NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|663513270|gb|AIF03814|]
View 

methionyl-tRNA formyltransferase (MTFMT, fmt) [uncultured marine group II/III euryarchaeote KM3_169_H09]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FMT_core super family cl00395
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 62-197 4.64e-23

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.


The actual alignment was detected with superfamily member cd08653:

Pssm-ID: 444886 [Multi-domain]  Cd Length: 152  Bit Score: 91.12  E-value: 4.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  62 IEAQLADlAEQGIDVphIEVPIHNSEQVMPHIREIDLDLIVFGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWS 141
Cdd:cd08653   15 LANALLD-AFGGVGV--IVVNSINGPEVVAALRALAPDVVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWA 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663513270 142 VYHDIP--IGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLcYETLVLAGA-LMKEAL 197
Cdd:cd08653   92 LANGDPdnVGVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSL-YLRLYRAGVeLMVEAI 149
 
Name Accession Description Interval E-value
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 62-197 4.64e-23

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: 91.12  E-value: 4.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  62 IEAQLADlAEQGIDVphIEVPIHNSEQVMPHIREIDLDLIVFGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWS 141
Cdd:cd08653   15 LANALLD-AFGGVGV--IVVNSINGPEVVAALRALAPDVVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWA 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663513270 142 VYHDIP--IGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLcYETLVLAGA-LMKEAL 197
Cdd:cd08653   92 LANGDPdnVGVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSL-YLRLYRAGVeLMVEAI 149
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
14-216 1.04e-18

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 83.23  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  14 HPYGREMLRQILSEGFVPTIVIT-EDSAIGdeerekflkRieGNDIAPTIEAQLAdlAEQGIDVPHIEVPihNSEQVMPH 92
Cdd:COG0223    9 PDFAVPSLEALLAAGHEVVAVVTqPDRPAG---------R--GRKLTPSPVKELA--LEHGIPVLQPESL--KDPEFLEE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  93 IREIDLDLIV---FGgtRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYHDIPI-GSSTHFCDNGIDTGELLLRR 168
Cdd:COG0223   74 LRALNPDLIVvvaYG--QILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTEtGVTIMQMDEGLDTGDILLQE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663513270 169 EVAVTRGMTYEDLCYETLVLAGALMKEALVAYSAGRwdEMRHPQGESE 216
Cdd:COG0223  152 EVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGT--LTPTPQDESG 197
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 93-197 4.30e-11

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: 60.00  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270   93 IREIDLDLIVFGG-TRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYH-DIPIGSSTHFCDNGIDTGELLLRREV 170
Cdd:pfam00551  75 LRALAADVIVLAGyMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAgDKETGVTIHFVDEGLDTGPILAQKAV 154

                          90       100
                  ....*....|....*....|....*..
gi 663513270  171 AVTRGMTYEDLCYETLVLAGALMKEAL 197
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
119-172 8.52e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 45.66  E-value: 8.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663513270 119 DGV--INSHPGLLPDCRGSASPAWSVYHDIPIGSSTHFCDNGIDTGELLLRREVAV 172
Cdd:PRK07579  84 NGVrcINIHPGFNPYNRGWFPQVFSIINGLKIGATIHEMDEQLDHGPIIAQREVEI 139
 
Name Accession Description Interval E-value
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 62-197 4.64e-23

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: 91.12  E-value: 4.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  62 IEAQLADlAEQGIDVphIEVPIHNSEQVMPHIREIDLDLIVFGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWS 141
Cdd:cd08653   15 LANALLD-AFGGVGV--IVVNSINGPEVVAALRALAPDVVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWA 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663513270 142 VYHDIP--IGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLcYETLVLAGA-LMKEAL 197
Cdd:cd08653   92 LANGDPdnVGVTVHLVDAGIDTGDVLAQARPPLAAGDTLLSL-YLRLYRAGVeLMVEAI 149
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
14-216 1.04e-18

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 83.23  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  14 HPYGREMLRQILSEGFVPTIVIT-EDSAIGdeerekflkRieGNDIAPTIEAQLAdlAEQGIDVPHIEVPihNSEQVMPH 92
Cdd:COG0223    9 PDFAVPSLEALLAAGHEVVAVVTqPDRPAG---------R--GRKLTPSPVKELA--LEHGIPVLQPESL--KDPEFLEE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  93 IREIDLDLIV---FGgtRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYHDIPI-GSSTHFCDNGIDTGELLLRR 168
Cdd:COG0223   74 LRALNPDLIVvvaYG--QILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTEtGVTIMQMDEGLDTGDILLQE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663513270 169 EVAVTRGMTYEDLCYETLVLAGALMKEALVAYSAGRwdEMRHPQGESE 216
Cdd:COG0223  152 EVPIGPDDTAGSLHDKLAELGAELLLETLDALEAGT--LTPTPQDESG 197
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 48-197 2.91e-18

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: 79.25  E-value: 2.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  48 KFLKRIEGNDIA--------PTIEAQLADLAEQGIDVPHievPIHNSEQVMPHIREIDLDLIV-FGGTRIIRGEILDHPA 118
Cdd:cd08369   15 KALLSKEGHEIVgvvthpdsPRGTAQLSLELVGGKVYLD---SNINTPELLELLKEFAPDLIVsINFRQIIPPEILKLPP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 119 DGVINSHPGLLPDCRGSASPAWSVYHDIP-IGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLCYETLVLAGALMKEAL 197
Cdd:cd08369   92 GGAINIHPSLLPRYRGVNPLAWAIINGEKeTGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEAL 171
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 17-172 2.32e-15

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: 71.53  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  17 GREMLRQILSEGFVPTIVITEDsaigdeeREKFlkrieGNDiapTIEAQLADLAEQ-GIDVPHIEvPIhNSEQVMPHIRE 95
Cdd:cd08651   11 SLIALEAILEAGGEVVGVITLD-------DSSS-----NND---SDYLDLDSFARKnGIPYYKFT-DI-NDEEIIEWIKE 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663513270  96 IDLDLI-VFGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYHDIPIGSSTHF-CDNGIDTGELLLRREVAV 172
Cdd:cd08651   74 ANPDIIfVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFwMDEGADSGDILSQEPFPI 152
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 21-197 1.32e-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: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 69.40  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  21 LRQILSEGFVPTIVITEDSAIGDEEREKFLKRIegndiaptieaqladlAEQGIDVPHIevpIHNSEQVMPHIREIDLD- 99
Cdd:cd08823   14 LGQLLSEGRLAGIAVPAHNASYFPQIFVFTGIR----------------RLVSKQRVDT---ANLKEQLAEWLRALAADt 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 100 LIVFGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYH-DIPIGSSTHFCDNGIDTGELLLRREVAVTRGMTY 178
Cdd:cd08823   75 VVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNqEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154

                        170
                 ....*....|....*....
gi 663513270 179 EDLCYETLVLAGALMKEAL 197
Cdd:cd08823  155 GLLCSRLAMLAVGLLEELY 173
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 55-216 1.61e-14

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: 69.78  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  55 GNDIAPTIEAQLADlaEQGIDVphIEVPIHNSEQVMPHIREIDLDLIV---FGgtRIIRGEILDHPADGVINSHPGLLPD 131
Cdd:cd08646   40 GKKLTPSPVKELAL--ELGLPV--LQPEKLKDEEFLEELKALKPDLIVvvaYG--QILPKEILDLPPYGCINVHPSLLPK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 132 CRGsASPawsVYH-----DIPIGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLcYETL-VLAGALMKEALVAYSAGRW 205
Cdd:cd08646  114 YRG-AAP---IQRailngDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGEL-LDKLaELGADLLLEVLDDIEAGKL 188

                        170
                 ....*....|.
gi 663513270 206 DemRHPQGESE 216
Cdd:cd08646  189 N--PVPQDESE 197
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 93-197 4.30e-11

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: 60.00  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270   93 IREIDLDLIVFGG-TRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYH-DIPIGSSTHFCDNGIDTGELLLRREV 170
Cdd:pfam00551  75 LRALAADVIVLAGyMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAgDKETGVTIHFVDEGLDTGPILAQKAV 154

                          90       100
                  ....*....|....*....|....*..
gi 663513270  171 AVTRGMTYEDLCYETLVLAGALMKEAL 197
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 106-181 9.95e-10

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: 56.69  E-value: 9.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663513270 106 TRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYHDIPIGSSTHF-CDNGIDTGELLLRREVAVTRGMTYEDL 181
Cdd:cd08647   87 SQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFwADDGLDTGPILLQKECDVLPNDTVDTL 163
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 92-181 1.36e-09

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: 56.19  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  92 HIREIDLDLIVFGG-TRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSV-YHDIPIGSSTHFCDNGIDTGELLLRRE 169
Cdd:COG0299   75 ALDAYGPDLVVLAGfMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALeAGVKVTGCTVHFVDEEVDTGPIIAQAA 154

                         90
                 ....*....|..
gi 663513270 170 VAVTRGMTYEDL 181
Cdd:COG0299  155 VPVLPDDTEETL 166
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 77-181 1.29e-06

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: 47.45  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  77 PHIEVPIHNSEQVMPHireidLDLIVFGGT-RIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYHDIPI-GSSTHF 154
Cdd:cd08822   51 PRAGVAVLPADAIPPG-----TDLIVAAHChAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPItGGTVYH 125

                         90       100
                 ....*....|....*....|....*..
gi 663513270 155 CDNGIDTGELLLRREVAVTRGMTYEDL 181
Cdd:cd08822  126 LDDGVDGGPIAAQDWCHVRPGDTAAEL 152
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 107-185 4.00e-06

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: 45.71  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 107 RIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVY-----HdipiGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDL 181
Cdd:cd08649   72 RILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLagetrH----GVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147


                 ....*..
gi 663513270 182 ---CYET 185
Cdd:cd08649  148 nlkCYEA 154
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
119-172 8.52e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 45.66  E-value: 8.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663513270 119 DGV--INSHPGLLPDCRGSASPAWSVYHDIPIGSSTHFCDNGIDTGELLLRREVAV 172
Cdd:PRK07579  84 NGVrcINIHPGFNPYNRGWFPQVFSIINGLKIGATIHEMDEQLDHGPIIAQREVEI 139
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 64-240 2.23e-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: 44.97  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  64 AQLAdlAEQGIdvphievPIHNSEQV-----MPHIREIDLDLIV-FGGTRIIRGEILDHPADGVINSHPGLLPDCRGSAS 137
Cdd:PRK08125  46 ARLA--AELGI-------PVYAPEDVnhplwVERIRELAPDVIFsFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAP 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 138 PAWSVYH-DIPIGSSTHFCDNGIDTGELLLRREVAVTRGMT----YEDLCYetlvLAGALMKEALVAYSAGRWDEmrHPQ 212
Cdd:PRK08125 117 LNWVLVNgETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTaltlHHKLCH----AARQLLEQTLPAIKHGNIPE--IPQ 190

                        170       180
                 ....*....|....*....|....*...
gi 663513270 213 GESEHPTFRNAGPDILEVVNHKLAEQTY 240
Cdd:PRK08125 191 DESQATYFGRRTPADGLIDWHKPASTLH 218
PRK06988 PRK06988
formyltransferase;
6-144 2.30e-04

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 41.60  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270   6 FAYlllkeHPYGREMLRQILSEGFVPTIVIT-EDSAigDEEreKFLKRIegndiaptieAQLAdlAEQGIDVPHIEVPih 84
Cdd:PRK06988   8 FAY-----HNVGVRCLQVLLARGVDVALVVThEDNP--TEN--IWFGSV----------AAVA--AEHGIPVITPADP-- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513270  85 NSEQVMPHIREIDLDLIV-FGGTRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVYH 144
Cdd:PRK06988  65 NDPELRAAVAAAAPDFIFsFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLN 125
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 52-216 4.58e-04

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 40.83  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  52 RIEGNDIAPTIEAQLAdlAEQGIDVPHIEVPIHNSEQ-VMPHIREIDLDLIV---FGgtRIIRGEILDHPADGVINSHPG 127
Cdd:PLN02285  49 RGRGRKLMPSPVAQLA--LDRGFPPDLIFTPEKAGEEdFLSALRELQPDLCItaaYG--NILPQKFLDIPKLGTVNIHPS 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270 128 LLPDCRGSASPAWSVYH-DIPIGSSTHFCDNGIDTGELLLRREVAVTRGMTYEDLCYETLVLAGALMKEALVAYSAGRWD 206
Cdd:PLN02285 125 LLPLYRGAAPVQRALQDgVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLLRELPSVLDGSAK 204

                        170
                 ....*....|
gi 663513270 207 EMRHPQGESE 216
Cdd:PLN02285 205 DKATPQDDSK 214
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 87-207 2.12e-03

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 38.14  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513270  87 EQVMPHIREIDLDLIVFGG-TRIIRGEILDHPADGVINSHPGLLPDCRGSASPAWSVyHDIPI-------GSSTHFCDNG 158
Cdd:PLN02331  68 DELVDALRGAGVDFVLLAGyLKLIPVELVRAYPRSILNIHPALLPAFGGKGYYGIKV-HKAVIasgarysGPTVHFVDEH 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663513270 159 IDTGELLLRREVAVTRGMTYEDLCYETLVLAGALMKEALVAYSAGR--WDE 207
Cdd:PLN02331 147 YDTGRILAQRVVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERivWRE 197
 
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