NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|938307554|gb|KPQ40867|]
View 

methionyl-tRNA formyltransferase [Phormidium sp. OSCR]

Protein Classification

methionyl-tRNA formyltransferase( domain architecture ID 11415469)

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

EC:  2.1.2.9
Gene Ontology:  GO:0004479|GO:0071951
PubMed:  8199241

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-331 1.22e-150

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


:

Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 425.29  E-value: 1.22e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAA-GHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDP-EFLEELRALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:COG0223   79 PDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFR 238
Cdd:COG0223  159 DTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALnpWPGAFTTLD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 239 GQSLKVKATVPLAEmyyeqlpeelvkplrswgdrlnPDSGEPAEVVQIIKNlGPVLQTGAGLLLLQEVQLAGKKTQSGWD 318
Cdd:COG0223  239 GKRLKIWKARVLEE----------------------AGGGAPGTILAVDKD-GLLVACGDGALRLLELQPAGKKRMSAAD 295
                        330
                 ....*....|...
gi 938307554 319 FANGTRLEMGEHL 331
Cdd:COG0223  296 FLRGYRLKPGERL 308
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-331 1.22e-150

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 425.29  E-value: 1.22e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAA-GHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDP-EFLEELRALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:COG0223   79 PDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFR 238
Cdd:COG0223  159 DTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALnpWPGAFTTLD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 239 GQSLKVKATVPLAEmyyeqlpeelvkplrswgdrlnPDSGEPAEVVQIIKNlGPVLQTGAGLLLLQEVQLAGKKTQSGWD 318
Cdd:COG0223  239 GKRLKIWKARVLEE----------------------AGGGAPGTILAVDKD-GLLVACGDGALRLLELQPAGKKRMSAAD 295
                        330
                 ....*....|...
gi 938307554 319 FANGTRLEMGEHL 331
Cdd:COG0223  296 FLRGYRLKPGERL 308
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
1-206 5.05e-104

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: 303.21  E-value: 5.05e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:cd08646    1 MRIVFMGTPDFAVPSLEALLKS-GHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDE-EFLEELKALK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:cd08646   79 PDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLI 206
Cdd:cd08646  159 DTAGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
1-329 1.16e-90

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: 273.51  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554    1 MNLIFLGTPQFAVPSLKTLIEHPqFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDN-FEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQL-EELPLVRELK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:TIGR00460  79 PDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFR 238
Cdd:TIGR00460 159 DNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALnpWPTAWLTFE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  239 GQSLKV-KATVPLAEMYyeqlpeelvkplrswgdrlnpdSGEPAEVV-----QIIKNLGpvlqtGAGLLLLQEVQLAGKK 312
Cdd:TIGR00460 239 GKNIKIhKAKVIDLSTY----------------------KAKPGEIVyhnkkGILVACG-----KDGILLLLSLQPPGKK 291
                         330
                  ....*....|....*..
gi 938307554  313 TQSGWDFANGTRLEMGE 329
Cdd:TIGR00460 292 VMRAEDFYNGSRHPWYV 308
PLN02285 PLN02285
methionyl-tRNA formyltransferase
2-324 3.12e-67

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 214.17  E-value: 3.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   2 NLIFLGTPQFAVPSLKTLI---EHP--QFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIP---VWQPQKiKKDVETL 73
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLdasQAPdsAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPpdlIFTPEK-AGEEDFL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  74 DKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKS 153
Cdd:PLN02285  87 SALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 154 SLEIHLLDNAWDVAARLAQDCGSLLVETL----QGLEAQTlqATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF 229
Cdd:PLN02285 167 RVEVDEDIKAPELLPLLFELGTKLLLRELpsvlDGSAKDK--ATPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAF 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 230 --YPNAVTEFRGQSLKVKATVPLAemyyeqlpeelVKPLRSwgdRLNPDSGEP---AEVVQIIKNLGPVLQTGAGLLLLQ 304
Cdd:PLN02285 245 agWPGTRAKFQLVDDGDGEREVLE-----------LKIITT---RVCEAGGEQtgsADAVTFKKDSLLVPCGGGTWLEVL 310
                        330       340
                 ....*....|....*....|
gi 938307554 305 EVQLAGKKTQSGWDFANGTR 324
Cdd:PLN02285 311 EVQPPGKKVMKAKDFWNGLR 330
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
1-182 1.94e-41

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: 142.43  E-value: 1.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554    1 MNLIFL--GTPQFAVPSLKTLIEHPQF-EVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGipvWQPqKIKKDVETLDKLR 77
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKG---LTP-RSLFDQELADALR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   78 NSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEI 157
Cdd:pfam00551  77 ALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPI 156
                         170       180
                  ....*....|....*....|....*
gi 938307554  158 HLLDNAWDVAARLAQDCGSLLVETL 182
Cdd:pfam00551 157 LPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-331 1.22e-150

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 425.29  E-value: 1.22e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAA-GHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDP-EFLEELRALN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:COG0223   79 PDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFR 238
Cdd:COG0223  159 DTAGSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALnpWPGAFTTLD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 239 GQSLKVKATVPLAEmyyeqlpeelvkplrswgdrlnPDSGEPAEVVQIIKNlGPVLQTGAGLLLLQEVQLAGKKTQSGWD 318
Cdd:COG0223  239 GKRLKIWKARVLEE----------------------AGGGAPGTILAVDKD-GLLVACGDGALRLLELQPAGKKRMSAAD 295
                        330
                 ....*....|...
gi 938307554 319 FANGTRLEMGEHL 331
Cdd:COG0223  296 FLRGYRLKPGERL 308
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
1-206 5.05e-104

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: 303.21  E-value: 5.05e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:cd08646    1 MRIVFMGTPDFAVPSLEALLKS-GHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDE-EFLEELKALK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:cd08646   79 PDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLI 206
Cdd:cd08646  159 DTAGELLDKLAELGADLLLEVLDDIEAGKLNPVPQDESEATYAPKI 204
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
1-329 1.16e-90

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: 273.51  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554    1 MNLIFLGTPQFAVPSLKTLIEHPqFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPVWQPQKIKKDvETLDKLRNSQ 80
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDN-FEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQL-EELPLVRELK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:TIGR00460  79 PDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFR 238
Cdd:TIGR00460 159 DNSGTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALnpWPTAWLTFE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  239 GQSLKV-KATVPLAEMYyeqlpeelvkplrswgdrlnpdSGEPAEVV-----QIIKNLGpvlqtGAGLLLLQEVQLAGKK 312
Cdd:TIGR00460 239 GKNIKIhKAKVIDLSTY----------------------KAKPGEIVyhnkkGILVACG-----KDGILLLLSLQPPGKK 291
                         330
                  ....*....|....*..
gi 938307554  313 TQSGWDFANGTRLEMGE 329
Cdd:TIGR00460 292 VMRAEDFYNGSRHPWYV 308
PLN02285 PLN02285
methionyl-tRNA formyltransferase
2-324 3.12e-67

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 214.17  E-value: 3.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   2 NLIFLGTPQFAVPSLKTLI---EHP--QFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIP---VWQPQKiKKDVETL 73
Cdd:PLN02285   8 RLVFLGTPEVAATVLDALLdasQAPdsAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPpdlIFTPEK-AGEEDFL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  74 DKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKS 153
Cdd:PLN02285  87 SALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 154 SLEIHLLDNAWDVAARLAQDCGSLLVETL----QGLEAQTlqATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF 229
Cdd:PLN02285 167 RVEVDEDIKAPELLPLLFELGTKLLLRELpsvlDGSAKDK--ATPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAF 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 230 --YPNAVTEFRGQSLKVKATVPLAemyyeqlpeelVKPLRSwgdRLNPDSGEP---AEVVQIIKNLGPVLQTGAGLLLLQ 304
Cdd:PLN02285 245 agWPGTRAKFQLVDDGDGEREVLE-----------LKIITT---RVCEAGGEQtgsADAVTFKKDSLLVPCGGGTWLEVL 310
                        330       340
                 ....*....|....*....|
gi 938307554 305 EVQLAGKKTQSGWDFANGTR 324
Cdd:PLN02285 311 EVQPPGKKVMKAKDFWNGLR 330
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
3-183 2.80e-45

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: 152.06  E-value: 2.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   3 LIFLGTPQFAVPSLKTLIEHPQFEVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGIPvwqpqkikkDVETLDKLRNSQAD 82
Cdd:cd08369    1 IVILGSGNIGQRVLKALLSKEGHEIVGVVTHPDSPRGTAQLSLELVGGKVYLDSNIN---------TPELLELLKEFAPD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  83 VFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDN 162
Cdd:cd08369   72 LIVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDT 151
                        170       180
                 ....*....|....*....|.
gi 938307554 163 AWDVAARLAQDCGSLLVETLQ 183
Cdd:cd08369  152 AGTLYQRLIELGPKLLKEALQ 172
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
1-202 4.34e-44

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: 150.19  E-value: 4.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRrgrGKTLIPSPVKTVAVDAGIPVWQPQKIKkDVETLDKLRNSQ 80
Cdd:cd08644    1 MKAVVFAYHEVGYRCLEALLAA-GFEVVAVFTHTDNP---GENIWFGSVAQLAREHGIPVFTPDDIN-HPEWVERLRALK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 ADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:cd08644   76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 938307554 161 DNAWDVAARLAQDCGSLLVETLQGLEAQTLQATPQDDEAATY 202
Cdd:cd08644  156 DTAKSLFHKLCVAARRLLARTLPALKAGKARERPQDETQASY 197
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
1-182 1.94e-41

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: 142.43  E-value: 1.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554    1 MNLIFL--GTPQFAVPSLKTLIEHPQF-EVSAVVTQPDKRRGRGKTLIPSPVKTVAVDAGipvWQPqKIKKDVETLDKLR 77
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKG---LTP-RSLFDQELADALR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   78 NSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEI 157
Cdd:pfam00551  77 ALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPI 156
                         170       180
                  ....*....|....*....|....*
gi 938307554  158 HLLDNAWDVAARLAQDCGSLLVETL 182
Cdd:pfam00551 157 LPDDTAETLYNRVADLEHKALPRVL 181
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
25-236 1.84e-40

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 150.13  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  25 FEVSAVVTQPDKRrgrGKTLIPSPVKTVAVDAGIPVWQPqkikKDVET---LDKLRNSQADVFVVVAYGQILSQEILEMP 101
Cdd:PRK08125  24 YEIAAVFTHTDNP---GENHFFGSVARLAAELGIPVYAP----EDVNHplwVERIRELAPDVIFSFYYRNLLSDEILQLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 102 RLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVAARLAQDCGSLLVET 181
Cdd:PRK08125  97 PAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQT 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 938307554 182 LQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRgfypnAVTE 236
Cdd:PRK08125 177 LPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVR-----AVTD 226
PRK06988 PRK06988
formyltransferase;
26-251 2.50e-35

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 130.20  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  26 EVSAVVTQPDkrrgrgktlipSP--------VKTVAVDAGIPVWQPQKIKkDVETLDKLRNSQADVFVVVAYGQILSQEI 97
Cdd:PRK06988  27 DVALVVTHED-----------NPteniwfgsVAAVAAEHGIPVITPADPN-DPELRAAVAAAAPDFIFSFYYRHMIPVDL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  98 LEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVAARLAQDCGSL 177
Cdd:PRK06988  95 LALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQT 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938307554 178 LVETLQGLEAQTLQATPQDDEAATYARLIEKSDYQLDWTRPAIALHNQVRGF---YPNAVTEFRGQSLKVKATVPLA 251
Cdd:PRK06988 175 LWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAVappYPGAFTDLGGTRFVVARARLAA 251
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
4-172 5.46e-29

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: 110.05  E-value: 5.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   4 IFLGTPQFAVPSLKTLIEHPqFEVSAVVTQPDKRRGR-GKTLIPSPVktvAVDAGIPVWQPQKIKkDVETLDKLRNSQAD 82
Cdd:cd08651    3 VFIGCVEFSLIALEAILEAG-GEVVGVITLDDSSSNNdSDYLDLDSF---ARKNGIPYYKFTDIN-DEEIIEWIKEANPD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  83 VFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDN 162
Cdd:cd08651   78 IIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDT 157
                        170
                 ....*....|
gi 938307554 163 AWDVAARLAQ 172
Cdd:cd08651  158 ANSLYDKIME 167
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
206-322 1.64e-20

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 84.63  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  206 IEKSDYQLDWTRPAIALHNQVRGF--YPNAVTEFRGQSLKVKATVPLaemyyeqlpeelvkplrswgdrLNPDSGEPAEV 283
Cdd:pfam02911   2 IKKEDGRIDWNQPAEEIHRLIRALdpWPGAYTFLNGKRVKLLKASVL----------------------DQESGAAPGTI 59
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 938307554  284 VQIIKNlGPVLQTGAGLLLLQEVQLAGKKTQSGWDFANG 322
Cdd:pfam02911  60 VTVDKG-GLLVACGDGALLILELQLEGKKPMSAEDFLNG 97
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
76-185 2.21e-20

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: 86.73  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  76 LRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSL 155
Cdd:cd08823   67 LRALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFT 146
                         90       100       110
                 ....*....|....*....|....*....|
gi 938307554 156 EIHLLDNAWDVAARLAQDCGSLLVETLQGL 185
Cdd:cd08823  147 PIHPDDTYGLLCSRLAMLAVGLLEELYQNL 176
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
69-172 7.96e-20

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: 84.57  E-value: 7.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  69 DVETLDKLRNSQADVfVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQ-TGMTTMQMDVGMDTG 147
Cdd:cd08653   36 GPEVVAALRALAPDV-VSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVTVHLVDAGIDTG 114
                         90       100
                 ....*....|....*....|....*
gi 938307554 148 AMLLKSSLEIHLLDNAWDVAARLAQ 172
Cdd:cd08653  115 DVLAQARPPLAAGDTLLSLYLRLYR 139
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
1-202 8.23e-20

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: 85.96  E-value: 8.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHPQfEVSAVVTQPDKRrgrGKtliPSPVKTVAVDAGIPVWQPQKIKKD----VETLDKL 76
Cdd:cd08647    1 MKIAVIGQSLFGQEVYKELRKEGH-EVVGVFTIPDKD---GK---ADPLALEAEKDGVPVFKFPRWRAKgqaiPEVVAKY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  77 RNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLE 156
Cdd:cd08647   74 KALGAELNVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 938307554 157 IHLLDNAWDVAARLaqdcgsLLVETLQGL-EAQTLQAT------PQDDEAATY 202
Cdd:cd08647  154 VLPNDTVDTLYNRF------LYPEGIKAMvEAVRLIAEgkapriPQPEEGATY 200
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
209-316 2.01e-18

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: 78.73  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 209 SDYQLDWTRPAIALHNQVRGF--YPNAVTEFRGQSLKVKATVPLAEmyyeqlpeelvkplrswgdrlnPDSGEPAEVVQI 286
Cdd:cd08704    1 EEGRIDWSKSAEEIHNLIRALnpWPGAYTTLNGKRLKILKAEVLEE----------------------SGEAAPGTILAV 58
                         90       100       110
                 ....*....|....*....|....*....|
gi 938307554 287 IKNlGPVLQTGAGLLLLQEVQLAGKKTQSG 316
Cdd:cd08704   59 DKK-GLLVACGDGALEILELQPEGKKRMSA 87
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
1-203 2.12e-14

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 70.57  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   1 MNLIFLGTPQFAVPSLKTLIEHpQFEVSAVVTQPDKRRGRGKTLipSPVKTVAVDAGIPVWQPQKIKKDVetldklrnsq 80
Cdd:cd08822    1 MKIAIAGQKWFGTAVLEALRAR-GIALLGVAAPEEGDRLAAAAR--TAGSRGLPRAGVAVLPADAIPPGT---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  81 aDVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLL 160
Cdd:cd08822   68 -DLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 938307554 161 DNAWDVAARLAQDCG-SLLVETLQGLEA-QTLQATPQDDEAATYA 203
Cdd:cd08822  147 DTAAELWRRALAPMGvKLLTQVIDALLRgGNLPAQPQDERLATWE 191
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
3-157 3.60e-11

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: 60.92  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   3 LIFLGTPQFAVPSLKTLIE---HPQFEVSAVVTQPDKRRGRgkTLIPSpvktvAVDAGIPVWQPQKIkkdvetLDKLRNS 79
Cdd:cd08820    2 IVFLGQKPIGEECLRTLLRlqdRGSFEIIAVLTNTSPADVW--EGSEP-----LYDIGSTERNLHKL------LEILENK 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938307554  80 QADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEI 157
Cdd:cd08820   69 GVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPI 146
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
57-163 9.77e-11

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: 59.58  E-value: 9.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  57 GIPVWQPqkikkdVETLDK-LRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGM 135
Cdd:cd08649   43 GIAVLEP------GEALEElLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGV 116
                         90       100
                 ....*....|....*....|....*...
gi 938307554 136 TTMQMDVGMDTGAMLLKSSLEIHLLDNA 163
Cdd:cd08649  117 TWHRIEEGVDAGDILVQRPFDIAPDDTA 144
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
26-183 2.68e-10

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: 58.55  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  26 EVSAVVT-QPDkrrgrgktlipSPVKTVAVDAGIPVW------QPQKIKKDVETLDKLRNSQADvFVVVA-YGQILSQEI 97
Cdd:cd08645   28 EIVLVISnNPD-----------AYGLERAKKAGIPTFvinrkdFPSREEFDEALLELLKEYKVD-LIVLAgFMRILSPEF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  98 LEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVAAR-LAQDCgS 176
Cdd:cd08645   96 LEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERiHALEH-R 174

                 ....*..
gi 938307554 177 LLVETLQ 183
Cdd:cd08645  175 LYPEAIK 181
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
20-183 1.64e-09

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


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 56.58  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  20 IEHPQF--EVSAVVT-QPDkrrgrgktlipSPVKTVAVDAGIPVW--QPQKIKK----DVETLDKLRNSQADvFVVVA-Y 89
Cdd:COG0299   22 IEAGDLpaEIVLVISnRPD-----------AYGLERARAAGIPTFvlDHKDFPSreafDAALLEALDAYGPD-LVVLAgF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  90 GQILSQEILE--MPRLgcINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVA 167
Cdd:COG0299   90 MRILTPEFVRafPGRI--INIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLA 167
                        170
                 ....*....|....*..
gi 938307554 168 AR-LAQDCgSLLVETLQ 183
Cdd:COG0299  168 ARiLEQEH-RLYPEAIR 183
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
53-170 6.63e-09

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: 54.68  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554   53 AVDAGIPVWQ------PQKIKKDVETLDKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCL 126
Cdd:TIGR00639  46 AAQAGIPTFVlslkdfPSREAFDQAIIEELRAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQAL 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 938307554  127 YHGEKQTGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVAARL 170
Cdd:TIGR00639 126 EAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRI 169
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
72-205 8.34e-08

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: 187723 [Multi-domain]  Cd Length: 211  Bit Score: 51.94  E-value: 8.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  72 TLDKLRNSQADVFVVVAYGQILSQEILEmpRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTTMQMDVGMDTGAMLL 151
Cdd:cd08821   36 SLEKLTQFNPEYIFFPHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYL 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 938307554 152 KSslEIHLLDNAWDVAARLAQDCGSLLVETLQgleaQTLQATPQDDEAATYARL 205
Cdd:cd08821  114 KR--DLSLKGTAEEIYERASKISLKMIPELVT----KKPKPIKQEGEPVTFKRR 161
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
58-143 1.81e-06

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


Pssm-ID: 187717 [Multi-domain]  Cd Length: 196  Bit Score: 47.94  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  58 IPVWQPQKIKKDVETLDKLRNSQADvFVVVA-YGQILSQEILEmpRLG--CINGHGSLLPKYRGAAPiqwclYH-----G 129
Cdd:cd08648   54 IPVTKDTKAEAEAEQLELLEEYGVD-LVVLArYMQILSPDFVE--RYPnrIINIHHSFLPAFKGAKP-----YHqaferG 125
                         90
                 ....*....|....*...
gi 938307554 130 EKQTGMT----TMQMDVG 143
Cdd:cd08648  126 VKLIGATahyvTEELDEG 143
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
58-147 3.25e-06

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 47.87  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  58 IPVWQPQKIKKDVETLDKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTT 137
Cdd:PRK13010 147 LPVTPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATA 226
                         90
                 ....*....|
gi 938307554 138 MQMDVGMDTG 147
Cdd:PRK13010 227 HFVTDDLDEG 236
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
210-316 4.88e-05

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. 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 domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that 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 C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.


Pssm-ID: 187730  Cd Length: 92  Bit Score: 41.46  E-value: 4.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554 210 DYQLDWTRPAIALHNQVRGF---YPNAVTEFRGQSLKVKATVPLAEmyyeqlpeelvkplrswgdrlNPDSGEPAEVVQI 286
Cdd:cd08702    2 DGLIDWRMSAREIYNLVRAVtkpYPGAFTFVGGQKIKIWKARPVDD---------------------AFYNGEPGKVLSV 60
                         90       100       110
                 ....*....|....*....|....*....|
gi 938307554 287 IKNlGPVLQTGAGLLLLQEVQLAGKKTQSG 316
Cdd:cd08702   61 DGD-PLIVACGDGALEILEAELDGGLPLAG 89
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
58-128 5.04e-05

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 44.20  E-value: 5.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938307554  58 IPVWQPQKIKKDVETLDKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPiqwclYH 128
Cdd:PRK13011 143 FPITPDTKPQQEAQVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKP-----YH 208
PLN02828 PLN02828
formyltetrahydrofolate deformylase
67-137 1.02e-03

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 40.11  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938307554  67 KKDVETLDKLRNSqaDVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAAPIQWCLYHGEKQTGMTT 137
Cdd:PLN02828 136 KREDEILELVKGT--DFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATS 204
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
53-169 3.48e-03

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 38.14  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938307554  53 AVDAGIPVWQPQKIKKDVETL------DKLRNSQADVFVVVAYGQILSQEILEMPRLGCINGHGSLLPKYRGAApiqwcl 126
Cdd:PLN02331  45 ARENGIPVLVYPKTKGEPDGLspdelvDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKG------ 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 938307554 127 YHGEKQ-----------TGMTTMQMDVGMDTGAMLLKSSLEIHLLDNAWDVAAR 169
Cdd:PLN02331 119 YYGIKVhkaviasgarySGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAAR 172
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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