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Conserved domains on  [gi|1694913894|ref|WP_140604494|]
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methionyl-tRNA formyltransferase [Litorilituus lipolyticus]

Protein Classification

methionyl-tRNA formyltransferase( domain architecture ID 11415469)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-320 1.88e-159

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


:

Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 447.63  E-value: 1.88e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:COG0223     1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:COG0223    81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYIPWPVAQFT 244
Cdd:COG0223   161 AGSLHDKLAELGAELLLETLDALEAGTLTPTP----QDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTT 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1694913894 245 FTEEnekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSAIRLLKLQLPGKKPLTVAELLNGRSewFQVG 320
Cdd:COG0223   237 LDGK-----RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPG 305
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-320 1.88e-159

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 447.63  E-value: 1.88e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:COG0223     1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:COG0223    81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYIPWPVAQFT 244
Cdd:COG0223   161 AGSLHDKLAELGAELLLETLDALEAGTLTPTP----QDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTT 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1694913894 245 FTEEnekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSAIRLLKLQLPGKKPLTVAELLNGRSewFQVG 320
Cdd:COG0223   237 LDGK-----RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPG 305
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-323 5.06e-108

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: 317.42  E-value: 5.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:TIGR00460  81 VIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYIPWPVAQFT 244
Cdd:TIGR00460 161 SGTLSDKLSELGAQLLIETLKELPEGKNKPEP----QDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAWLT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 245 FTEENEKQHRIRVWSAAaeqySGKETAGTILSADKAGILVAT-NNSAIRLLKLQLPGKKPLTVAELLNG-RSEWFQVGNN 322
Cdd:TIGR00460 237 FEGKNIKIHKAKVIDLS----TYKAKPGEIVYHNKKGILVACgKDGILLLLSLQPPGKKVMRAEDFYNGsRHPWYVPGSS 312


                  .
gi 1694913894 323 I 323
Cdd:TIGR00460 313 A 313
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 5-212 1.52e-106

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: 309.37  E-value: 1.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:cd08646     1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDEEFLEELKALKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:cd08646    81 LIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKL 212
Cdd:cd08646   161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVP----QDESEATYAPKI 204
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 6-312 3.18e-59

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 193.37  E-value: 3.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   6 NIIFAGTPDFAAQHLAALI------NSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQ---PKNFKELSAQQ 76
Cdd:PLN02285    8 RLVFLGTPEVAATVLDALLdasqapDSAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPPDLiftPEKAGEEDFLS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  77 TLAGYNADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKST 156
Cdd:PLN02285   88 ALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQER 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 157 CNISENDTSASLYEKLAQLGPKALLETL-DIMAAPSFDAikhNTVQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAY 235
Cdd:PLN02285  168 VEVDEDIKAPELLPLLFELGTKLLLRELpSVLDGSAKDK---ATPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 236 IPWPVAQFTF------TEENE----KQHRIRVWSAAAEQysgKETAGTILSADKAGILVATNNSAIRLLKLQLPGKKPLT 305
Cdd:PLN02285  245 AGWPGTRAKFqlvddgDGEREvlelKIITTRVCEAGGEQ---TGSADAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMK 321


                  ....*..
gi 1694913894 306 VAELLNG 312
Cdd:PLN02285  322 AKDFWNG 328
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-184 2.48e-54

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: 175.56  E-value: 2.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHH-NIVAVYCPPDKPAGRGKKLTACATKLLATEHNLpveQPKNFKELSAQQTLAGYNA 83
Cdd:pfam00551   4 AVLISGTGSNLQALIDALRKGGQDaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGL---TPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  84 DIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEND 163
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1694913894 164 TSASLYEKLAQLGPKALLETL 184
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
5-320 1.88e-159

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 447.63  E-value: 1.88e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:COG0223     1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPAGRGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:COG0223    81 LIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYIPWPVAQFT 244
Cdd:COG0223   161 AGSLHDKLAELGAELLLETLDALEAGTLTPTP----QDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAFTT 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1694913894 245 FTEEnekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSAIRLLKLQLPGKKPLTVAELLNGRSewFQVG 320
Cdd:COG0223   237 LDGK-----RLKIWKARVLEEAGGGAPGTILAVDKDGLLVACGDGALRLLELQPAGKKRMSAADFLRGYR--LKPG 305
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 5-323 5.06e-108

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: 317.42  E-value: 5.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAGRGKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:TIGR00460  81 VIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYIPWPVAQFT 244
Cdd:TIGR00460 161 SGTLSDKLSELGAQLLIETLKELPEGKNKPEP----QDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAWLT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 245 FTEENEKQHRIRVWSAAaeqySGKETAGTILSADKAGILVAT-NNSAIRLLKLQLPGKKPLTVAELLNG-RSEWFQVGNN 322
Cdd:TIGR00460 237 FEGKNIKIHKAKVIDLS----TYKAKPGEIVYHNKKGILVACgKDGILLLLSLQPPGKKVMRAEDFYNGsRHPWYVPGSS 312


                  .
gi 1694913894 323 I 323
Cdd:TIGR00460 313 A 313
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 5-212 1.52e-106

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: 309.37  E-value: 1.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNAD 84
Cdd:cd08646     1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPRGRGKKLTPSPVKELALELGLPVLQPEKLKDEEFLEELKALKPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:cd08646    81 LIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1694913894 165 SASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKL 212
Cdd:cd08646   161 AGELLDKLAELGADLLLEVLDDIEAGKLNPVP----QDESEATYAPKI 204
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 6-312 3.18e-59

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 193.37  E-value: 3.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   6 NIIFAGTPDFAAQHLAALI------NSHHNIVAVYCPPDKPAGRGKKLTACATKLLATEHNLPVEQ---PKNFKELSAQQ 76
Cdd:PLN02285    8 RLVFLGTPEVAATVLDALLdasqapDSAFEVAAVVTQPPARRGRGRKLMPSPVAQLALDRGFPPDLiftPEKAGEEDFLS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  77 TLAGYNADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKST 156
Cdd:PLN02285   88 ALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQER 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 157 CNISENDTSASLYEKLAQLGPKALLETL-DIMAAPSFDAikhNTVQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAY 235
Cdd:PLN02285  168 VEVDEDIKAPELLPLLFELGTKLLLRELpSVLDGSAKDK---ATPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 236 IPWPVAQFTF------TEENE----KQHRIRVWSAAAEQysgKETAGTILSADKAGILVATNNSAIRLLKLQLPGKKPLT 305
Cdd:PLN02285  245 AGWPGTRAKFqlvddgDGEREvlelKIITTRVCEAGGEQ---TGSADAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMK 321


                  ....*..
gi 1694913894 306 VAELLNG 312
Cdd:PLN02285  322 AKDFWNG 328
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 5-184 2.48e-54

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: 175.56  E-value: 2.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHH-NIVAVYCPPDKPAGRGKKLTACATKLLATEHNLpveQPKNFKELSAQQTLAGYNA 83
Cdd:pfam00551   4 AVLISGTGSNLQALIDALRKGGQDaDVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGL---TPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  84 DIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEND 163
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|.
gi 1694913894 164 TSASLYEKLAQLGPKALLETL 184
Cdd:pfam00551 161 TAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-185 1.83e-48

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: 160.15  E-value: 1.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   7 IIFAGTPDFAAQHLAALINS-HHNIVAVYCPPDKPAGRGKKLtacatklLATEHNLPVEQPKNFKELSAQqTLAGYNADI 85
Cdd:cd08369     1 IVILGSGNIGQRVLKALLSKeGHEIVGVVTHPDSPRGTAQLS-------LELVGGKVYLDSNINTPELLE-LLKEFAPDL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  86 MVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTS 165
Cdd:cd08369    73 IVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTA 152

                         170       180
                  ....*....|....*....|
gi 1694913894 166 ASLYEKLAQLGPKALLETLD 185
Cdd:cd08369   153 GTLYQRLIELGPKLLKEALQ 172
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 7-278 9.64e-44

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 158.99  E-value: 9.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   7 IIFAgTPDFAAQHLAALINSHHNIVAVYCPPDKPagrGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNADIM 86
Cdd:PRK08125    4 VVFA-YHDIGCVGIEALLAAGYEIAAVFTHTDNP---GENHFFGSVARLAAELGIPVYAPEDVNHPLWVERIRELAPDVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  87 VVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSA 166
Cdd:PRK08125   80 FSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 167 SLYEKLAQLGPKALLETLDIMAAPSFDAikhnTVQDNVQATYAHKLDKAEAELDWQLDAATLNRKIRAYI-PWPVAqFTF 245
Cdd:PRK08125  160 TLHHKLCHAARQLLEQTLPAIKHGNIPE----IPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAVTdPWPGA-FSY 234

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1694913894 246 TEEnekqHRIRVWSAAAEQYSGKETAGTILSAD 278
Cdd:PRK08125  235 VGE----QKFTVWSSRVLPDASGAQPGTVLSVA 263
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 20-211 1.68e-33

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: 122.45  E-value: 1.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  20 LAALINSHHNIVAVYCPPDKPagrGKKLTACATKLLATEHNLPVEQPKNFKELSAQQTLAGYNADIMVVVAYGLLLPEVI 99
Cdd:cd08644    16 LEALLAAGFEVVAVFTHTDNP---GENIWFGSVAQLAREHGIPVFTPDDINHPEWVERLRALKPDLIFSFYYRHMISEDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 100 LSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEKLAQLGPKA 179
Cdd:cd08644    93 LEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLCVAARRL 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1694913894 180 LLETLdimaapsfDAIKHNTV----QDNVQATYAHK 211
Cdd:cd08644   173 LARTL--------PALKAGKArerpQDETQASYFGG 200
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
211-313 1.81e-29

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 108.52  E-value: 1.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 211 KLDKAEAELDWQLDAATLNRKIRAYIPWPVAqFTFTEENekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSA 290
Cdd:pfam02911   1 KIKKEDGRIDWNQPAEEIHRLIRALDPWPGA-YTFLNGK----RVKLLKASVLDQESGAAPGTIVTVDKGGLLVACGDGA 75

                          90       100
                  ....*....|....*....|...
gi 1694913894 291 IRLLKLQLPGKKPLTVAELLNGR 313
Cdd:pfam02911  76 LLILELQLEGKKPMSAEDFLNGF 98
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 215-306 4.78e-28

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: 104.15  E-value: 4.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 215 AEAELDWQLDAATLNRKIRAYIPWPVAQFTFTEEnekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSAIRLL 294
Cdd:cd08704     1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGK-----RLKILKAEVLEESGEAAPGTILAVDKKGLLVACGDGALEIL 75

                          90
                  ....*....|..
gi 1694913894 295 KLQLPGKKPLTV 306
Cdd:cd08704    76 ELQPEGKKRMSA 87
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 6-180 8.56e-26

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: 101.19  E-value: 8.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   6 NIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRgkKLTACATKLLATEHNLPVeqpKNFKELSAQQTLA---GYN 82
Cdd:cd08651     1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNN--DSDYLDLDSFARKNGIPY---YKFTDINDEEIIEwikEAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  83 ADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEN 162
Cdd:cd08651    76 PDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKD 155

                         170
                  ....*....|....*...
gi 1694913894 163 DTSASLYEKLAQLGPKAL 180
Cdd:cd08651   156 DTANSLYDKIMEAAKQQI 173
PRK06988 PRK06988
formyltransferase;
55-309 4.45e-23

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 97.07  E-value: 4.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  55 LATEHNLPVEQPKNFKELSAQQTLAGYNADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIE 134
Cdd:PRK06988   50 VAAEHGIPVITPADPNDPELRAAVAAAAPDFIFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 135 TGVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEKLAQLGPKALLETLDIMAAPSFDAIKhntvQDNVQATYAHKLDK 214
Cdd:PRK06988  130 TGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPALLAGEAPHLP----NDLAQGSYFGGRKP 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 215 AEAELDWQLDAATLNRKIRAYI-PWPVAqftFTEENEKqhRIRVWSAaaeqySGKETAGTILSADKAGILVATN------ 287
Cdd:PRK06988  206 EDGRIDWSKPAAQVYNLIRAVApPYPGA---FTDLGGT--RFVVARA-----RLAAPGAAAARDLPPGLHVSDNalfgvc 275

                         250       260
                  ....*....|....*....|....*..
gi 1694913894 288 --NSAIRLLKL---QLPGKKPLTVAEL 309
Cdd:PRK06988  276 gdGRAVSILELrrqQDGGETVVTPAQF 302
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 28-188 7.68e-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: 7.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  28 HNIVAVYCPPDKpAGRGKKLTACATKllateHNLPVEQPKNF--KELSAQQTLAGYN---ADIMVVVAYGLLLPEVILST 102
Cdd:cd08647    24 HEVVGVFTIPDK-DGKADPLALEAEK-----DGVPVFKFPRWraKGQAIPEVVAKYKalgAELNVLPFCSQFIPMEVIDA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 103 PKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEK-LAQLGPKALL 181
Cdd:cd08647    98 PKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNRfLYPEGIKAMV 177


                  ....*..
gi 1694913894 182 ETLDIMA 188
Cdd:cd08647   178 EAVRLIA 184
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 83-188 5.15e-19

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


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 82.88  E-value: 5.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  83 ADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEN 162
Cdd:cd08823    72 ADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPD 151

                          90       100
                  ....*....|....*....|....*.
gi 1694913894 163 DTSASLYEKLAQLGPKALLETLDIMA 188
Cdd:cd08823   152 DTYGLLCSRLAMLAVGLLEELYQNLA 177
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 5-209 2.52e-17

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


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 78.66  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   5 LNIIFAGTPDFAAQHLAALINSHHNIVAVYCPPDKPAGRGKKLTAcatkllaTEHNLPVEQPKnfkeLSAQQTLAGyNAD 84
Cdd:cd08822     1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLAAAARTA-------GSRGLPRAGVA----VLPADAIPP-GTD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  85 IMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDT 164
Cdd:cd08822    69 LIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDT 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1694913894 165 SASLYEK-LAQLGPKALLETLDimaapsfDAIKHNTV----QDNVQATYA 209
Cdd:cd08822   149 AAELWRRaLAPMGVKLLTQVID-------ALLRGGNLpaqpQDERLATWE 191
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 63-176 8.26e-17

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


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 76.10  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  63 VEQPKNFKELSAQQTLAGYNADImVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIE-TGVTIMQ 141
Cdd:cd08653    28 VIVVNSINGPEVVAALRALAPDV-VSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVTVHL 106

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1694913894 142 MDKGLDTGDMILKSTCNISENDTSASLYEKLAQLG 176
Cdd:cd08653   107 VDAGIDTGDVLAQARPPLAAGDTLLSLYLRLYRAG 141
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 20-189 1.62e-16

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: 76.61  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  20 LAALINSHHN------IVAVYCppDKPAGRGKKLtacatkllATEHNLPVE--QPKNFKELSA-----QQTLAGYNADIm 86
Cdd:COG0299    15 LQALIDAIEAgdlpaeIVLVIS--NRPDAYGLER--------ARAAGIPTFvlDHKDFPSREAfdaalLEALDAYGPDL- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  87 VVVA-YGLLLPEVILS--TPKLgcINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEND 163
Cdd:COG0299    84 VVLAgFMRILTPEFVRafPGRI--INIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDD 161

                         170       180
                  ....*....|....*....|....*.
gi 1694913894 164 TSASLYEKLAQLGPKALLETLDIMAA 189
Cdd:COG0299   162 TEETLAARILEQEHRLYPEAIRLLAE 187
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 20-184 3.12e-16

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: 75.50  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  20 LAALINSHHN------IVAVYCppDKPAGRGKKLtacatkllATEHNLPVE--QPKNFK---ELSAQ--QTLAGYNADIM 86
Cdd:cd08645    13 LQALIDAIKSgklnaeIVLVIS--NNPDAYGLER--------AKKAGIPTFviNRKDFPsreEFDEAllELLKEYKVDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  87 VVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSA 166
Cdd:cd08645    83 VLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPE 162

                         170
                  ....*....|....*...
gi 1694913894 167 SLYEKLAQLGPKALLETL 184
Cdd:cd08645   163 TLAERIHALEHRLYPEAI 180
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 7-171 4.27e-13

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 66.31  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894   7 IIFAGTPDFAAQHLAALINSHHN----IVAVYCPPDKPAGRgkkltACATKLLATEHNLPVEQpknfkelSAQQTLAGYN 82
Cdd:cd08820     2 IVFLGQKPIGEECLRTLLRLQDRgsfeIIAVLTNTSPADVW-----EGSEPLYDIGSTERNLH-------KLLEILENKG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  83 ADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISEN 162
Cdd:cd08820    70 VDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSD 149


                  ....*....
gi 1694913894 163 DTSASLYEK 171
Cdd:cd08820   150 CTVISLYIL 158
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
 218-309 9.91e-11

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: 57.63  E-value: 9.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 218 ELDWQLDAATLNRKIRA-YIPWPVAqFTFTEENekqhRIRVWSA-AAEQYSGKETAGTILSADKAGILVATNNSAIRLLK 295
Cdd:cd08702     4 LIDWRMSAREIYNLVRAvTKPYPGA-FTFVGGQ----KIKIWKArPVDDAFYNGEPGKVLSVDGDPLIVACGDGALEILE 78

                          90
                  ....*....|....
gi 1694913894 296 LQLPGKKPLTVAEL 309
Cdd:cd08702    79 AELDGGLPLAGEQL 92
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 30-172 2.95e-10

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: 58.54  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  30 IVAVYCppDKPAGRGKKLtacatkllATEHNLP--VEQPKNF-------KELSAQqtLAGYNADIMVVVAYGLLLPEVIL 100
Cdd:TIGR00639  30 VVLVIS--NKPDAYGLER--------AAQAGIPtfVLSLKDFpsreafdQAIIEE--LRAHEVDLVVLAGFMRILGPTFL 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1694913894 101 STPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEKL 172
Cdd:TIGR00639  98 SRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRI 169
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
107-199 1.74e-09

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 57.22  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 107 CINVHGSLLPKWRGAAPIQRSLeAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEKLAQLGPKALLETLDI 186
Cdd:PRK07579   88 CINIHPGFNPYNRGWFPQVFSI-INGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHFDA 166

                          90
                  ....*....|...
gi 1694913894 187 MAAPSFDAIKHNT 199
Cdd:PRK07579  167 IRDGSYTAKKPAT 179
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 56-176 3.07e-09

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: 55.34  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  56 ATEHNLPVEQPKNfkelSAQQTLAGYNADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIET 135
Cdd:cd08649    39 AAAEGIAVLEPGE----ALEELLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRH 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1694913894 136 GVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEKLAQLG 176
Cdd:cd08649   115 GVTWHRIEEGVDAGDILVQRPFDIAPDDTALSLNLKCYEAG 155
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 107-185 5.01e-09

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: 55.40  E-value: 5.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694913894 107 CINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKStcNISENDTSASLYEKLAQLGPKALLETLD 185
Cdd:cd08821    67 CVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKR--DLSLKGTAEEIYERASKISLKMIPELVT 143
FMT_C_like cd08370
Carboxy-terminal domain of Formyltransferase and similar domains; This family represents the ...
 223-297 1.02e-07

Carboxy-terminal domain of Formyltransferase and similar domains; This family represents the C-terminal domain of formyltransferase and similar proteins. This domain is found in a variety of enzymes with formyl transferase and alkyladenine DNA glycosylase activities. The proteins with formyltransferase function include methionyl-tRNA formyltransferase, ArnA, 10-formyltetrahydrofolate dehydrogenase and HypX proteins. Although most proteins with formyl transferase activity contain this C-terminal domain, prokaryotic glycinamide ribonucleotide transformylase (GART), a single domain protein, only contains the core catalytic domain. Thus, the C-terminal domain is not required for formyl transferase catalytic activity and may be involved in substrate binding. Some members of this family have shown nucleic acid binding capacity. The C-terminal domain of methionyl-tRNA formyltransferase is involved in tRNA binding. Alkyladenine DNA glycosylase is a distant member of this family with very low sequence similarity to other members. It catalyzes the first step in base excision repair (BER) by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site and shows ability to bind to DNA.


Pssm-ID: 187727  Cd Length: 73  Bit Score: 48.57  E-value: 1.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1694913894 223 LDAATLNRKIRAyIPWPvAQFTFTEENekqhRIRVWSAAAEQYSGKE--TAGTILSADKAGILVATNNSAIRLLKLQ 297
Cdd:cd08370     1 LDAESLERTIRA-LPYQ-GARLEIDGE----RVRLLEAEVVDDVTNEarHSGKILFVDYQCITVATGDGALLITALQ 71
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 59-171 2.86e-05

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: 44.09  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  59 HNLPVEqpKNFKELSAQQTLA---GYNADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIET 135
Cdd:cd08648    52 HHIPVT--KDTKAEAEAEQLElleEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLI 129

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1694913894 136 GVTIMQMDKGLDTGDMILKSTCNISENDTSASLYEK 171
Cdd:cd08648   130 GATAHYVTEELDEGPIIEQDVERVSHRDSVEDLVRK 165
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 82-185 6.88e-05

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 43.58  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  82 NADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISE 161
Cdd:PLN02828  147 GTDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSH 226

                          90       100
                  ....*....|....*....|....
gi 1694913894 162 NDTSASLYEKLAQLGPKALLETLD 185
Cdd:PLN02828  227 RDNLRSFVQKSENLEKQCLAKAIK 250
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 11-168 1.85e-03

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 38.91  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  11 GTPDFAAQHLAALINSHHNIVAVYCPpDKPAgrgkkltaCATKLLATEHNLPV-EQPKNFKE---LSAQQ---TLAGYNA 83
Cdd:PLN02331    9 GGSNFRAIHDACLDGRVNGDVVVVVT-NKPG--------CGGAEYARENGIPVlVYPKTKGEpdgLSPDElvdALRGAGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  84 DIMVVVAYGLLLP-EVILSTPKlGCINVHGSLLPKWRG---------AAPIqrslEAGDIETGVTIMQMDKGLDTGDMIL 153
Cdd:PLN02331   80 DFVLLAGYLKLIPvELVRAYPR-SILNIHPALLPAFGGkgyygikvhKAVI----ASGARYSGPTVHFVDEHYDTGRILA 154

                         170
                  ....*....|....*
gi 1694913894 154 KSTCNISENDTSASL 168
Cdd:PLN02331  155 QRVVPVLATDTPEEL 169
FMT_core_HypX_N cd08650
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...
 96-185 3.37e-03

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.


Pssm-ID: 187719 [Multi-domain]  Cd Length: 151  Bit Score: 37.60  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  96 PEVILSTPKlgCINVH-GslLPKWRGAAPIQRSLEAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSASLY-EKLA 173
Cdd:cd08650    61 PEEIWSNYP--CLIVHpG--IVGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYrGEVT 136

                          90
                  ....*....|..
gi 1694913894 174 QLGPKALLETLD 185
Cdd:cd08650   137 DAAVKAVLEAVE 148
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 55-176 4.13e-03

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 38.24  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894  55 LATEHNLPVEQPKNFKELSAQQTLAGYN------ADIMVVVAYGLLLPEVILSTPKLGCINVHGSLLPKWRGAAPIQRSL 128
Cdd:PRK13010  136 LAVQHDIPFHHLPVTPDTKAQQEAQILDlietsgAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAH 215

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1694913894 129 EAGDIETGVTIMQMDKGLDTGDMILKSTCNISENDTSaslyEKLAQLG 176
Cdd:PRK13010  216 ARGVKLIGATAHFVTDDLDEGPIIEQDVERVDHSYSP----EDLVAKG 259
FMT_C_OzmH_like cd08700
C-terminal subdomain of the Formyltransferase-like domain found in OzmH-like proteins; Domain ...
 219-311 6.85e-03

C-terminal subdomain of the Formyltransferase-like domain found in OzmH-like proteins; Domain found in OzmH-like proteins with similarity to the C-terminal domain of Formyltransferase. OzmH is one of the proteins involved in the synthesis of Oxazolomycin (OZM), which is a hybrid peptide-polyketide antibiotic that exhibits potent antitumor and antiviral activities. OzmH 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 phosphopantetheine (PP)-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187728  Cd Length: 100  Bit Score: 35.67  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694913894 219 LDWQLDAATLNRKIRA-----Y-IPWPVAQFTFTEEnekqhRIRVWSAAAEQYSGKETAGTILSADKAGILVATNNSAIR 292
Cdd:cd08700     5 LDFTRPAAELSALVRAldfggYwNPLCVAKILLADR-----VLLVGKAEVLAVSSGGAPGTVLAVDADGWTVATGDGAVR 79

                          90
                  ....*....|....*....
gi 1694913894 293 LLKLQLPGKKPLTVAELLN 311
Cdd:cd08700    80 LSGLTDLDGAAVDLAALAQ 98
 
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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