1FMT,1F4R,2FMT


Conserved Protein Domain Family
FMT_C_like

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cd08370: FMT_C_like 
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Carboxy-terminal domain of Formyltransferase and similar domains
This family represents the C-terminal domain of formyltransferase and similar proteins. This domain is found in a variety of enzymes with formyl transferase and alkyladenine DNA glycosylase activities. The proteins with formyltransferase function include methionyl-tRNA formyltransferase, ArnA, 10-formyltetrahydrofolate dehydrogenase and HypX proteins. Although most proteins with formyl transferase activity contain this C-terminal domain, prokaryotic glycinamide ribonucleotide transformylase (GART), a single domain protein, only contains the core catalytic domain. Thus, the C-terminal domain is not required for formyl transferase catalytic activity and may be involved in substrate binding. Some members of this family have shown nucleic acid binding capacity. The C-terminal domain of methionyl-tRNA formyltransferase is involved in tRNA binding. Alkyladenine DNA glycosylase is a distant member of this family with very low sequence similarity to other members. It catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site and shows ability to bind to DNA.
Statistics
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PSSM-Id: 187727
Aligned: 10 rows
Threshold Bit Score: 53.1931
Created: 18-Nov-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
1FMT_A        218 LSAAQLERCIrafn-pwpMSWLEIeg-----qPVKVWKASVIdtatnaapg----------------------tileank 269  Escherichia coli
1F4R_A         14 QPAVPLARAFl-------GQVLVRrlpngtelRGRIVETEAYlgpedeaahsrggrqtprnrgmfmkpgtlyvyiiygmy 86   human
2FMT_A        218 LSAAQLERCIrafn-pwpMSWLEIeg-----qPVKVWKASVIdtatnaapg----------------------tileank 269  Escherichia coli
ZP_01035523   201 QTAESLARLVral---dhGGYANPl------nRTRIIAGDRVllvgraevvpgs---------------gapgvvlsvda 256  Roseovarius s...
YP_002429809  228 KDLELFINAFddp---yaGASTELdg-----rLVRLKQARVEtldgp-----------------------------fhpf 270  Desulfatibaci...
YP_002532617  225 LDTESILRTIrag--ypqGAFAFNqy----neKIRILHAERTdypq--------------------------------qi 266  Bacillus cere...
YP_001520946  186 DTTAEIVRKIrsa--dsqPGLLDVlf----geQFYLYGAHPEntltgkpg-----------------------eliaqry 236  Acaryochloris...
ZP_02190621   199 RSAETICRTIdalsypfmGARTRIdg-----rEVIVDEARIVddlvferrdi--------------------gkiwsldp 253  alpha proteob...
ZP_01733753   208 LDALVLERTInalgfpygGARSKMdd-----kIIILDEVKALndvkienrts--------------------gkilfldn 262  Flavobacteria...
ZP_04922888   204 QSSAYIKRFIdsvgypysGAITNVde-----nKVVVLDAEVVqdvvcehrhv--------------------gkvifven 258  Vibrio sp. Ex25
1FMT_A        270 qGIQVATg--dGILNLLSLQPA 289  Escherichia coli
1F4R_A         87 fCMNISSqgdgACVLLRALEPL 108  human
2FMT_A        270 qGIQVATg--dGILNLLSLQPA 289  Escherichia coli
ZP_01035523   257 tRLTVATa--aGALRLSALTGP 276  Roseovarius sp. 217
YP_002429809  271 mTGLVYRin-sTGVYIATPQGS 291  Desulfatibacillum alkenivorans AK-01
YP_002532617  267 qSIGIFReh-nDKILVSTKDGW 287  Bacillus cereus Q1
YP_001520946  237 gAICRATi--dGAVWITHLKRK 256  Acaryochloris marina MBIC11017
ZP_02190621   254 dGPIVVCg--rGCLRVTAAHST 273  alpha proteobacterium BAL199
ZP_01733753   263 nQPTIVCg--nGLIKIEKAHYL 282  Flavobacteria bacterium BAL38
ZP_04922888   259 gCPVVICg--kGLLKITKAVVK 278  Vibrio sp. Ex25
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