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Conserved domains on  [gi|45550868|ref|NP_651857|]
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uncharacterized protein Dmel_CG1750 [Drosophila melanogaster]

Protein Classification

methionyl-tRNA formyltransferase( domain architecture ID 11415469)

methionyl-tRNA formyltransferase catalyzes formylation of the initiator methionyl-tRNA

CATH:  3.40.50.170|3.10.25.10
EC:  2.1.2.9
Gene Ontology:  GO:0004479|GO:0071951
PubMed:  8199241

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
37-325 1.11e-80

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


:

Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 248.10  E-value: 1.11e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANC--------VRTYAEKEKLPLQKwPI---DPSVCPQF-----D 100
Cdd:COG0223   2 RIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRgrkltpspVKELALEHGIPVLQ-PEslkDPEFLEELralnpD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 101 LGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDV 180
Cdd:COG0223  81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMD-EGLDTGDILLQEEVPIGPDD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 181 FMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSElSAIEIYTRHRALYGYKNLTTNFL 260
Cdd:COG0223 160 TAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSR-PAEEIHRLIRALNPWPGAFTTLD 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45550868 261 GKQVQLLELRLPEKRVPVqEPGAISYLRKSRsLIIGCAQQSqLEVLQLRVEGRKPMSAQDFNNGF 325
Cdd:COG0223 239 GKRLKIWKARVLEEAGGG-APGTILAVDKDG-LLVACGDGA-LRLLELQPAGKKRMSAADFLRGY 300
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
37-325 1.11e-80

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 248.10  E-value: 1.11e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANC--------VRTYAEKEKLPLQKwPI---DPSVCPQF-----D 100
Cdd:COG0223   2 RIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRgrkltpspVKELALEHGIPVLQ-PEslkDPEFLEELralnpD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 101 LGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDV 180
Cdd:COG0223  81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMD-EGLDTGDILLQEEVPIGPDD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 181 FMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSElSAIEIYTRHRALYGYKNLTTNFL 260
Cdd:COG0223 160 TAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSR-PAEEIHRLIRALNPWPGAFTTLD 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45550868 261 GKQVQLLELRLPEKRVPVqEPGAISYLRKSRsLIIGCAQQSqLEVLQLRVEGRKPMSAQDFNNGF 325
Cdd:COG0223 239 GKRLKIWKARVLEEAGGG-APGTILAVDKDG-LLVACGDGA-LRLLELQPAGKKRMSAADFLRGY 300
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 37-225 8.59e-77

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: 234.26  E-value: 8.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANC--------VRTYAEKEKLPLQKWP-------IDPSVCPQFDL 101
Cdd:cd08646   2 RIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRgkkltpspVKELALELGLPVLQPEklkdeefLEELKALKPDL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 102 GVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDVF 181
Cdd:cd08646  82 IVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMD-EGLDTGDILAQEEVPIDPDDT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 45550868 182 MPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKI 225
Cdd:cd08646 161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 37-329 1.28e-71

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: 224.97  E-value: 1.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868    37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPA--------NCVRTYAEKEKLP---------LQKWPIDPSVCPqf 99
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkkltpPPVKVLAEEKGIPvfqpekqrqLEELPLVRELKP-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   100 DLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPhRFDIGDILAQREVAINPD 179
Cdd:TIGR00460  80 DVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVP-KMDAGDILKQETFPIEEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   180 VFMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSeLSAIEIYTRHRALYGYKNLTTNF 259
Cdd:TIGR00460 159 DNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWN-QSAEELLNKIRALNPWPTAWLTF 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   260 LGKQVQLLELRLPEKRVPVQEPGAISYLRKSrSLIIGCAQQSQLEVLQLRVEGRKPMSAQDFNNGFLKQA 329
Cdd:TIGR00460 238 EGKNIKIHKAKVIDLSTYKAKPGEIVYHNKK-GILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSRHPW 306
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 98-324 3.84e-40

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 144.07  E-value: 3.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   98 QFDLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMkIEPHRFDIGDILAQREVAIN 177
Cdd:PLN02285  93 QPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVA-FTVRALDAGPVIAQERVEVD 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  178 PDVFMPDLHASLASLGAELLVDTINNL---SVRLKeAKPQDSSRVSYAPKITSKITEiIWSELSAIEIYTRHRALYGYKN 254
Cdd:PLN02285 172 EDIKAPELLPLLFELGTKLLLRELPSVldgSAKDK-ATPQDDSKATHAPKISPEESW-LSFDEEARVLHNKVRAFAGWPG 249

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550868  255 LTTNFL-----GKQVQLLELRLPEKRVP--VQEPGAI--SYLRKSRSLIIGCAQQSQLEVLQLRVEGRKPMSAQDFNNG 324
Cdd:PLN02285 250 TRAKFQlvddgDGEREVLELKIITTRVCeaGGEQTGSadAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMKAKDFWNG 328
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 37-201 2.12e-23

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: 95.05  E-value: 2.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868    37 KILFFGTDNFSlpSLQALHKNC------GDRLGVVTSfkSPANCVRTYAEKEKLPLQ---KWPIDPSvcPQF-------- 99
Cdd:pfam00551   2 KIAVLISGTGS--NLQALIDALrkggqdADVVLVISN--KDKAAGLGRAEQAGIPTFvfeHKGLTPR--SLFdqeladal 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   100 -----DLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREV 174
Cdd:pfam00551  76 ralaaDVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVD-EGLDTGPILAQKAV 154

                         170       180
                  ....*....|....*....|....*..
gi 45550868   175 AINPDVFMPDLHASLASLGAELLVDTI 201
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
37-325 1.11e-80

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 248.10  E-value: 1.11e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANC--------VRTYAEKEKLPLQKwPI---DPSVCPQF-----D 100
Cdd:COG0223   2 RIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRgrkltpspVKELALEHGIPVLQ-PEslkDPEFLEELralnpD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 101 LGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDV 180
Cdd:COG0223  81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMD-EGLDTGDILLQEEVPIGPDD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 181 FMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSElSAIEIYTRHRALYGYKNLTTNFL 260
Cdd:COG0223 160 TAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSR-PAEEIHRLIRALNPWPGAFTTLD 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45550868 261 GKQVQLLELRLPEKRVPVqEPGAISYLRKSRsLIIGCAQQSqLEVLQLRVEGRKPMSAQDFNNGF 325
Cdd:COG0223 239 GKRLKIWKARVLEEAGGG-APGTILAVDKDG-LLVACGDGA-LRLLELQPAGKKRMSAADFLRGY 300
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 37-225 8.59e-77

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: 234.26  E-value: 8.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANC--------VRTYAEKEKLPLQKWP-------IDPSVCPQFDL 101
Cdd:cd08646   2 RIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRgkkltpspVKELALELGLPVLQPEklkdeefLEELKALKPDL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 102 GVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDVF 181
Cdd:cd08646  82 IVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMD-EGLDTGDILAQEEVPIDPDDT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 45550868 182 MPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKI 225
Cdd:cd08646 161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 37-329 1.28e-71

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: 224.97  E-value: 1.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868    37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPA--------NCVRTYAEKEKLP---------LQKWPIDPSVCPqf 99
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkkltpPPVKVLAEEKGIPvfqpekqrqLEELPLVRELKP-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   100 DLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPhRFDIGDILAQREVAINPD 179
Cdd:TIGR00460  80 DVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVP-KMDAGDILKQETFPIEEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   180 VFMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSeLSAIEIYTRHRALYGYKNLTTNF 259
Cdd:TIGR00460 159 DNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWN-QSAEELLNKIRALNPWPTAWLTF 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   260 LGKQVQLLELRLPEKRVPVQEPGAISYLRKSrSLIIGCAQQSQLEVLQLRVEGRKPMSAQDFNNGFLKQA 329
Cdd:TIGR00460 238 EGKNIKIHKAKVIDLSTYKAKPGEIVYHNKK-GILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSRHPW 306
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 98-324 3.84e-40

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 144.07  E-value: 3.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   98 QFDLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMkIEPHRFDIGDILAQREVAIN 177
Cdd:PLN02285  93 QPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVA-FTVRALDAGPVIAQERVEVD 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  178 PDVFMPDLHASLASLGAELLVDTINNL---SVRLKeAKPQDSSRVSYAPKITSKITEiIWSELSAIEIYTRHRALYGYKN 254
Cdd:PLN02285 172 EDIKAPELLPLLFELGTKLLLRELPSVldgSAKDK-ATPQDDSKATHAPKISPEESW-LSFDEEARVLHNKVRAFAGWPG 249

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550868  255 LTTNFL-----GKQVQLLELRLPEKRVP--VQEPGAI--SYLRKSRSLIIGCAQQSQLEVLQLRVEGRKPMSAQDFNNG 324
Cdd:PLN02285 250 TRAKFQlvddgDGEREVLELKIITTRVCeaGGEQTGSadAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMKAKDFWNG 328
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 38-202 4.26e-31

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: 115.46  E-value: 4.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  38 ILFFGTDNFSLPSLQALHKNCGDRL-GVVTSFKSPANCVRTYAE--KEKLPLQKWPIDPSVCP-----QFDLGVVVSFGH 109
Cdd:cd08369   1 IVILGSGNIGQRVLKALLSKEGHEIvGVVTHPDSPRGTAQLSLElvGGKVYLDSNINTPELLEllkefAPDLIVSINFRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 110 LIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPhRFDIGDILAQREVAINPDVFMPDLHASL 189
Cdd:cd08369  81 IIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDE-GIDTGDIIAQEVIPISPDDTAGTLYQRL 159

                       170
                ....*....|...
gi 45550868 190 ASLGAELLVDTIN 202
Cdd:cd08369 160 IELGPKLLKEALQ 172
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 37-201 2.12e-23

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: 95.05  E-value: 2.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868    37 KILFFGTDNFSlpSLQALHKNC------GDRLGVVTSfkSPANCVRTYAEKEKLPLQ---KWPIDPSvcPQF-------- 99
Cdd:pfam00551   2 KIAVLISGTGS--NLQALIDALrkggqdADVVLVISN--KDKAAGLGRAEQAGIPTFvfeHKGLTPR--SLFdqeladal 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   100 -----DLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREV 174
Cdd:pfam00551  76 ralaaDVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVD-EGLDTGPILAQKAV 154

                         170       180
                  ....*....|....*....|....*..
gi 45550868   175 AINPDVFMPDLHASLASLGAELLVDTI 201
Cdd:pfam00551 155 PILPDDTAETLYNRVADLEHKALPRVL 181
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 103-249 9.35e-21

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 93.12  E-value: 9.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  103 VVVSF--GHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDV 180
Cdd:PRK08125  78 VIFSFyyRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMV-KRADAGAIVAQQRVAIAPDD 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550868  181 FMPDLHASLASLGAELLVDTINNLSVRLKEAKPQDSSRVSYAPKITSKITEIIWSeLSAIEIYTRHRAL 249
Cdd:PRK08125 157 TALTLHHKLCHAARQLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWH-KPASTLHNLVRAV 224
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 49-205 7.68e-19

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: 82.88  E-value: 7.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  49 PSLQALHKNCGDRLGVVTSFKSPANCVRTYAEKEKLPLQKWPIDPsvcpQFDLGVVVSFGHLIPGSIINGFPYGMINVHA 128
Cdd:cd08823  26 IAVPAHNASYFPQIFVFTGIRRLVSKQRVDTANLKEQLAEWLRAL----AADTVVVFTFPYRIPQHILDLPPLGFYNLHP 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45550868 129 SLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPhRFDIGDILAQREVAINPDVFMPDLHASLASLGAELLVDTINNLS 205
Cdd:cd08823 102 GLLPAYRGPDPLFWQIRNQEQETAITVHKMTA-EIDRGPIVLEQFTPIHPDDTYGLLCSRLAMLAVGLLEELYQNLA 177
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 36-221 2.75e-18

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: 82.01  E-value: 2.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  36 PKILFFGTDNFSLPSLQALHKNCGDRLGVVTS---------FKSPANCvrtyAEKEKLPL--------QKWPIDPSVCpQ 98
Cdd:cd08644   1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHtdnpgeniwFGSVAQL----AREHGIPVftpddinhPEWVERLRAL-K 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  99 FDLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPhRFDIGDILAQREVAINP 178
Cdd:cd08644  76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTK-KPDAGAIVDQEKVPILP 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 45550868 179 DVFMPDLHASLASLGAELLVDTINNL-SVRLKEAkPQDSSRVSY 221
Cdd:cd08644 155 DDTAKSLFHKLCVAARRLLARTLPALkAGKARER-PQDETQASY 197
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 37-204 1.32e-17

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: 79.23  E-value: 1.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPANCV------RTYAEKEKLPLQKWPI--DPSV-----CPQFDLGV 103
Cdd:cd08651   1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDsdyldlDSFARKNGIPYYKFTDinDEEIiewikEANPDIIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 104 VVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPHrFDIGDILAQREVAINPDVFMP 183
Cdd:cd08651  81 VFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEG-ADSGDILSQEPFPIDKDDTAN 159

                       170       180
                ....*....|....*....|.
gi 45550868 184 DLHASLASLGAELLVDTINNL 204
Cdd:cd08651 160 SLYDKIMEAAKQQIDKFLPRL 180
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
224-326 1.87e-15

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 71.15  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   224 KITSKITEIIWSElSAIEIYTRHRALYGYKNLTTNFLGKQVQLLELRLPEKRVPvQEPGAISYLRKSrSLIIGCAQqSQL 303
Cdd:pfam02911   1 KIKKEDGRIDWNQ-PAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASVLDQESG-AAPGTIVTVDKG-GLLVACGD-GAL 76

                          90       100
                  ....*....|....*....|...
gi 45550868   304 EVLQLRVEGRKPMSAQDFNNGFL 326
Cdd:pfam02911  77 LILELQLEGKKPMSAEDFLNGFR 99
PRK06988 PRK06988
formyltransferase;
36-321 4.96e-15

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 74.73  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   36 PKILFFGTDNFSLPSLQALHKNCGDRLGVVTSFKSPA-----NCVRTYAEKEKLPLQKwPIDP----------SVCPQFd 100
Cdd:PRK06988   3 PRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPTeniwfGSVAAVAAEHGIPVIT-PADPndpelraavaAAAPDF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  101 lgvVVSF--GHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSI--MKIEPhrfDIGDILAQREVAI 176
Cdd:PRK06988  81 ---IFSFyyRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLheMVAKP---DAGAIVDQTAVPI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  177 NPD-----VFMPDLHAS---LASLGAELLVDTINNLSVRLKEA------KPQDSsrvsyapkitskitEIIWSElSAIEI 242
Cdd:PRK06988 155 LPDdtaaqVFDKVTVAAeqtLWRVLPALLAGEAPHLPNDLAQGsyfggrKPEDG--------------RIDWSK-PAAQV 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  243 YTRHRAL-YGYKNLTTNFLGKQVQLLELRLPE---KRVPVQEPGAISYLRKsrsLIIGCAQQSQLEVLQLR---VEGRKP 315
Cdd:PRK06988 220 YNLIRAVaPPYPGAFTDLGGTRFVVARARLAApgaAAARDLPPGLHVSDNA---LFGVCGDGRAVSILELRrqqDGGETV 296


                 ....*.
gi 45550868  316 MSAQDF 321
Cdd:PRK06988 297 VTPAQF 302
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 37-204 2.22e-13

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: 66.85  E-value: 2.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFF-GTDNFSLPSLQALHKNCGD-RLGVVTSFKSPAnCVRTYAEkeklplqkwpIDPSVcpqfdlgVVVSFGHLIPGS 114
Cdd:cd08653   1 RIVLLtGDDPSHLYLANALLDAFGGvGVIVVNSINGPE-VVAALRA----------LAPDV-------VSVYGCGIIKDA 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 115 IINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDA-STGVSIMKIEPhRFDIGDILAQREVAINPDVFMPDLHASLASLG 193
Cdd:cd08653  63 LLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPdNVGVTVHLVDA-GIDTGDVLAQARPPLAAGDTLLSLYLRLYRAG 141

                       170
                ....*....|.
gi 45550868 194 AELLVDTINNL 204
Cdd:cd08653 142 VELMVEAIADL 152
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 37-179 3.89e-11

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: 61.70  E-value: 3.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFGTDNFSLPSLQALHKNCGDRLGVVT--SFKSPANCVRTYAEKEKLPLQKWP-------IDPSVCPQF-----DLG 102
Cdd:cd08647   2 KIAVIGQSLFGQEVYKELRKEGHEVVGVFTipDKDGKADPLALEAEKDGVPVFKFPrwrakgqAIPEVVAKYkalgaELN 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45550868 103 VVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPD 179
Cdd:cd08647  82 VLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWAD-DGLDTGPILLQKECDVLPN 157
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 231-318 1.03e-10

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.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 57.54  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 231 EIIWSElSAIEIYTRHRALYGYKNLTTNFLGKQVQLLELRLPEKRVPVQEPGAISYLRKsrSLIIGCAqQSQLEVLQLRV 310
Cdd:cd08704   4 RIDWSK-SAEEIHNLIRALNPWPGAYTTLNGKRLKILKAEVLEESGEAAPGTILAVDKK--GLLVACG-DGALEILELQP 79


                ....*...
gi 45550868 311 EGRKPMSA 318
Cdd:cd08704  80 EGKKRMSA 87
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 37-201 3.30e-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: 58.22  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  37 KILFFG---TDNFSLPSLQALHKNCGDRLGVVTSFKSPANcVRTYAEKEKLPLQKWPIDPSV-----CPQFDLGVVVSFG 108
Cdd:cd08820   1 RIVFLGqkpIGEECLRTLLRLQDRGSFEIIAVLTNTSPAD-VWEGSEPLYDIGSTERNLHKLleileNKGVDILISVQYH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 109 HLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDVFMPDLHAS 188
Cdd:cd08820  80 WILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMA-EGIDSGDIIFEKRFPIPSDCTVISLYIL 158

                       170
                ....*....|...
gi 45550868 189 LASLGAELLVDTI 201
Cdd:cd08820 159 AHYAAIALFGEHI 171
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 111-223 3.64e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 58.63  E-value: 3.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 111 IPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPDVFMPDL-HASL 189
Cdd:cd08822  79 ISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLD-DGVDGGPIAAQDWCHVRPGDTAAELwRRAL 157

                        90       100       110
                ....*....|....*....|....*....|....*
gi 45550868 190 ASLGAELLVDTINNLSV-RLKEAKPQDSSRVSYAP 223
Cdd:cd08822 158 APMGVKLLTQVIDALLRgGNLPAQPQDERLATWEP 192
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 109-179 3.47e-09

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: 55.47  E-value: 3.47e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550868 109 HLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEPHrFDIGDILAQREVAINPD 179
Cdd:cd08645  89 RILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEE-VDTGPIIAQAAVPVLPG 158
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 107-204 2.35e-08

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: 53.50  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868 107 FGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSImkiepHrF-----DIGDILAQREVAINPDvf 181
Cdd:COG0299  89 FMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTV-----H-FvdeevDTGPIIAQAAVPVLPD-- 160

                        90       100
                ....*....|....*....|....*..
gi 45550868 182 mpDLHASLAS--LGAE--LLVDTINNL 204
Cdd:COG0299 161 --DTEETLAAriLEQEhrLYPEAIRLL 185
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
98-204 1.82e-06

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 48.36  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   98 QFDLGVVVSFGHLIPGSIINGFPygMINVHASLLPKWRGAAPIIYAIMKgDASTGVSIMKIEpHRFDIGDILAQREVAIN 177
Cdd:PRK07579  65 RYDLVLSFHCKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSIIN-GLKIGATIHEMD-EQLDHGPIIAQREVEIE 140

                         90       100
                 ....*....|....*....|....*..
gi 45550868  178 PDVFMPDLHASLASLGAELLVDTINNL 204
Cdd:PRK07579 141 SWDSSGSVYARVMDIERELVLEHFDAI 167
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 58-179 1.41e-05

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: 44.56  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868  58 CGDRL--------GVVTSfkSPAncVRTYAEKEKLPLQKWPIDPS--VCPQ-FDLGVVVSFGHLIPGSIINGFPYGMINV 126
Cdd:cd08649  14 CAEQLlaaghriaAVVST--DPA--IRAWAAAEGIAVLEPGEALEelLSDEpFDWLFSIVNLRILPSEVLALPRKGAINF 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 45550868 127 HASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPD 179
Cdd:cd08649  90 HDGPLPRYAGLNATSWALLAGETRHGVTWHRIE-EGVDAGDILVQRPFDIAPD 141
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 110-179 2.40e-05

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 44.68  E-value: 2.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45550868  110 LIPGSIINGFPYGMINVHASLLPKWRGAApiIYA-------IMKGDASTGVSIMKIEPHrFDIGDILAQREVAINPD 179
Cdd:PLN02331  90 LIPVELVRAYPRSILNIHPALLPAFGGKG--YYGikvhkavIASGARYSGPTVHFVDEH-YDTGRILAQRVVPVLAT 163
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 100-187 9.38e-04

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: 39.66  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550868   100 DLGVVVSFGHLIPGSIINGFPYGMINVHASLLPKWRGAAPIIYAIMKGDASTGVSIMKIEpHRFDIGDILAQREVAINPD 179
Cdd:TIGR00639  81 DLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVD-EEVDTGPIIAQAKVPILPE 159


                  ....*...
gi 45550868   180 VFMPDLHA 187
Cdd:TIGR00639 160 DTEETLEQ 167
 
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.
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