NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499342857|ref|WP_011032396|]
View 

MULTISPECIES: phosphoribosylglycinamide formyltransferase [Methanosarcina]

Protein Classification

phosphoribosylglycinamide formyltransferase( domain architecture ID 10001018)

phosphoribosylglycinamide formyltransferase catalyzes the transfer of a formyl group from lO-formyltetrahydrofolate to glycinamide ribonucleotide

CATH:  3.40.50.170
EC:  2.1.2.2
Gene Symbol:  purN
Gene Ontology:  GO:0006974|GO:0004644|GO:0006189
SCOP:  4000065

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-199 3.17e-116

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 328.53  E-value: 3.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGISAVFLDSRG-RDRAEYDREILKVLRQYDT 82
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDfPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499342857 163 TEETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVT 199
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVR 198
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-199 3.17e-116

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 328.53  E-value: 3.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGISAVFLDSRG-RDRAEYDREILKVLRQYDT 82
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDfPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499342857 163 TEETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVT 199
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVR 198
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-186 1.51e-106

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 303.54  E-value: 1.51e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGISAVFLDSRG-RDRAEYDREILKVLRQYDT 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKL-NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDfPSREEFDEALLELLKEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:cd08645   80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                        170       180
                 ....*....|....*....|....
gi 499342857 163 TEETLTDRILEQEHIIYPEAVRLF 186
Cdd:cd08645  160 TPETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-192 2.36e-87

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 255.37  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857    4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGI-SAVFLDSRGRDRAEYDREILKVLRQYDT 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKI-PASVVLVISNKPDAYGLERAAQAGIpTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 499342857  163 TEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 2.19e-70

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 211.77  E-value: 2.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857    3 VKIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGI-SAVFLDSRGRDRAEYDREILKVLRQYD 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQ-DADVVLVISNKDKAAGLGRAEQAGIpTFVFEHKGLTPRSLFDQELADALRALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   82 TDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPG 161
Cdd:pfam00551  80 ADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPD 159

                         170       180
                  ....*....|....*....|..
gi 499342857  162 DTEETLTDRILEQEHIIYPEAV 183
Cdd:pfam00551 160 DTAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-192 2.42e-56

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 177.19  E-value: 2.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGIS-AVFLDSRGRDRAEYDREILKVLRQYDT 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRV-NGDVVVVVTNKPGCGGAEYARENGIPvLVYPKTKGEPDGLSPDELVDALRGAGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAF--KGLHA---QKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVP 157
Cdd:PLN02331  80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGikvHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499342857 158 VLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
 
Name Accession Description Interval E-value
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 4-199 3.17e-116

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 328.53  E-value: 3.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGISAVFLDSRG-RDRAEYDREILKVLRQYDT 82
Cdd:COG0299    3 RIAVLISGRGSNLQALIDAIEAGDL-PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDfPSREAFDAALLEALDAYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:COG0299   82 DLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 499342857 163 TEETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVT 199
Cdd:COG0299  162 TEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVR 198
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 4-186 1.51e-106

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 303.54  E-value: 1.51e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGISAVFLDSRG-RDRAEYDREILKVLRQYDT 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKL-NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDfPSREEFDEALLELLKEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:cd08645   80 DLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGD 159

                        170       180
                 ....*....|....*....|....
gi 499342857 163 TEETLTDRILEQEHIIYPEAVRLF 186
Cdd:cd08645  160 TPETLAERIHALEHRLYPEAIKLL 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 4-192 2.36e-87

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 255.37  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857    4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGI-SAVFLDSRGRDRAEYDREILKVLRQYDT 82
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKI-PASVVLVISNKPDAYGLERAAQAGIpTFVLSLKDFPSREAFDQAIIEELRAHEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGD 162
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPED 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 499342857  163 TEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:TIGR00639 161 TEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 3-183 2.19e-70

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 211.77  E-value: 2.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857    3 VKIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGI-SAVFLDSRGRDRAEYDREILKVLRQYD 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQ-DADVVLVISNKDKAAGLGRAEQAGIpTFVFEHKGLTPRSLFDQELADALRALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   82 TDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPG 161
Cdd:pfam00551  80 ADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPD 159

                         170       180
                  ....*....|....*....|..
gi 499342857  162 DTEETLTDRILEQEHIIYPEAV 183
Cdd:pfam00551 160 DTAETLYNRVADLEHKALPRVL 181
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 4-192 2.42e-56

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 177.19  E-value: 2.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALERAKNHGIS-AVFLDSRGRDRAEYDREILKVLRQYDT 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRV-NGDVVVVVTNKPGCGGAEYARENGIPvLVYPKTKGEPDGLSPDELVDALRGAGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  83 DLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAF--KGLHA---QKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVP 157
Cdd:PLN02331  80 DFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFggKGYYGikvHKAVIASGARYSGPTVHFVDEHYDTGRILAQRVVP 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499342857 158 VLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:PLN02331 160 VLATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
 4-196 1.74e-41

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 141.34  E-value: 1.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTD 83
Cdd:COG0788   88 RVAILVSKEDHCLNDLLYRWRSGEL-PAEIPAVISNHPDLRPL--AEWFGIPFHHIPVTKETKAEAEARLLELLEEYDID 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  84 LLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDT 163
Cdd:COG0788  165 LVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVERVDHRDT 244

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499342857 164 EETLTD--RILEQehIIYPEAVRLFVEGKLKVEGR 196
Cdd:COG0788  245 PEDLVRkgRDVEK--RVLARAVRWHLEDRVLVNGN 277
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-185 2.22e-39

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 132.80  E-value: 2.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   7 VLVSGRGSNLQAIIDSIEKgyIKNAAVNVVISNKADAYALERAKNHGISAVFLdsrgRDRAEYDREILKVLRQYDTDLLL 86
Cdd:cd08369    1 IVILGSGNIGQRVLKALLS--KEGHEIVGVVTHPDSPRGTAQLSLELVGGKVY----LDSNINTPELLELLKEFAPDLIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  87 LAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEET 166
Cdd:cd08369   75 SINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGT 154

                        170
                 ....*....|....*....
gi 499342857 167 LTDRILEQEHIIYPEAVRL 185
Cdd:cd08369  155 LYQRLIELGPKLLKEALQK 173
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 4-199 2.76e-39

Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.


Pssm-ID: 187717 [Multi-domain]  Cd Length: 196  Bit Score: 133.07  E-value: 2.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTD 83
Cdd:cd08648    2 RVAIFVSKEDHCLYDLLHRWREGEL-PCEIPLVISNHPDLRPL--AERFGIPFHHIPVTKDTKAEAEAEQLELLEEYGVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  84 LLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDT 163
Cdd:cd08648   79 LVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSHRDS 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499342857 164 EETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVT 199
Cdd:cd08648  159 VEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNKTV 194
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
 4-198 4.62e-34

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 122.15  E-value: 4.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857    4 KIAVLVSGRGSNLQAIIDSIEKGYIkNAAVNVVISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTD 83
Cdd:TIGR00655  86 RVAILVSKEDHCLGDLLWRWYSGEL-DAEIALVISNHEDLRSL--VERFGIPFHYIPATKDNRVEHEKRQLELLKQYQVD 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   84 LLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDT 163
Cdd:TIGR00655 163 LVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVDHTDN 242

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 499342857  164 EETLTDRILEQEHIIYPEAVRLFVEGKLKV-EGRNV 198
Cdd:TIGR00655 243 VEDLIRAGRDIEKVVLARAVKLHLEDRVFVyENKTV 278
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
 36-168 4.62e-32

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 117.13  E-value: 4.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  36 VISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLP 115
Cdd:PRK06027 122 VISNHDDLRSL--VERFGIPFHHVPVTKETKAEAEARLLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLP 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499342857 116 AFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLT 168
Cdd:PRK06027 200 AFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDHRDTAEDLV 252
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 36-190 6.62e-30

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 111.23  E-value: 6.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  36 VISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLP 115
Cdd:PRK13011 122 VVSNHPDLEPL--AAWHGIPFHHFPITPDTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLP 199

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499342857 116 AFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQEHIIYPEAVRLFVEGK 190
Cdd:PRK13011 200 GFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVDHAYSPEDLVAKGRDVECLTLARAVKAHIERR 274
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 4-199 3.36e-27

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 104.06  E-value: 3.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   4 KIAVLVSGRGSNLQAIIDSIEKGYIKnAAVNVVISNK---ADAYALERAKNHGISAVFL-DSRGRDRAEydrEILKVLRq 79
Cdd:PLN02828  72 KIAVLASKQDHCLIDLLHRWQDGRLP-VDITCVISNHergPNTHVMRFLERHGIPYHYLpTTKENKRED---EILELVK- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  80 yDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVL 159
Cdd:PLN02828 147 -GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVS 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499342857 160 PGDTEETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVT 199
Cdd:PLN02828 226 HRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGTNKT 265
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 36-195 3.81e-27

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 104.11  E-value: 3.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  36 VISNKADAYALerAKNHGISAVFLDSRGRDRAEYDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLP 115
Cdd:PRK13010 126 IISNHPDLQPL--AVQHDIPFHHLPVTPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLP 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857 116 AFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLKVEG 195
Cdd:PRK13010 204 GFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRVFING 283
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
47-192 5.56e-23

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 93.25  E-value: 5.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  47 ERAKNHGIsAVFLDSRGRDRaeydrEILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKG---LHaq 123
Cdd:COG0223   50 ELALEHGI-PVLQPESLKDP-----EFLEELRALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGaapIQ-- 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499342857 124 kQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:COG0223  122 -WAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLT 189
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 47-170 3.48e-20

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 84.03  E-value: 3.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  47 ERAKNHGISaVFLDSRGRDRaeydrEILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKG---LHAq 123
Cdd:cd08646   50 ELALELGLP-VLQPEKLKDE-----EFLEELKALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGaapIQR- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499342857 124 kqAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDR 170
Cdd:cd08646  123 --AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDK 167
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 37-190 9.71e-19

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 80.19  E-value: 9.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  37 ISNKADAYALERAKNhGISaVFLDSRGRDRAEYDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPA 116
Cdd:cd08647   35 KDGKADPLALEAEKD-GVP-VFKFPRWRAKGQAIPEVVAKYKALGAELNVLPFCSQFIPMEVIDAPKHGSIIYHPSILPR 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499342857 117 FKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQEHI-IYPEAVRLFVEGK 190
Cdd:cd08647  113 HRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRFLYPEGIkAMVEAVRLIAEGK 187
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 70-184 1.24e-18

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 78.41  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  70 DREILKVLRQYDTDLLLLAGYfRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAF-EYGVKVAGCTVHFVDEGLDSG 148
Cdd:cd08653   36 GPEVVAALRALAPDVVSVYGC-GIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALaNGDPDNVGVTVHLVDAGIDTG 114

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499342857 149 PIIIQRCVPVLPGDTEETLTDRILEQEHIIYPEAVR 184
Cdd:cd08653  115 DVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAIA 150
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 72-201 1.18e-17

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 78.98  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857   72 EILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPII 151
Cdd:TIGR00460  69 EELPLVRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDIL 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499342857  152 IQRCVPVLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLKVEGRNVTAP 201
Cdd:TIGR00460 149 KQETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEA 198
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 38-173 1.65e-16

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 73.84  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  38 SNKADAYALERAKNHGISAVFLDSRGrdraeyDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAF 117
Cdd:cd08651   38 NDSDYLDLDSFARKNGIPYYKFTDIN------DEEIIEWIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKN 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499342857 118 KGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILE 173
Cdd:cd08651  112 RGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIME 167
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 34-174 5.15e-14

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 68.95  E-value: 5.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  34 NVVISNKADAYALERaknhGI--SAVFLDSRGRDRaeydrEILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHP 111
Cdd:PLN02285  53 RKLMPSPVAQLALDR----GFppDLIFTPEKAGEE-----DFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHP 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499342857 112 SLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQ 174
Cdd:PLN02285 124 SLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFEL 186
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 81-188 5.90e-14

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 67.10  E-value: 5.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  81 DTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLP 160
Cdd:cd08822   66 GTDLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRP 145

                         90       100
                 ....*....|....*....|....*...
gi 499342857 161 GDTEETLTDRILeqehiiYPEAVRLFVE 188
Cdd:cd08822  146 GDTAAELWRRAL------APMGVKLLTQ 167
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 77-171 8.74e-12

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 60.92  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  77 LRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCV 156
Cdd:cd08823   67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146

                         90
                 ....*....|....*
gi 499342857 157 PVLPGDTEETLTDRI 171
Cdd:cd08823  147 PIHPDDTYGLLCSRL 161
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 47-192 4.11e-10

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 56.97  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  47 ERAKNHGISaVFLDSRGRDRaeydrEILKVLRQYDTDLLLlAGYFR-LLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQ 125
Cdd:cd08644   47 QLAREHGIP-VFTPDDINHP-----EWVERLRALKPDLIF-SFYYRhMISEDILEIARLGAFNLHGSLLPKYRGRAPLNW 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499342857 126 AFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQEHIIYPEAVRLFVEGKLK 192
Cdd:cd08644  120 ALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRLLARTLPALKAGKAR 186
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 54-188 4.21e-10

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 56.30  E-value: 4.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  54 ISAVFLDSRGRDRAEYDREI-------------LKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFKGL 120
Cdd:cd08820   29 IIAVLTNTSPADVWEGSEPLydigsternlhklLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGC 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499342857 121 HAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDrileqehIIYPEAVRLFVE 188
Cdd:cd08820  109 NQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYI-------LAHYAAIALFGE 169
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
105-175 4.83e-08

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 51.44  E-value: 4.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499342857 105 RILNIHPSLLPAFKGLHAQKQAFEYGVKVaGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLTDRILEQE 175
Cdd:PRK07579  87 RCINIHPGFNPYNRGWFPQVFSIINGLKI-GATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIE 156
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 48-168 5.07e-08

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 50.33  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  48 RAKNHGISAVF---------LDSRGRDRAEYDREILKVLRQYDTDLLLLAGYFRLLGSEIINAYRNRILNIHPSLLPAFK 118
Cdd:cd08649   19 LAAGHRIAAVVstdpairawAAAEGIAVLEPGEALEELLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499342857 119 GLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETLT 168
Cdd:cd08649   99 GLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLN 148
PRK06988 PRK06988
formyltransferase;
85-163 4.51e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 45.84  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499342857  85 LLLAGYFR-LLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDT 163
Cdd:PRK06988  80 FIFSFYYRhMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDT 159
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 90-167 1.12e-05

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 45.36  E-value: 1.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499342857  90 YFR-LLGSEIINAYRNRILNIHPSLLPAFKGLHAQKQAFEYGVKVAGCTVHFVDEGLDSGPIIIQRCVPVLPGDTEETL 167
Cdd:PRK08125  83 YYRnLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTL 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH