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Conserved domains on  [gi|18422794|ref|NP_568682|]
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formyltetrahydrofolate deformylase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02828 PLN02828
formyltetrahydrofolate deformylase
56-323 0e+00

formyltetrahydrofolate deformylase


:

Pssm-ID: 178422  Cd Length: 268  Bit Score: 557.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   56 LSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGALNSVVRVPSIDPKYKIALLLSKQ 135
Cdd:PLN02828   1 LSDCIASRGGNILGVDVFVPENKNVFYSRSEFIFDPVKWPRAQMDEDFQEISKHFKALKSVVRVPGLDPKYKIAVLASKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  136 DHCLVEMLHKWQDGKLPVDITCVISNHERASNTHVMRFLERHGIPYHYVSTTKENKREDDILELVKDTDFLVLARYMQIL 215
Cdd:PLN02828  81 DHCLIDLLHRWQDGRLPVDITCVISNHERGPNTHVMRFLERHGIPYHYLPTTKENKREDEILELVKGTDFLVLARYMQIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  216 SGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDL 295
Cdd:PLN02828 161 SGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENL 240
                        250       260
                 ....*....|....*....|....*...
gi 18422794  296 EKKCLTRAIKSYCELRVLPYGTNKTVVF 323
Cdd:PLN02828 241 EKQCLAKAIKSYCELRVLPYGTNKTVVF 268
 
Name Accession Description Interval E-value
PLN02828 PLN02828
formyltetrahydrofolate deformylase
56-323 0e+00

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 557.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   56 LSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGALNSVVRVPSIDPKYKIALLLSKQ 135
Cdd:PLN02828   1 LSDCIASRGGNILGVDVFVPENKNVFYSRSEFIFDPVKWPRAQMDEDFQEISKHFKALKSVVRVPGLDPKYKIAVLASKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  136 DHCLVEMLHKWQDGKLPVDITCVISNHERASNTHVMRFLERHGIPYHYVSTTKENKREDDILELVKDTDFLVLARYMQIL 215
Cdd:PLN02828  81 DHCLIDLLHRWQDGRLPVDITCVISNHERGPNTHVMRFLERHGIPYHYLPTTKENKREDEILELVKGTDFLVLARYMQIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  216 SGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDL 295
Cdd:PLN02828 161 SGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENL 240
                        250       260
                 ....*....|....*....|....*...
gi 18422794  296 EKKCLTRAIKSYCELRVLPYGTNKTVVF 323
Cdd:PLN02828 241 EKQCLAKAIKSYCELRVLPYGTNKTVVF 268
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
44-323 3.76e-117

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 339.33  E-value: 3.76e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  44 FHCQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGAlnsVVRVPSID 123
Cdd:COG0788   8 LSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPGLDFDLEALRAAFAPLAERFGM---DWRLHDSD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 124 PKYKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHErasnthVMRFL-ERHGIPYHYVSTTKENKREDD--ILELV 200
Cdd:COG0788  85 RRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHP------DLRPLaEWFGIPFHHIPVTKETKAEAEarLLELL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 201 K--DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVES 278
Cdd:COG0788 159 EeyDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVER 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18422794 279 VSHRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:COG0788 239 VDHRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNG-NKTVVF 282
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
126-323 1.35e-109

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: 316.81  E-value: 1.35e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 126 YKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERAsnthvMRFLERHGIPYHYVSTTKENKREDD----ILELVK 201
Cdd:cd08648   1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDL-----RPLAERFGIPFHHIPVTKDTKAEAEaeqlELLEEY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 202 DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSH 281
Cdd:cd08648  76 GVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSH 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18422794 282 RDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:cd08648 156 RDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYG-NKTVVF 196
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
46-323 9.68e-90

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 269.69  E-value: 9.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794    46 CQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDF-QTIAQRYGALNSVVrvPSIDP 124
Cdd:TIGR00655   7 CPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFRLEESSLLAAFkSALAEKFEMTWELI--LADKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   125 KyKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERASNThvmrfLERHGIPYHYVSTTKENKREDD--ILELVK- 201
Cdd:TIGR00655  85 K-RVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSL-----VERFGIPFHYIPATKDNRVEHEkrQLELLKq 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   202 -DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVS 280
Cdd:TIGR00655 159 yQVDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 18422794   281 HRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:TIGR00655 239 HTDNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYE-NKTVVF 280
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
127-304 2.14e-34

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: 123.94  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   127 KIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERASnthVMRFLERHGIPYHYVST---TKENKREDDILELVK-- 201
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAA---GLGRAEQAGIPTFVFEHkglTPRSLFDQELADALRal 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   202 DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSH 281
Cdd:pfam00551  79 AADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILP 158
                         170       180
                  ....*....|....*....|...
gi 18422794   282 RDNLRSFVQKSEDLEKKCLTRAI 304
Cdd:pfam00551 159 DDTAETLYNRVADLEHKALPRVL 181
 
Name Accession Description Interval E-value
PLN02828 PLN02828
formyltetrahydrofolate deformylase
56-323 0e+00

formyltetrahydrofolate deformylase


Pssm-ID: 178422  Cd Length: 268  Bit Score: 557.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   56 LSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGALNSVVRVPSIDPKYKIALLLSKQ 135
Cdd:PLN02828   1 LSDCIASRGGNILGVDVFVPENKNVFYSRSEFIFDPVKWPRAQMDEDFQEISKHFKALKSVVRVPGLDPKYKIAVLASKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  136 DHCLVEMLHKWQDGKLPVDITCVISNHERASNTHVMRFLERHGIPYHYVSTTKENKREDDILELVKDTDFLVLARYMQIL 215
Cdd:PLN02828  81 DHCLIDLLHRWQDGRLPVDITCVISNHERGPNTHVMRFLERHGIPYHYLPTTKENKREDEILELVKGTDFLVLARYMQIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  216 SGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDL 295
Cdd:PLN02828 161 SGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIEQMVERVSHRDNLRSFVQKSENL 240
                        250       260
                 ....*....|....*....|....*...
gi 18422794  296 EKKCLTRAIKSYCELRVLPYGTNKTVVF 323
Cdd:PLN02828 241 EKQCLAKAIKSYCELRVLPYGTNKTVVF 268
PurU COG0788
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ...
44-323 3.76e-117

Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440551 [Multi-domain]  Cd Length: 282  Bit Score: 339.33  E-value: 3.76e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  44 FHCQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGAlnsVVRVPSID 123
Cdd:COG0788   8 LSCPDRPGIVAAVTGFLAEHGGNITEADQFVDPETGRFFMRVEFEAPGLDFDLEALRAAFAPLAERFGM---DWRLHDSD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 124 PKYKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHErasnthVMRFL-ERHGIPYHYVSTTKENKREDD--ILELV 200
Cdd:COG0788  85 RRKRVAILVSKEDHCLNDLLYRWRSGELPAEIPAVISNHP------DLRPLaEWFGIPFHHIPVTKETKAEAEarLLELL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 201 K--DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVES 278
Cdd:COG0788 159 EeyDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVER 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 18422794 279 VSHRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:COG0788 239 VDHRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNG-NKTVVF 282
FMT_core_Formyl-FH4-Hydrolase_C cd08648
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ...
126-323 1.35e-109

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: 316.81  E-value: 1.35e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 126 YKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERAsnthvMRFLERHGIPYHYVSTTKENKREDD----ILELVK 201
Cdd:cd08648   1 KRVAIFVSKEDHCLYDLLHRWREGELPCEIPLVISNHPDL-----RPLAERFGIPFHHIPVTKDTKAEAEaeqlELLEEY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 202 DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSH 281
Cdd:cd08648  76 GVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVERVSH 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18422794 282 RDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:cd08648 156 RDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYG-NKTVVF 196
purU PRK06027
formyltetrahydrofolate deformylase; Reviewed
46-323 1.49e-109

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 235676 [Multi-domain]  Cd Length: 286  Bit Score: 320.13  E-value: 1.49e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   46 CQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGALNSVVRVpsiDPK 125
Cdd:PRK06027  13 CPDRPGIVAAVSNFLYEHGGNIVDADQFVDPETGRFFMRVEFEGDGLIFNLETLRADFAALAEEFEMDWRLLDS---AER 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  126 YKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHErasntHVMRFLERHGIPYHYVSTTKENKR--EDDILELVKDT 203
Cdd:PRK06027  90 KRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHD-----DLRSLVERFGIPFHHVPVTKETKAeaEARLLELIDEY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  204 --DFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSH 281
Cdd:PRK06027 165 qpDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIEQDVIRVDH 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18422794  282 RDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:PRK06027 245 RDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYG-NKTVVF 285
PurU TIGR00655
formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. ...
46-323 9.68e-90

formyltetrahydrofolate deformylase; This model describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273199 [Multi-domain]  Cd Length: 280  Bit Score: 269.69  E-value: 9.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794    46 CQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDF-QTIAQRYGALNSVVrvPSIDP 124
Cdd:TIGR00655   7 CPDQKGLVAAISTFIAKHGANIISNDQHTDPETGRFFMRVEFQLEGFRLEESSLLAAFkSALAEKFEMTWELI--LADKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   125 KyKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERASNThvmrfLERHGIPYHYVSTTKENKREDD--ILELVK- 201
Cdd:TIGR00655  85 K-RVAILVSKEDHCLGDLLWRWYSGELDAEIALVISNHEDLRSL-----VERFGIPFHYIPATKDNRVEHEkrQLELLKq 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   202 -DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVS 280
Cdd:TIGR00655 159 yQVDLVVLAKYMQILSPDFVKRYPNKIINIHHSFLPAFIGANPYQRAYERGVKIIGATAHYVTEELDEGPIIEQDVVRVD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 18422794   281 HRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:TIGR00655 239 HTDNVEDLIRAGRDIEKVVLARAVKLHLEDRVFVYE-NKTVVF 280
PRK13011 PRK13011
formyltetrahydrofolate deformylase; Reviewed
45-323 1.93e-78

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 237266 [Multi-domain]  Cd Length: 286  Bit Score: 241.04  E-value: 1.93e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   45 HCQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIfDPVKWPRSQVDEDFQTIAQRYGAlnsVVRVPSIDP 124
Cdd:PRK13011  13 SCPSAAGIVAAVTGFLAEHGCYITELHSFDDRLSGRFFMRVEFH-SEEGLDEDALRAGFAPIAARFGM---QWELHDPAA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  125 KYKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHerasnTHVMRFLERHGIPYHYVSTTKENK--REDDILELVKD 202
Cdd:PRK13011  89 RPKVLIMVSKFDHCLNDLLYRWRIGELPMDIVGVVSNH-----PDLEPLAAWHGIPFHHFPITPDTKpqQEAQVLDVVEE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  203 T--DFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVS 280
Cdd:PRK13011 164 SgaELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPIIEQDVERVD 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 18422794  281 HRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:PRK13011 244 HAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNG-NRTVVF 285
purU PRK13010
formyltetrahydrofolate deformylase; Reviewed
46-323 2.15e-73

formyltetrahydrofolate deformylase; Reviewed


Pssm-ID: 139334 [Multi-domain]  Cd Length: 289  Bit Score: 228.14  E-value: 2.15e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   46 CQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVK-WPRSQVDEDFQTIAQRYGALNSVVRVPSidp 124
Cdd:PRK13010  16 CPSAPGIVAAVSGFLAEKGCYIVELTQFDDDESGRFFMRVSFHAQSAEaASVDTFRQEFQPVAEKFDMQWAIHPDGQ--- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  125 KYKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERASNTHVmrfleRHGIPYHYVSTTKENK--REDDILELVK- 201
Cdd:PRK13010  93 RPKVVIMVSKFDHCLNDLLYRWRMGELDMDIVGIISNHPDLQPLAV-----QHDIPFHHLPVTPDTKaqQEAQILDLIEt 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  202 -DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVS 280
Cdd:PRK13010 168 sGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAHFVTDDLDEGPIIEQDVERVD 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 18422794  281 HRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVLPYGtNKTVVF 323
Cdd:PRK13010 248 HSYSPEDLVAKGRDVECLTLARAVKAFIEHRVFING-DRTVVF 289
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
147-305 2.85e-41

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: 141.76  E-value: 2.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 147 QDGKLPVDITCVISNHERAsntHVMRFLERHGIPYHYVSTTKENKRED---DILELVK--DTDFLVLARYMQILSGNFLK 221
Cdd:cd08645  21 KSGKLNAEIVLVISNNPDA---YGLERAKKAGIPTFVINRKDFPSREEfdeALLELLKeyKVDLIVLAGFMRILSPEFLE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 222 GYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDLEKKCLT 301
Cdd:cd08645  98 AFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIHALEHRLYP 177

                ....
gi 18422794 302 RAIK 305
Cdd:cd08645 178 EAIK 181
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
147-312 1.87e-38

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: 135.16  E-value: 1.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 147 QDGKLPVDITCVISNHERAsnthvmRFLER---HGIPYHYVSTTKENKRED---DILELVK--DTDFLVLARYMQILSGN 218
Cdd:COG0299  23 EAGDLPAEIVLVISNRPDA------YGLERaraAGIPTFVLDHKDFPSREAfdaALLEALDayGPDLVVLAGFMRILTPE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 219 FLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDLEKK 298
Cdd:COG0299  97 FVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARILEQEHR 176
                       170
                ....*....|....
gi 18422794 299 CLTRAIKSYCELRV 312
Cdd:COG0299 177 LYPEAIRLLAEGRL 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
127-304 2.14e-34

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: 123.94  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   127 KIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERASnthVMRFLERHGIPYHYVST---TKENKREDDILELVK-- 201
Cdd:pfam00551   2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAA---GLGRAEQAGIPTFVFEHkglTPRSLFDQELADALRal 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   202 DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSH 281
Cdd:pfam00551  79 AADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILP 158
                         170       180
                  ....*....|....*....|...
gi 18422794   282 RDNLRSFVQKSEDLEKKCLTRAI 304
Cdd:pfam00551 159 DDTAETLYNRVADLEHKALPRVL 181
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
128-306 2.06e-33

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: 121.24  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 128 IALLLSKqdHCLVEMLHKWQDGKLpVDITCVISNHERASNTHVMRFLERHGIPYHYVsttkeNKREDDILELVKDT--DF 205
Cdd:cd08369   1 IVILGSG--NIGQRVLKALLSKEG-HEIVGVVTHPDSPRGTAQLSLELVGGKVYLDS-----NINTPELLELLKEFapDL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 206 LVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNL 285
Cdd:cd08369  73 IVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTA 152
                       170       180
                ....*....|....*....|.
gi 18422794 286 RSFVQKSEDLEKKCLTRAIKS 306
Cdd:cd08369 153 GTLYQRLIELGPKLLKEALQK 173
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
127-313 1.07e-32

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: 119.78  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   127 KIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERAsnthvmRFLER---HGIPYHYVSTTKENKR---EDDILELV 200
Cdd:TIGR00639   2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDA------YGLERaaqAGIPTFVLSLKDFPSReafDQAIIEEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   201 K--DTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVES 278
Cdd:TIGR00639  76 RahEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVP 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 18422794   279 VSHRDNLRSFVQKSEDLEKKCLTRAIKSYCELRVL 313
Cdd:TIGR00639 156 ILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
ACT_F4HF-DF cd04875
N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate ...
41-112 8.21e-20

N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase); This CD includes the N-terminal ACT domain of formyltetrahydrofolate deformylase (F4HF-DF; formyltetrahydrofolate hydrolase) which catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formyl-FH4 hydrolase generates the formate that is used by purT-encoded 5'-phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase, a hexamer which is activated by methionine and inhibited by glycine, is proposed to regulate the balance FH4 and C1-FH4 in response to changing growth conditions. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153147 [Multi-domain]  Cd Length: 74  Bit Score: 81.84  E-value: 8.21e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18422794  41 VHVFHCQDAVGIVAKLSDCIAAKGGNILGYDVFVPENNNVFYSRSEFIFDPVKWPRSQVDEDFQTIAQRYGA 112
Cdd:cd04875   1 ILTLSCPDRPGIVAAVSGFLAEHGGNIVESDQFVDPDSGRFFMRVEFELEGFDLSREALEAAFAPVAAEFDM 72
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
147-312 3.53e-15

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 73.19  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  147 QDGKLPVDITCVISNHERASNTHVMRfleRHGIPyhyVSTTKENKREDDIL---ELVK-----DTDFLVLARYMQILSGN 218
Cdd:PLN02331  21 LDGRVNGDVVVVVTNKPGCGGAEYAR---ENGIP---VLVYPKTKGEPDGLspdELVDalrgaGVDFVLLAGYLKLIPVE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  219 FLKGYGKDVINIHHGLLPSFKG-GYPAKQAFDA----GVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSE 293
Cdd:PLN02331  95 LVRAYPRSILNIHPALLPAFGGkGYYGIKVHKAviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVL 174
                        170
                 ....*....|....*....
gi 18422794  294 DLEKKCLTRAIKSYCELRV 312
Cdd:PLN02331 175 HEEHQLYVEVVAALCEERI 193
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
153-299 2.27e-11

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


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 63.59  E-value: 2.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 153 VDITCVISNHERASN-------THVMRFLERHGIPYHyvstTKENKREDDILELVKDT--DFLVLARYMQILSGNFLK-- 221
Cdd:COG0223  24 HEVVAVVTQPDRPAGrgrkltpSPVKELALEHGIPVL----QPESLKDPEFLEELRALnpDLIVVVAYGQILPKEVLDip 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18422794 222 GYGkdVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNlrsfvqkSEDLEKKC 299
Cdd:COG0223 100 RLG--CINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDT-------AGSLHDKL 168
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
173-322 2.83e-11

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: 63.19  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794   173 FLERHGIPYhyvsTTKENKREDDILELVKD--TDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDA 250
Cdd:TIGR00460  51 LAEEKGIPV----FQPEKQRQLEELPLVRElkPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILN 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18422794   251 GVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDLEKKCLTRAiksyceLRVLPYGTNKTVV 322
Cdd:TIGR00460 127 GDKKTGVTIMQMVPKMDAGDILKQETFPIEEEDNSGTLSDKLSELGAQLLIET------LKELPEGKNKPEP 192
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
150-299 1.26e-10

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: 60.15  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 150 KLPVDITCVISNHERAS-------NTHVMRFLERHGIPYHyvstTKENKREDDILELVKDT--DFLVLARYMQILSGNFL 220
Cdd:cd08646  21 KSGHEVVAVVTQPDKPRgrgkkltPSPVKELALELGLPVL----QPEKLKDEEFLEELKALkpDLIVVVAYGQILPKEIL 96
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18422794 221 KGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNlrsfvqkSEDLEKKC 299
Cdd:cd08646  97 DLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDT-------AGELLDKL 168
PLN02285 PLN02285
methionyl-tRNA formyltransferase
170-274 2.21e-10

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 60.86  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  170 VMRFLERHGIPYHYVsTTKENKREDDILELVKDT--DFLVLARYMQILSGNFLK--GYGkdVINIHHGLLPSFKGGYPAK 245
Cdd:PLN02285  60 VAQLALDRGFPPDLI-FTPEKAGEEDFLSALRELqpDLCITAAYGNILPQKFLDipKLG--TVNIHPSLLPLYRGAAPVQ 136
                         90       100
                 ....*....|....*....|....*....
gi 18422794  246 QAFDAGVKLIGATSHFVTEELDSGPIIEQ 274
Cdd:PLN02285 137 RALQDGVNETGVSVAFTVRALDAGPVIAQ 165
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
206-304 6.11e-10

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


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 56.84  E-value: 6.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 206 LVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAG-VKLIGATSHFVTEELDSGPIIEQMVESVSHRDN 284
Cdd:cd08653  50 VVSVYGCGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGdPDNVGVTVHLVDAGIDTGDVLAQARPPLAAGDT 129
                        90       100
                ....*....|....*....|
gi 18422794 285 LRSFVQKSEDLEKKCLTRAI 304
Cdd:cd08653 130 LLSLYLRLYRAGVELMVEAI 149
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
152-306 3.83e-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: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 55.35  E-value: 3.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 152 PVDITCVISNHERASNTH-----VMRFLERHGIPYHYVSttkeNKREDDILELVKDT--DFLVLARYMQILSGNFLKGYG 224
Cdd:cd08651  22 GGEVVGVITLDDSSSNNDsdyldLDSFARKNGIPYYKFT----DINDEEIIEWIKEAnpDIIFVFGWSQLLKPEILAIPR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 225 KDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDLEKKCLTRAI 304
Cdd:cd08651  98 LGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDTANSLYDKIMEAAKQQIDKFL 177

                ..
gi 18422794 305 KS 306
Cdd:cd08651 178 PR 179
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
170-291 2.38e-07

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: 50.42  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 170 VMRFLERHGIPYHYVSTTKENKREDDILELvkDTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFD 249
Cdd:cd08644  45 VAQLAREHGIPVFTPDDINHPEWVERLRAL--KPDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALI 122
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18422794 250 AGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQK 291
Cdd:cd08644 123 NGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHK 164
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
165-272 8.99e-07

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


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 48.21  E-value: 8.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 165 ASNTHVmRFLERHGIPYHYVSTTKENKREDDILELVKDTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPA 244
Cdd:cd08820  33 LTNTSP-ADVWEGSEPLYDIGSTERNLHKLLEILENKGVDILISVQYHWILPGSILEKAKEIAFNLHNAPLPEYRGCNQF 111
                        90       100
                ....*....|....*....|....*...
gi 18422794 245 KQAFDAGVKLIGATSHFVTEELDSGPII 272
Cdd:cd08820 112 SHAILNGDDQFGTTIHWMAEGIDSGDII 139
PRK06988 PRK06988
formyltransferase;
136-304 2.66e-06

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 48.15  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  136 DHCLVEMLHKwqdgklPVDITCVISnHERASNTH-----VMRFLERHGIPYhyvsTTKENKREDDILELVKDT--DFLVL 208
Cdd:PRK06988  15 VRCLQVLLAR------GVDVALVVT-HEDNPTENiwfgsVAAVAAEHGIPV----ITPADPNDPELRAAVAAAapDFIFS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  209 ARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDNLRSF 288
Cdd:PRK06988  84 FYYRHMIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQV 163
                        170
                 ....*....|....*.
gi 18422794  289 VQKSEDLEKKCLTRAI 304
Cdd:PRK06988 164 FDKVTVAAEQTLWRVL 179
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
184-274 9.20e-06

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: 45.51  E-value: 9.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794 184 VSTTKENKREDDILeLVKDTDFLVLARYMQILSGNFLKGYGKDVINIHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVT 263
Cdd:cd08823  54 VDTANLKEQLAEWL-RALAADTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMT 132
                        90
                ....*....|.
gi 18422794 264 EELDSGPIIEQ 274
Cdd:cd08823 133 AEIDRGPIVLE 143
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
228-304 1.38e-05

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


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 45.66  E-value: 1.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18422794  228 INIHHGLLPSFKGGYPakQAFDAGVKL-IGATSHFVTEELDSGPIIEQMVESVSHRDNLRSFVQKSEDLEKKCLTRAI 304
Cdd:PRK07579  89 INIHPGFNPYNRGWFP--QVFSIINGLkIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVLEHF 164
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
154-284 1.06e-04

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


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 43.82  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422794  154 DITCVISNHERASNTH----VMRFLERHGIPYHYVSTTKENKREDDILELVKDTDFLVLarYMQILSGNFLKGYGKDVIN 229
Cdd:PRK08125  25 EIAAVFTHTDNPGENHffgsVARLAAELGIPVYAPEDVNHPLWVERIRELAPDVIFSFY--YRNLLSDEILQLAPAGAFN 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18422794  230 IHHGLLPSFKGGYPAKQAFDAGVKLIGATSHFVTEELDSGPIIEQMVESVSHRDN 284
Cdd:PRK08125 103 LHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDT 157
 
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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