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Conserved domains on  [gi|490296984|ref|WP_004192441|]
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MULTISPECIES: formyltransferase [pseudomallei group]

Protein Classification

formyltransferase( domain architecture ID 11482518)

formyltransferase catalyzes the addition of a formyl group to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06988 PRK06988
formyltransferase;
1-315 0e+00

formyltransferase;


:

Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 603.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:PRK06988   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPTENIWFGSVAAVAAEHGIPVITPADPNDPELRAAVAAAAPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:PRK06988  81 IFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVAPPYPGAFTDLGGT 240
Cdd:PRK06988 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAVAPPYPGAFTDLGGT 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296984 241 RFVIARARLAAPGTAAARAAvdlPPGLHVSDNALFGVCGDSRAVSILELRRPHDGGEAVVSPAQFAQFIHSSRHS 315
Cdd:PRK06988 241 RFVVARARLAAPGAAAARDL---PPGLHVSDNALFGVCGDGRAVSILELRRQQDGGETVVTPAQFAQFIHSSRHS 312
 
Name Accession Description Interval E-value
PRK06988 PRK06988
formyltransferase;
1-315 0e+00

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 603.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:PRK06988   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPTENIWFGSVAAVAAEHGIPVITPADPNDPELRAAVAAAAPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:PRK06988  81 IFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVAPPYPGAFTDLGGT 240
Cdd:PRK06988 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAVAPPYPGAFTDLGGT 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296984 241 RFVIARARLAAPGTAAARAAvdlPPGLHVSDNALFGVCGDSRAVSILELRRPHDGGEAVVSPAQFAQFIHSSRHS 315
Cdd:PRK06988 241 RFVVARARLAAPGAAAARDL---PPGLHVSDNALFGVCGDGRAVSILELRRQQDGGETVVTPAQFAQFIHSSRHS 312
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 3-205 4.74e-116

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: 333.16  E-value: 4.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   3 PRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDFIF 82
Cdd:cd08644    1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENIWFGSVAQLAREHGIPVFTPDDINHPEWVERLRALKPDLIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  83 SFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQ 162
Cdd:cd08644   81 SFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490296984 163 VFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKP 205
Cdd:cd08644  161 LFHKLCVAARRLLARTLPALKAGKARERPQDETQASYFGGRKP 203
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
4-307 6.62e-114

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 331.68  E-value: 6.62e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   4 RAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSP---TEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:COG0223    2 RIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:COG0223   82 IVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVApPYPGAFTDLGGT 240
Cdd:COG0223  162 GSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALN-PWPGAFTTLDGK 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296984 241 RFVIARARLAAPGTaaaraavDLPPG--LHVSDNALFGVCGDsRAVSILELRRPhdgGEAVVSPAQFAQ 307
Cdd:COG0223  241 RLKIWKARVLEEAG-------GGAPGtiLAVDKDGLLVACGD-GALRLLELQPA---GKKRMSAADFLR 298
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 4-314 4.19e-47

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: 160.64  E-value: 4.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984    4 RAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPT---EHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:TIGR00460  82 IVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVApPYPGAFTDLGGT 240
Cdd:TIGR00460 162 GTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALN-PWPTAWLTFEGK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296984  241 RFVIARARLAAPGTAAARaavdlpPGLHVSDN--ALFGVCGDSRAVSILELRRPhdgGEAVVSpaqFAQFIHSSRH 314
Cdd:TIGR00460 241 NIKIHKAKVIDLSTYKAK------PGEIVYHNkkGILVACGKDGILLLLSLQPP---GKKVMR---AEDFYNGSRH 304
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 25-179 1.11e-22

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: 92.74  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   25 GVDVALVVTHEDSP---TEHIWFGSVAAVAAEHGIAVITPADPAGADvraALASAKPDFIFSFYYRHMLPVDLLALAARG 101
Cdd:pfam00551  27 DADVVLVISNKDKAaglGRAEQAGIPTFVFEHKGLTPRSLFDQELAD---ALRALAADVIVLAGYMRILPPEFLQAPPGG 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296984  102 AYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQTLWRVL 179
Cdd:pfam00551 104 ILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
PRK06988 PRK06988
formyltransferase;
1-315 0e+00

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 603.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:PRK06988   1 MKPRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDNPTENIWFGSVAAVAAEHGIPVITPADPNDPELRAAVAAAAPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:PRK06988  81 IFSFYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVAPPYPGAFTDLGGT 240
Cdd:PRK06988 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAVAPPYPGAFTDLGGT 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296984 241 RFVIARARLAAPGTAAARAAvdlPPGLHVSDNALFGVCGDSRAVSILELRRPHDGGEAVVSPAQFAQFIHSSRHS 315
Cdd:PRK06988 241 RFVVARARLAAPGAAAARDL---PPGLHVSDNALFGVCGDGRAVSILELRRQQDGGETVVTPAQFAQFIHSSRHS 312
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 3-205 4.74e-116

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: 333.16  E-value: 4.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   3 PRAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDFIF 82
Cdd:cd08644    1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENIWFGSVAQLAREHGIPVFTPDDINHPEWVERLRALKPDLIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  83 SFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQ 162
Cdd:cd08644   81 SFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490296984 163 VFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKP 205
Cdd:cd08644  161 LFHKLCVAARRLLARTLPALKAGKARERPQDETQASYFGGRKP 203
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 1-280 6.35e-114

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 343.50  E-value: 6.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   1 MKprAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPTEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:PRK08125   1 MK--AVVFAYHDIGCVGIEALLAAGYEIAAVFTHTDNPGENHFFGSVARLAAELGIPVYAPEDVNHPLWVERIRELAPDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:PRK08125  79 IFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVAPPYPGAFTDLGGT 240
Cdd:PRK08125 159 LTLHHKLCHAARQLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAVTDPWPGAFSYVGEQ 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490296984 241 RFVIARARLAAPGTaaaraavDLPPGLHVSDNALFGVCGD 280
Cdd:PRK08125 239 KFTVWSSRVLPDAS-------GAQPGTVLSVAPLRIACGE 271
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
4-307 6.62e-114

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 331.68  E-value: 6.62e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   4 RAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSP---TEHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:COG0223    2 RIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRKLTPSPVKELALEHGIPVLQPESLKDPEFLEELRALNPDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:COG0223   82 IVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVApPYPGAFTDLGGT 240
Cdd:COG0223  162 GSLHDKLAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALN-PWPGAFTTLDGK 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296984 241 RFVIARARLAAPGTaaaraavDLPPG--LHVSDNALFGVCGDsRAVSILELRRPhdgGEAVVSPAQFAQ 307
Cdd:COG0223  241 RLKIWKARVLEEAG-------GGAPGtiLAVDKDGLLVACGD-GALRLLELQPA---GKKRMSAADFLR 298
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 4-314 4.19e-47

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: 160.64  E-value: 4.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984    4 RAVVFAYHNVGVRCLQVLLARGVDVALVVTHEDSPT---EHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDF 80
Cdd:TIGR00460   2 RIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgKKLTPPPVKVLAEEKGIPVFQPEKQRQLEELPLVRELKPDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   81 IFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:TIGR00460  82 IVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  161 AQVFDKVTVAAEQTLWRVLPALLAGEAPHLPNDLSQGSYYGGRKPEDGRIDWTQPAANVYNLIRAVApPYPGAFTDLGGT 240
Cdd:TIGR00460 162 GTLSDKLSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALN-PWPTAWLTFEGK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296984  241 RFVIARARLAAPGTAAARaavdlpPGLHVSDN--ALFGVCGDSRAVSILELRRPhdgGEAVVSpaqFAQFIHSSRH 314
Cdd:TIGR00460 241 NIKIHKAKVIDLSTYKAK------PGEIVYHNkkGILVACGKDGILLLLSLQPP---GKKVMR---AEDFYNGSRH 304
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 6-181 2.88e-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: 151.67  E-value: 2.88e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   6 VVFAYHNVGVRCLQVLL-ARGVDVALVVTHEDSPtehiwFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDFIFSF 84
Cdd:cd08369    2 VILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSP-----RGTAQLSLELVGGKVYLDSNINTPELLELLKEFAPDLIVSI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  85 YYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVF 164
Cdd:cd08369   77 NFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLY 156

                        170
                 ....*....|....*..
gi 490296984 165 DKVTVAAEQTLWRVLPA 181
Cdd:cd08369  157 QRLIELGPKLLKEALQK 173
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 15-199 3.17e-45

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: 152.60  E-value: 3.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  15 VRCLQVLLARGVDVALVVTHEDSPT---EHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDFIFSFYYRHMLP 91
Cdd:cd08646   13 VPSLEALLKSGHEVVAVVTQPDKPRgrgKKLTPSPVKELALELGLPVLQPEKLKDEEFLEELKALKPDLIVVVAYGQILP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  92 VDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAA 171
Cdd:cd08646   93 KEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLDKLAELG 172

                        170       180
                 ....*....|....*....|....*...
gi 490296984 172 EQTLWRVLPALLAGEAPHLPNDLSQGSY 199
Cdd:cd08646  173 ADLLLEVLDDIEAGKLNPVPQDESEATY 200
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 15-160 7.38e-34

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: 121.98  E-value: 7.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  15 VRCLQVLLARGVDVALVVTHEDSptehiwfgsVAAVAAEHGIAVITPadpaGADVRAALASAKPDFIFSFYYRHMLPVDL 94
Cdd:cd08649   12 IQCAEQLLAAGHRIAAVVSTDPA---------IRAWAAAEGIAVLEP----GEALEELLSDEPFDWLFSIVNLRILPSEV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296984  95 LALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTA 160
Cdd:cd08649   79 LALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTA 144
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 5-182 3.30e-32

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: 117.75  E-value: 3.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   5 AVVFAYHnvgvrCLQVLLARGVDVALVVTHEDSPT-EHIWFGSVAAVAAEHGIAVITPADPAGADVRAALASAKPDFIFS 83
Cdd:cd08651    7 CVEFSLI-----ALEAILEAGGEVVGVITLDDSSSnNDSDYLDLDSFARKNGIPYYKFTDINDEEIIEWIKEANPDIIFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  84 FYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQV 163
Cdd:cd08651   82 FGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSL 161

                        170
                 ....*....|....*....
gi 490296984 164 FDKVTVAAEQTLWRVLPAL 182
Cdd:cd08651  162 YDKIMEAAKQQIDKFLPRL 180
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 47-306 2.95e-25

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 103.23  E-value: 2.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  47 VAAVAAEHGIA---VITPADPAGADVRAALASAKPDFIFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAV 123
Cdd:PLN02285  60 VAQLALDRGFPpdlIFTPEKAGEEDFLSALRELQPDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGAAPVQRAL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 124 LNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPALLAGEAPH--LPNDLSQGSYYG 201
Cdd:PLN02285 140 QDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLLRELPSVLDGSAKDkaTPQDDSKATHAP 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 202 GRKPEDGRIDWTQPAANVYNLIRAVApPYPGAFTDL------GGTRFV----IARARLAAPGTAAARAAVDLPpglhVSD 271
Cdd:PLN02285 220 KISPEESWLSFDEEARVLHNKVRAFA-GWPGTRAKFqlvddgDGEREVlelkIITTRVCEAGGEQTGSADAVT----FKK 294

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 490296984 272 NALFGVCGDSRAVSILELRRPhdgGEAVVSPAQFA 306
Cdd:PLN02285 295 DSLLVPCGGGTWLEVLEVQPP---GKKVMKAKDFW 326
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
 206-288 4.22e-25

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: 96.54  E-value: 4.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 206 EDGRIDWTQPAANVYNLIRAVAPPYPGAFTDLGGTRFVIARARLaapgtaAARAAVDLPPGLHVS--DNALFGVCGDSrA 283
Cdd:cd08702    1 EDGLIDWRMSAREIYNLVRAVTKPYPGAFTFVGGQKIKIWKARP------VDDAFYNGEPGKVLSvdGDPLIVACGDG-A 73


                 ....*
gi 490296984 284 VSILE 288
Cdd:cd08702   74 LEILE 78
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 25-179 1.11e-22

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: 92.74  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   25 GVDVALVVTHEDSP---TEHIWFGSVAAVAAEHGIAVITPADPAGADvraALASAKPDFIFSFYYRHMLPVDLLALAARG 101
Cdd:pfam00551  27 DADVVLVISNKDKAaglGRAEQAGIPTFVFEHKGLTPRSLFDQELAD---ALRALAADVIVLAGYMRILPPEFLQAPPGG 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296984  102 AYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQTLWRVL 179
Cdd:pfam00551 104 ILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNRVADLEHKALPRVL 181
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 75-159 5.15e-21

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: 88.27  E-value: 5.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  75 SAKPDFIFSFYYRhmLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPI 154
Cdd:cd08823   71 AADTVVVFTFPYR--IPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPI 148


                 ....*
gi 490296984 155 LPDDT 159
Cdd:cd08823  149 HPDDT 153
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 55-179 5.50e-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: 5.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  55 GIAVITPADPAGADVRAALASAKPDFIfSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETE-TGAT 133
Cdd:cd08653   25 GVGVIVVNSINGPEVVAALRALAPDVV-SVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDPDnVGVT 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490296984 134 LHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQTLWRVL 179
Cdd:cd08653  104 VHLVDAGIDTGDVLAQARPPLAAGDTLLSLYLRLYRAGVELMVEAI 149
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
204-307 5.18e-19

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 80.40  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  204 KPEDGRIDWTQPAANVYNLIRAVaPPYPGAFTDLGGTRFVIARARLAAPGTaaaraavDLPPG--LHVSDNALFGVCGDs 281
Cdd:pfam02911   3 KKEDGRIDWNQPAEEIHRLIRAL-DPWPGAYTFLNGKRVKLLKASVLDQES-------GAAPGtiVTVDKGGLLVACGD- 73

                          90       100
                  ....*....|....*....|....*.
gi 490296984  282 RAVSILELRRPhdgGEAVVSPAQFAQ 307
Cdd:pfam02911  74 GALLILELQLE---GKKPMSAEDFLN 96
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 206-292 8.30e-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: 76.80  E-value: 8.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 206 EDGRIDWTQPAANVYNLIRAVApPYPGAFTDLGGTRFVIARARLAAPGTAAARAAVdlppgLHVSDNALFGVCGDSrAVS 285
Cdd:cd08704    1 EEGRIDWSKSAEEIHNLIRALN-PWPGAYTTLNGKRLKILKAEVLEESGEAAPGTI-----LAVDKKGLLVACGDG-ALE 73


                 ....*..
gi 490296984 286 ILELRRP 292
Cdd:cd08704   74 ILELQPE 80
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 16-171 1.25e-15

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 73.24  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  16 RCLQVLLARG-VDVALVVTheDSPTEHIWFGSVAAVAAEHGIAVITPADpagadvrAALASAKPDFIFSFYYRHMLPVDL 94
Cdd:cd08820   16 RTLLRLQDRGsFEIIAVLT--NTSPADVWEGSEPLYDIGSTERNLHKLL-------EILENKGVDILISVQYHWILPGSI 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296984  95 LALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAA 171
Cdd:cd08820   87 LEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYILAHYAA 163
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 25-186 4.81e-15

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: 72.37  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  25 GVDVALVVT-HEDSPtehiwfgsVAAVAAEHGI--AVITPADPA-----GADVRAALASAKPDFIFSFYYRHMLPVDLLA 96
Cdd:COG0299   28 PAEIVLVISnRPDAY--------GLERARAAGIptFVLDHKDFPsreafDAALLEALDAYGPDLVVLAGFMRILTPEFVR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  97 laargAY-----NMHGSLLPKYRGRvPTNWAVL-NGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVA 170
Cdd:COG0299  100 -----AFpgriiNIHPSLLPAFPGL-HAHRQALeAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARILEQ 173

                        170
                 ....*....|....*.
gi 490296984 171 AEQTLWRVLPALLAGE 186
Cdd:COG0299  174 EHRLYPEAIRLLAEGR 189
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 51-185 5.33e-14

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: 69.32  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   51 AAEHGIA--VITPADPAG-----ADVRAALASAKPDFIFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAV 123
Cdd:TIGR00639  46 AAQAGIPtfVLSLKDFPSreafdQAIIEELRAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQAL 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296984  124 LNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQTLWRVLPALLAG 185
Cdd:TIGR00639 126 EAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQG 187
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 14-177 1.05e-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: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 62.86  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  14 GVRCLQVLLARGVDVALVVTHEDSptehiwfgsvAAVAAEHGIAVITPADPAGADVRAALASAKP-DFIFSFYYRHMLPV 92
Cdd:cd08822   12 GTAVLEALRARGIALLGVAAPEEG----------DRLAAAARTAGSRGLPRAGVAVLPADAIPPGtDLIVAAHCHAFISA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  93 DLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAaqvfdkvtvaae 172
Cdd:cd08822   82 KTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA------------ 149


                 ....*
gi 490296984 173 QTLWR 177
Cdd:cd08822  150 AELWR 154
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 27-182 2.23e-11

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 62.02  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  27 DVALVVTheDSPTehiwfGSVAAVAAEHGIAVITPADPAGA-------DVRAALASAKPDFIFSFYYRHMLPVDLLALAA 99
Cdd:PLN02331  28 DVVVVVT--NKPG-----CGGAEYARENGIPVLVYPKTKGEpdglspdELVDALRGAGVDFVLLAGYLKLIPVELVRAYP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 100 RGAYNMHGSLLPKYRGR----VPTNWAVLN-GETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDKVTVAAEQT 174
Cdd:PLN02331 101 RSILNIHPALLPAFGGKgyygIKVHKAVIAsGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEEHQL 180


                 ....*...
gi 490296984 175 LWRVLPAL 182
Cdd:PLN02331 181 YVEVVAAL 188
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 70-249 1.12e-07

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


Pssm-ID: 187723 [Multi-domain]  Cd Length: 211  Bit Score: 51.55  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  70 RAALASAKPDFIFSFYYRHMLPVDLLAlaargayN-----MHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAG 144
Cdd:cd08821   37 LEKLTQFNPEYIFFPHWSWIIPKEIFE-------NfecvvFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 145 AIVGQTAVPILpdDTAAQVFDKvtvaAEQTLWRVLPALLAgeapHLPNDLSQ---GSYYGGRKPEDGRIDWTQPAANVYN 221
Cdd:cd08821  110 PIYLKRDLSLK--GTAEEIYER----ASKISLKMIPELVT----KKPKPIKQegePVTFKRRTPEQSNISNEANLEKIYD 179

                        170       180
                 ....*....|....*....|....*....
gi 490296984 222 LIRAV-APPYPGAFTDLGGTRFVIARARL 249
Cdd:cd08821  180 FIRMLdADGYPSAFIELGNYRIEFSRASL 208
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
79-245 2.82e-07

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 50.67  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  79 DFIFSFYYRHMLPVDLLAlAARgAYNMHGSLLPKYRGRVPTNWAVLNGEtETGATLHEMAAKPDAGAIVGQTAVPILPDD 158
Cdd:PRK07579  67 DLVLSFHCKQRFPAKLVN-GVR-CINIHPGFNPYNRGWFPQVFSIINGL-KIGATIHEMDEQLDHGPIIAQREVEIESWD 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984 159 TAAQVFDKVTVAAEQTLWRVLPALLAGEAPHL-PNdlSQGSYYGGRKPEDGR---IDWTQPAANVYNLIRAVA-PPYPGA 233
Cdd:PRK07579 144 SSGSVYARVMDIERELVLEHFDAIRDGSYTAKkPA--TEGNLNSKKDFKQLReidLDERGTFRHFINRLRALThDDYKNA 221

                        170
                 ....*....|...
gi 490296984 234 -FTDLGGTRFVIA 245
Cdd:PRK07579 222 yFVDESGRKVFVR 234
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 90-166 2.12e-05

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: 44.75  E-value: 2.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296984  90 LPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVFDK 166
Cdd:cd08647   90 IPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNR 166
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
 3-161 2.37e-04

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: 41.39  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984   3 PRAVVFA---YHnvgvrCLQVLLAR------GVDVALVVT-HEDsptehiwfgsVAAVAAEHGIAV----ITPADPAGAD 68
Cdd:cd08648    1 KRVAIFVskeDH-----CLYDLLHRwregelPCEIPLVISnHPD----------LRPLAERFGIPFhhipVTKDTKAEAE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  69 --VRAALASAKPDFIFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAI 146
Cdd:cd08648   66 aeQLELLEEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPI 145

                        170
                 ....*....|....*
gi 490296984 147 VGQTAVPILPDDTAA 161
Cdd:cd08648  146 IEQDVERVSHRDSVE 160
FMT_core_HypX_N cd08650
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...
 53-171 5.80e-04

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: 39.52  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  53 EHGIAVITPADPAGADVRAALASAKPDFIFSFYYRHMLPVDLlalaargaYNMHGSLL-----PKYRGRVPTNWAVLNGE 127
Cdd:cd08650   23 ERGHEVSVEYALSDDEMREAVALFAPDLIICPFLKKRIPEEI--------WSNYPCLIvhpgiVGDRGPSSLDWAILEGE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490296984 128 TETGATLHEMAAKPDAGAIVGQTAVPILPDDTAAQVF-DKVTVAA 171
Cdd:cd08650   95 KEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYrGEVTDAA 139
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
 50-149 5.36e-03

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 37.85  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  50 VAAEHGIAV----ITPADPAG--ADVRAALASAKPDFIFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAV 123
Cdd:PRK13010 136 LAVQHDIPFhhlpVTPDTKAQqeAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAH 215

                         90       100
                 ....*....|....*....|....*.
gi 490296984 124 LNGETETGATLHEMAAKPDAGAIVGQ 149
Cdd:PRK13010 216 ARGVKLIGATAHFVTDDLDEGPIIEQ 241
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
 17-154 6.92e-03

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 37.65  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296984  17 CLQVLLAR------GVDVALVVT-HEDsptehiwfgsVAAVAAEHGIAV----ITPADPAG--ADVRAALASAKPDFIFS 83
Cdd:PRK13011 102 CLNDLLYRwrigelPMDIVGVVSnHPD----------LEPLAAWHGIPFhhfpITPDTKPQqeAQVLDVVEESGAELVVL 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296984  84 FYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQTAVPI 154
Cdd:PRK13011 172 ARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERV 242
PLN02828 PLN02828
formyltetrahydrofolate deformylase
 79-149 8.72e-03

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 37.03  E-value: 8.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296984  79 DFIFSFYYRHMLPVDLLALAARGAYNMHGSLLPKYRGRVPTNWAVLNGETETGATLHEMAAKPDAGAIVGQ 149
Cdd:PLN02828 149 DFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQ 219
 
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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