2FMT,2BLN,2BW0,1FMT


Conserved Protein Domain Family
Met_tRNA_FMT_C

?
cd08704: Met_tRNA_FMT_C 
Click on image for an interactive view with Cn3D
C-terminal domain of Formyltransferase and other enzymes
C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Statistics
?
PSSM-Id: 187732
Aligned: 423 rows
Threshold Bit Score: 49.837
Created: 27-May-2010
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
 
substrate
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:substrate binding site [chemical binding site]
Evidence:
  • Comment:This site describes the binding site for tRNA and formyl-methionine (fMet) at the 3' end of the tRNA.
  • Structure:2FMT_B; Escherichia coli Methionyl-Trnafmet Formyltransferase dimer complexed with two Formyl-Methionyl-tRNAs; contacts at 4A
    View structure with Cn3D
  • Citation:PMID 9843487

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                               #                # #                                     
2FMT_A       210 EEARIDWsLSAAQLERCIRafnpWPMSWLEIeg------qPVKVWKASVIdtatnaapg-----------tileankqGI 272 Escherichia coli
EAY58162     213 NMGKLDFtQTAEQVDRHVRamnpWPGTFCDSpl------gILKFLSGSVWkdesgktetp---------gmiwegpkqEI 277 Leptospirillum ...
Q9RRQ3       211 EDGFVRWaDPAQAVLDRFRgvaaWPQTTAFFgg------kRLKLAGLTLGqgkgqpgk-------------vlqvgagGL 271 Deinococcus rad...
ZP_01452122  223 DERVVDWsQPAASVARVVRcfspQPGARTQAqg------kWLKLIVGSVTdqrstmaa------------gsvagtdgAL 284 Mariprofundus f...
ZP_05912134  204 DDAHLDFtEPAQAIIDRSRgvspSPGPWADVde------kRTKLFGLTPApevtdppev-----------glltswekTA 266 Brevibacterium ...
YP_002760136 208 STAQLDFaAPATQVQRVVRafdpRPGAWGTLrg------gDVKCFSARLVgdgsddaldeptr--ssppgtvrsvdadGM 279 Gemmatimonas au...
A0L3X7       210 EEGLVDWsQPAIQIQRAVQafdpWPCAFTLWqg------kPLKLFAASVVvghgtpge-------------vievekdGF 270 Magnetococcus s...
ZP_04658033  211 ETAQIDWsRTARELDALVRglnpVPYAETHLgd------aLYKIGMLSLTgertdaphg----------tiltadrraGL 274 Selenomonas flu...
YP_003267009 206 DDGAVDWsRSASEVDCHIRamdpWPGAFSAIgd------tRIKLFLSRVApeasvaevgaeagvhapepgqilgvdddGL 279 Haliangium ochr...
ZP_01910184  219 AEGEVDWsTSQRRVIDHIRgmdpWPCAWTKRspdegkaegKAVILKLTGGgasdwsrpega------spgqvlgvddqGM 292 Plesiocystis pa...
Feature 1                       # # ## #  
2FMT_A       273 QVATg-dGILNLLSLQPAgKKAMSA 296 Escherichia coli
EAY58162     278 LVRCg-aGVYCVREIQKAgGKAMSA 301 Leptospirillum sp. Group II UBA
Q9RRQ3       272 TVACg-eGAVCIATVQPEaKKAQPA 295 Deinococcus radiodurans
ZP_01452122  285 DIVCgdgALYRIESLQPEgKKAMSA 309 Mariprofundus ferrooxydans PV-1
ZP_05912134  267 VLGCg-dGWVHVAEIQPFgKARMAA 290 Brevibacterium linens BL2
YP_002760136 280 IVRCg-vGAVRVLDVQPSgKPRMPV 303 Gemmatimonas aurantiaca T-27
A0L3X7       271 VVACg-dGALRVAQVQAAgKKRMSS 294 Magnetococcus sp. MC-1
ZP_04658033  275 RVAAg-dEIVQVTEIQAPgKRMMAA 298 Selenomonas flueggei ATCC 43531
YP_003267009 280 HVACg-rGAVCIAGLQASgGRRISA 303 Haliangium ochraceum DSM 14365
ZP_01910184  293 HVCAg-dGVVRVATVQAPgKRRMAP 316 Plesiocystis pacifica SIR-1

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap