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Conserved domains on  [gi|57528326|ref|NP_001009697|]
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methionyl-tRNA formyltransferase, mitochondrial [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fmt super family cl36662
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 44-353 2.12e-121

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]


The actual alignment was detected with superfamily member TIGR00460:

Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 353.63  E-value: 2.12e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326    44 RVLFFGTDHFAREALRAL----------------HAARDNKEekLIEKLEVVTVPsispKGLPVKQYAIQSQLpvYEWPD 107
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELrednfevvgvvtqpdkPAGRGKKL--TPPPVKVLAEE----KGIPVFQPEKQRQL--EELPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   108 MGSGEYDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQET 187
Cdd:TIGR00460  74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPK-MDAGDILKQET 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   188 VAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAIGdiv 267
Cdd:TIGR00460 153 FPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDW-NQSAEELLNKIRALN--- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   268 PLQTLWMENTVKLLDLVEVNNSILADPKVMgqtvtPGSVVYHRPSQMLLVHCKDGWIGVRSI--MHKKTLTATDFYNGYL 345
Cdd:TIGR00460 229 PWPTAWLTFEGKNIKIHKAKVIDLSTYKAK-----PGEIVYHNKKGILVACGKDGILLLLSLqpPGKKVMRAEDFYNGSR 303


                  ....*...
gi 57528326   346 HAWYQKNS 353
Cdd:TIGR00460 304 HPWYVPGS 311
 
Name Accession Description Interval E-value
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 44-353 2.12e-121

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: 353.63  E-value: 2.12e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326    44 RVLFFGTDHFAREALRAL----------------HAARDNKEekLIEKLEVVTVPsispKGLPVKQYAIQSQLpvYEWPD 107
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELrednfevvgvvtqpdkPAGRGKKL--TPPPVKVLAEE----KGIPVFQPEKQRQL--EELPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   108 MGSGEYDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQET 187
Cdd:TIGR00460  74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPK-MDAGDILKQET 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   188 VAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAIGdiv 267
Cdd:TIGR00460 153 FPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDW-NQSAEELLNKIRALN--- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   268 PLQTLWMENTVKLLDLVEVNNSILADPKVMgqtvtPGSVVYHRPSQMLLVHCKDGWIGVRSI--MHKKTLTATDFYNGYL 345
Cdd:TIGR00460 229 PWPTAWLTFEGKNIKIHKAKVIDLSTYKAK-----PGEIVYHNKKGILVACGKDGILLLLSLqpPGKKVMRAEDFYNGSR 303


                  ....*...
gi 57528326   346 HAWYQKNS 353
Cdd:TIGR00460 304 HPWYVPGS 311
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 43-239 2.10e-74

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: 229.64  E-value: 2.10e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  43 WRVLFFGTDHFAREALRALHAARdnkeeklIEKLEVVTVPsISPKG-------LPVKQYAIQSQLPVYEWPDMGSGE--- 112
Cdd:cd08646   1 MRIVFMGTPDFAVPSLEALLKSG-------HEVVAVVTQP-DKPRGrgkkltpSPVKELALELGLPVLQPEKLKDEEfle 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 113 ------YDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQE 186
Cdd:cd08646  73 elkalkPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEG-LDTGDILAQE 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57528326 187 TVAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKV 239
Cdd:cd08646 152 EVPIDPDDTAGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
44-344 4.08e-63

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 204.18  E-value: 4.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFFGTDHFAREALRALHAARdnkeeklIEKLEVVTVPSiSPKGL-------PVKQYAIQSQLPVYEWPDMGSGE---- 112
Cdd:COG0223   2 RIVFMGTPDFAVPSLEALLAAG-------HEVVAVVTQPD-RPAGRgrkltpsPVKELALEHGIPVLQPESLKDPEflee 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 113 -----YDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQET 187
Cdd:COG0223  74 lralnPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEG-LDTGDILLQEE 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 188 VAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAigdiv 267
Cdd:COG0223 153 VPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDW-SRPAEEIHRLIRA----- 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 268 pLQ------TLWMENTVKLLDlvevnnsilADPKVMGQTVTPGSVVyHRPSQMLLVHCKDGWIGVRSIM--HKKTLTATD 339
Cdd:COG0223 227 -LNpwpgafTTLDGKRLKIWK---------ARVLEEAGGGAPGTIL-AVDKDGLLVACGDGALRLLELQpaGKKRMSAAD 295


                ....*
gi 57528326 340 FYNGY 344
Cdd:COG0223 296 FLRGY 300
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 44-344 9.64e-26

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 105.93  E-value: 9.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   44 RVLFFGTDHFAREALRALHAArDNKEEKLIEKLEVVTVPSiSPKGL-------PVKQYAIQSQLPvyewPDM-----GSG 111
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLDA-SQAPDSAFEVAAVVTQPP-ARRGRgrklmpsPVAQLALDRGFP----PDLiftpeKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  112 EY-----------DVGVVASFGRLLSEalilKF----PYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIM-QVRpk 175
Cdd:PLN02285  82 EEdflsalrelqpDLCITAAYGNILPQ----KFldipKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAfTVR-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  176 RFDVGPILKQETVAVPPKSTSKELEAVLSKLGANMLIsvlKNLP-----ESLNNGRPQPAEGVTYAPKVSAGTSCVKWEE 250
Cdd:PLN02285 156 ALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLL---RELPsvldgSAKDKATPQDDSKATHAPKISPEESWLSFDE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  251 QTSeqVL-------------RLHLAIGDIVPLQTlwmentvkllDLVEVnnSILADP---KVMGQTVTPGSVVYHRPSqm 314
Cdd:PLN02285 233 EAR--VLhnkvrafagwpgtRAKFQLVDDGDGER----------EVLEL--KIITTRvceAGGEQTGSADAVTFKKDS-- 296

                        330       340       350
                 ....*....|....*....|....*....|...
gi 57528326  315 LLVHCKDG-WIGVRSIM--HKKTLTATDFYNGY 344
Cdd:PLN02285 297 LLVPCGGGtWLEVLEVQppGKKVMKAKDFWNGL 329
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 45-215 1.99e-25

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: 101.21  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326    45 VLFFGTDHFareaLRALH-AARDNKEEkliekLEVVTVPSiSPKGLPVKQYAIQSQLP--VYEWPDMGS-GEY------- 113
Cdd:pfam00551   5 VLISGTGSN----LQALIdALRKGGQD-----ADVVLVIS-NKDKAAGLGRAEQAGIPtfVFEHKGLTPrSLFdqelada 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   114 ------DVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRpKRFDVGPILKQET 187
Cdd:pfam00551  75 lralaaDVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVD-EGLDTGPILAQKA 153

                         170       180
                  ....*....|....*....|....*...
gi 57528326   188 VAVPPKSTSKELEAVLSKLGANMLISVL 215
Cdd:pfam00551 154 VPILPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 44-353 2.12e-121

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: 353.63  E-value: 2.12e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326    44 RVLFFGTDHFAREALRAL----------------HAARDNKEekLIEKLEVVTVPsispKGLPVKQYAIQSQLpvYEWPD 107
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELrednfevvgvvtqpdkPAGRGKKL--TPPPVKVLAEE----KGIPVFQPEKQRQL--EELPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   108 MGSGEYDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQET 187
Cdd:TIGR00460  74 VRELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPK-MDAGDILKQET 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   188 VAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAIGdiv 267
Cdd:TIGR00460 153 FPIEEEDNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDW-NQSAEELLNKIRALN--- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   268 PLQTLWMENTVKLLDLVEVNNSILADPKVMgqtvtPGSVVYHRPSQMLLVHCKDGWIGVRSI--MHKKTLTATDFYNGYL 345
Cdd:TIGR00460 229 PWPTAWLTFEGKNIKIHKAKVIDLSTYKAK-----PGEIVYHNKKGILVACGKDGILLLLSLqpPGKKVMRAEDFYNGSR 303


                  ....*...
gi 57528326   346 HAWYQKNS 353
Cdd:TIGR00460 304 HPWYVPGS 311
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 43-239 2.10e-74

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: 229.64  E-value: 2.10e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  43 WRVLFFGTDHFAREALRALHAARdnkeeklIEKLEVVTVPsISPKG-------LPVKQYAIQSQLPVYEWPDMGSGE--- 112
Cdd:cd08646   1 MRIVFMGTPDFAVPSLEALLKSG-------HEVVAVVTQP-DKPRGrgkkltpSPVKELALELGLPVLQPEKLKDEEfle 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 113 ------YDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQE 186
Cdd:cd08646  73 elkalkPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEG-LDTGDILAQE 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57528326 187 TVAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKV 239
Cdd:cd08646 152 EVPIDPDDTAGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
44-344 4.08e-63

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 204.18  E-value: 4.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFFGTDHFAREALRALHAARdnkeeklIEKLEVVTVPSiSPKGL-------PVKQYAIQSQLPVYEWPDMGSGE---- 112
Cdd:COG0223   2 RIVFMGTPDFAVPSLEALLAAG-------HEVVAVVTQPD-RPAGRgrkltpsPVKELALEHGIPVLQPESLKDPEflee 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 113 -----YDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPKrFDVGPILKQET 187
Cdd:COG0223  74 lralnPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEG-LDTGDILLQEE 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 188 VAVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAigdiv 267
Cdd:COG0223 153 VPIGPDDTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDW-SRPAEEIHRLIRA----- 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 268 pLQ------TLWMENTVKLLDlvevnnsilADPKVMGQTVTPGSVVyHRPSQMLLVHCKDGWIGVRSIM--HKKTLTATD 339
Cdd:COG0223 227 -LNpwpgafTTLDGKRLKIWK---------ARVLEEAGGGAPGTIL-AVDKDGLLVACGDGALRLLELQpaGKKRMSAAD 295


                ....*
gi 57528326 340 FYNGY 344
Cdd:COG0223 296 FLRGY 300
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 45-216 1.20e-26

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: 104.29  E-value: 1.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  45 VLFFGTDHFAREALRALHaardnkEEKLIEKLEVVTVP----------SISPKGLPVKQYAIQSQLPVYEwpdMGSGEYD 114
Cdd:cd08369   1 IVILGSGNIGQRVLKALL------SKEGHEIVGVVTHPdsprgtaqlsLELVGGKVYLDSNINTPELLEL---LKEFAPD 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 115 VGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPkRFDVGPILKQETVAVPPKS 194
Cdd:cd08369  72 LIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDE-GIDTGDIIAQEVIPISPDD 150

                       170       180
                ....*....|....*....|..
gi 57528326 195 TSKELEAVLSKLGANMLISVLK 216
Cdd:cd08369 151 TAGTLYQRLIELGPKLLKEALQ 172
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 44-344 9.64e-26

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 105.93  E-value: 9.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   44 RVLFFGTDHFAREALRALHAArDNKEEKLIEKLEVVTVPSiSPKGL-------PVKQYAIQSQLPvyewPDM-----GSG 111
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLDA-SQAPDSAFEVAAVVTQPP-ARRGRgrklmpsPVAQLALDRGFP----PDLiftpeKAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  112 EY-----------DVGVVASFGRLLSEalilKF----PYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIM-QVRpk 175
Cdd:PLN02285  82 EEdflsalrelqpDLCITAAYGNILPQ----KFldipKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAfTVR-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  176 RFDVGPILKQETVAVPPKSTSKELEAVLSKLGANMLIsvlKNLP-----ESLNNGRPQPAEGVTYAPKVSAGTSCVKWEE 250
Cdd:PLN02285 156 ALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLL---RELPsvldgSAKDKATPQDDSKATHAPKISPEESWLSFDE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  251 QTSeqVL-------------RLHLAIGDIVPLQTlwmentvkllDLVEVnnSILADP---KVMGQTVTPGSVVYHRPSqm 314
Cdd:PLN02285 233 EAR--VLhnkvrafagwpgtRAKFQLVDDGDGER----------EVLEL--KIITTRvceAGGEQTGSADAVTFKKDS-- 296

                        330       340       350
                 ....*....|....*....|....*....|...
gi 57528326  315 LLVHCKDG-WIGVRSIM--HKKTLTATDFYNGY 344
Cdd:PLN02285 297 LLVPCGGGtWLEVLEVQppGKKVMKAKDFWNGL 329
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 45-215 1.99e-25

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: 101.21  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326    45 VLFFGTDHFareaLRALH-AARDNKEEkliekLEVVTVPSiSPKGLPVKQYAIQSQLP--VYEWPDMGS-GEY------- 113
Cdd:pfam00551   5 VLISGTGSN----LQALIdALRKGGQD-----ADVVLVIS-NKDKAAGLGRAEQAGIPtfVFEHKGLTPrSLFdqelada 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   114 ------DVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRpKRFDVGPILKQET 187
Cdd:pfam00551  75 lralaaDVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVD-EGLDTGPILAQKA 153

                         170       180
                  ....*....|....*....|....*...
gi 57528326   188 VAVPPKSTSKELEAVLSKLGANMLISVL 215
Cdd:pfam00551 154 VPILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 44-237 3.23e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 73.26  E-value: 3.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFFGTDHFAREALRALHAARDnkeeklieKLEVVTVPSISPKGLPVKQYAIQSQLPVYEWPDMGSGEY----DVGVVA 119
Cdd:cd08822   2 KIAIAGQKWFGTAVLEALRARGI--------ALLGVAAPEEGDRLAAAARTAGSRGLPRAGVAVLPADAIppgtDLIVAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 120 SFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRpKRFDVGPILKQETVAVPPKSTSKEL 199
Cdd:cd08822  74 HCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLD-DGVDGGPIAAQDWCHVRPGDTAAEL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 57528326 200 -EAVLSKLGANMLISVLKNLPESLN-NGRPQPAEGVTYAP 237
Cdd:cd08822 153 wRRALAPMGVKLLTQVIDALLRGGNlPAQPQDERLATWEP 192
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 124-322 1.20e-14

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 75.40  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  124 LLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVrPKRFDVGPILKQETVAVPPKSTSKELEAVL 203
Cdd:PRK08125  87 LLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRM-VKRADAGAIVAQQRVAIAPDDTALTLHHKL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  204 SKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWeEQTSEQVLRLHLAIGDIVPLQ---------TLWm 274
Cdd:PRK08125 166 CHAARQLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDW-HKPASTLHNLVRAVTDPWPGAfsyvgeqkfTVW- 243

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 57528326  275 entvklldlvevNNSILADPkvmgQTVTPGSVVYHRPsqmLLVHCKDG 322
Cdd:PRK08125 244 ------------SSRVLPDA----SGAQPGTVLSVAP---LRIACGEG 272
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 117-218 3.79e-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: 70.17  E-value: 3.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 117 VVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVRPkRFDVGPILKQETVAVPPKSTS 196
Cdd:cd08823  76 VVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTA-EIDRGPIVLEQFTPIHPDDTY 154

                        90       100
                ....*....|....*....|..
gi 57528326 197 KELEAVLSKLGANMLISVLKNL 218
Cdd:cd08823 155 GLLCSRLAMLAVGLLEELYQNL 176
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 120-235 6.50e-14

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: 70.07  E-value: 6.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 120 SFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTI--MQVRPkrfDVGPILKQETVAVPPKSTSK 197
Cdd:cd08644  83 YYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLhrMTKKP---DAGAIVDQEKVPILPDDTAK 159

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 57528326 198 EleaVLSKL--GANMLISvlKNLPESLNN---GRPQPAEGVTY 235
Cdd:cd08644 160 S---LFHKLcvAARRLLA--RTLPALKAGkarERPQDETQASY 197
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
238-345 6.72e-14

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 66.91  E-value: 6.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   238 KVSAGTSCVKWEeQTSEQVLRLHLAIgDIVP-LQTLWMENTVKLLDLVEVNNSILADPkvmgqtvtpGSVVYHRPSQmLL 316
Cdd:pfam02911   1 KIKKEDGRIDWN-QPAEEIHRLIRAL-DPWPgAYTFLNGKRVKLLKASVLDQESGAAP---------GTIVTVDKGG-LL 68

                          90       100       110
                  ....*....|....*....|....*....|.
gi 57528326   317 VHCKDGWIGVRSIM--HKKTLTATDFYNGYL 345
Cdd:pfam02911  69 VACGDGALLILELQleGKKPMSAEDFLNGFR 99
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 112-201 5.58e-13

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: 66.98  E-value: 5.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 112 EYDVGVV--ASFGRLLSEALILKFPYGILNVHPSCLPRWRGpapiIHT---VL-HGDTVTGVTIMQVRPKrFDVGPILKQ 185
Cdd:COG0299  78 AYGPDLVvlAGFMRILTPEFVRAFPGRIINIHPSLLPAFPG----LHAhrqALeAGVKVTGCTVHFVDEE-VDTGPIIAQ 152

                        90
                ....*....|....*.
gi 57528326 186 ETVAVPPKSTSKELEA 201
Cdd:COG0299 153 AAVPVLPDDTEETLAA 168
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 44-218 1.28e-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: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 64.93  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFF-GTDHFAREALRALHAArdnkeeklIEKLEVVTVPSIspKGLPVKQyAIQSQLPvyewpdmgsgeyDVgVVASFG 122
Cdd:cd08653   1 RIVLLtGDDPSHLYLANALLDA--------FGGVGVIVVNSI--NGPEVVA-ALRALAP------------DV-VSVYGC 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 123 RLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTV-TGVTIMQVRPkRFDVGPILKQETVAVPPKSTSKELEA 201
Cdd:cd08653  57 GIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVTVHLVDA-GIDTGDVLAQARPPLAAGDTLLSLYL 135

                       170
                ....*....|....*..
gi 57528326 202 VLSKLGANMLISVLKNL 218
Cdd:cd08653 136 RLYRAGVELMVEAIADL 152
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 112-201 3.01e-12

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: 64.72  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 112 EYDVGVV--ASFGRLLSEALILKFPYGILNVHPSCLPRWRGpapiIHT---VL-HGDTVTGVTIMQVRPKrFDVGPILKQ 185
Cdd:cd08645  76 EYKVDLIvlAGFMRILSPEFLEAFPGRIINIHPSLLPKFYG----LHAheaALeAGVKVTGCTVHFVDEE-VDTGPIIAQ 150

                        90
                ....*....|....*.
gi 57528326 186 ETVAVPPKSTSKELEA 201
Cdd:cd08645 151 AAVPVLPGDTPETLAE 166
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 44-218 7.59e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 63.44  E-value: 7.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFFGTDHFAREALRALHAARDN-------KEEKLIEKLEVVTVPSISPK-GLPVKQYAIQSQLPVYEWpdMGSGEYDV 115
Cdd:cd08651   1 RIVFIGCVEFSLIALEAILEAGGEvvgvitlDDSSSNNDSDYLDLDSFARKnGIPYYKFTDINDEEIIEW--IKEANPDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 116 GVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVrPKRFDVGPILKQETVAVPPKST 195
Cdd:cd08651  79 IFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWM-DEGADSGDILSQEPFPIDKDDT 157

                       170       180
                ....*....|....*....|...
gi 57528326 196 SKELEAVLSKLGANMLISVLKNL 218
Cdd:cd08651 158 ANSLYDKIMEAAKQQIDKFLPRL 180
PRK06988 PRK06988
formyltransferase;
134-198 1.39e-10

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 61.63  E-value: 1.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57528326  134 PYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTI--MQVRPkrfDVGPILKQETVAVPPKSTSKE 198
Cdd:PRK06988  99 PRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLheMVAKP---DAGAIVDQTAVPILPDDTAAQ 162
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 78-237 5.08e-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: 58.61  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  78 VVTVPSISPKGLPVKQYAIQSQLPVYEWPD-MGSGEYDVGVVASFGRLLSEALILKF-----PYGILNV--------HPS 143
Cdd:cd08647  29 VFTIPDKDGKADPLALEAEKDGVPVFKFPRwRAKGQAIPEVVAKYKALGAELNVLPFcsqfiPMEVIDApkhgsiiyHPS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 144 CLPRWRGPAPIIHTVLHGDTVTGVTIMQVrPKRFDVGPILKQETVAVPPKSTSKEL-EAVLSKLGANMLISVLKNLPESL 222
Cdd:cd08647 109 ILPRHRGASAINWTLIHGDKKAGFTIFWA-DDGLDTGPILLQKECDVLPNDTVDTLyNRFLYPEGIKAMVEAVRLIAEGK 187

                       170
                ....*....|....*
gi 57528326 223 NNGRPQPAEGVTYAP 237
Cdd:cd08647 188 APRIPQPEEGATYEG 202
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 44-199 1.01e-07

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: 51.29  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  44 RVLFFGTDHFAREALRALHAARDNKEEKLIEkleVVTvpsiSPKGLPVKQ-----YAIQSQLPVYEWPD--MGSGEYDVG 116
Cdd:cd08820   1 RIVFLGQKPIGEECLRTLLRLQDRGSFEIIA---VLT----NTSPADVWEgseplYDIGSTERNLHKLLeiLENKGVDIL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326 117 VVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQVrPKRFDVGPILKQETVAVPPKSTS 196
Cdd:cd08820  74 ISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWM-AEGIDSGDIIFEKRFPIPSDCTV 152


                ...
gi 57528326 197 KEL 199
Cdd:cd08820 153 ISL 155
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 58-201 1.05e-07

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 52.00  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326   58 LRALHAArdnKEEKLIEKlEVVTVPSISPkGLPVKQYAIQSQLPVYEWPDMGSG--------------EYDVGVV--ASF 121
Cdd:PLN02331  13 FRAIHDA---CLDGRVNG-DVVVVVTNKP-GCGGAEYARENGIPVLVYPKTKGEpdglspdelvdalrGAGVDFVllAGY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57528326  122 GRLLSEALILKFPYGILNVHPSCLPRWRGPApiihtvLHGDTV-----------TGVTIMQVRPKrFDVGPILKQETVAV 190
Cdd:PLN02331  88 LKLIPVELVRAYPRSILNIHPALLPAFGGKG------YYGIKVhkaviasgarySGPTVHFVDEH-YDTGRILAQRVVPV 160

                        170
                 ....*....|.
gi 57528326  191 PPKSTSKELEA 201
Cdd:PLN02331 161 LATDTPEELAA 171
 
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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