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Q1MQA7 (Q1MQA7_LAWIP) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00182 SAAS SAAS005794

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182 SAAS SAAS005794

Sequence similarities

Belongs to the fmt family. HAMAP-Rule MF_00182

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region117 – 1204Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
Q1MQA7 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: E9DB9BE81986FC4B

FASTA32235,502
        10         20         30         40         50         60 
MILQNKPLRI VFMGTPEFAA IILQKIVASG KVDIIASYCQ PDRPVGRGHK VQFSAVKILS 

        70         80         90        100        110        120 
NSLRIPVYQP VNFKSEYEIE KLYALKPDLL VVAAYGLILP QSVLDIPAIS PLNVHASLLP 

       130        140        150        160        170        180 
CYRGAAPIQR ALMNNDKKTG VTIIRMEKGL DTGAMFTHEE IPINMEDTAA TMHEKLAQLG 

       190        200        210        220        230        240 
GKLLINIFEQ IIQGTLSDPT PQDDIQATYA PKLTKSDGCI YWDMPAENVH AVVRGVTPWP 

       250        260        270        280        290        300 
GAQTSFKLVN RNPINILFQP GEIGSNELFK YNEGDSPLPG SILGLKGNAI AIACKDVPYL 

       310        320 
IYTLRPEGRK TMTAKDFWNG YL

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References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00 EMBL CAJ54820.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180252 Genomic DNA. Translation: CAJ54820.1.
RefSeqYP_595141.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MQA7.
ModBaseSearch...

Protein-protein interaction databases

STRING363253.LI0766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4059748.
KEGGlip:LI0766.
PATRIC22305013. VBILawInt40445_0833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMADWNKSAR.
ProtClustDBCLSK706351.

Enzyme and pathway databases

BioCycLINT363253:GH6E-922-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ1MQA7_LAWIP
AccessionPrimary (citable) accession number: Q1MQA7
Entry history
Integrated into UniProtKB/TrEMBL: May 30, 2006
Last sequence update: May 30, 2006
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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