphaerobacterineaeSphaerobacteraceaeSphaerobacter
ProteomesiUP000002027 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 PotentialImportedAdd
BLAST
Chaini24 – 314291 PotentialImportedPRO_5000537677Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi479434.Sthe_1176.

Structurei

3D structure databases

ProteinModelPortaliD1C2Z5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1154Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Keywords - Domaini

SignalImported

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiKVWQSRV.
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.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D1C2Z5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISVVFLGS PAFAVPSLRA LALDARFTIP LVVTQPDRPA GRGRRPRPPA
60 70 80 90 100
VKDAAIELGL PVFQPETLRD PAAVERLAAA VPDVLVVVAY GEILRQSVLD
110 120 130 140 150
LAPLGCLNVH PSLLPRYRGS SPVQAAILNG DTETGISIIK LVRRMDAGPI
160 170 180 190 200
VAQRRVPLDG TETAGTLSER LANLAAEMLP DVVAAWVAGE LEAEPQDDAA
210 220 230 240 250
ATYTRELTTA DARIDWGKDA AEIERLVRAM QPWPKAWSIL EGRRLAVLAC
260 270 280 290 300
DISHKPSTEP PGTINVSARP PRVATGTTDL VLLRVQPEGK REMAAEDWAR
310
GARLPHGARF APVE
Length:314
Mass (Da):33,662
Last modified:January 19, 2010 - v1
Checksum:i3BBACF9AA3D417ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001823 Genomic DNA. Translation: ACZ38612.1.
RefSeqiWP_012871659.1. NC_013523.1.
YP_003319434.1. NC_013523.1.

Genome annotation databases

EnsemblBacteriaiACZ38612; ACZ38612; Sthe_1176.
KEGGisti:Sthe_1176.
PATRICi32425101. VBISphThe120955_1190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001823 Genomic DNA. Translation: ACZ38612.1.
RefSeqiWP_012871659.1. NC_013523.1.
YP_003319434.1. NC_013523.1.

3D structure databases

ProteinModelPortaliD1C2Z5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi479434.Sthe_1176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACZ38612; ACZ38612; Sthe_1176.
KEGGisti:Sthe_1176.
PATRICi32425101. VBISphThe120955_1190.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiKVWQSRV.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciSTHE479434:GHJN-1202-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.
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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 20745 / S 6022Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 20745 / S 6022Imported.

Entry informationi

Entry nameiD1C2Z5_SPHTD
AccessioniPrimary (citable) accession number: D1C2Z5
Entry historyi
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: June 24, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.