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Conserved domains on  [gi|1519726848|gb|RPG95919|]
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MAG: phosphoribosylformylglycinamidine synthase subunit PurQ [Candidatus Pelagibacter sp. TMED286]

Protein Classification

phosphoribosylformylglycinamidine synthase subunit PurQ( domain architecture ID 10012055)

phosphoribosylformylglycinamidine synthase subunit PurQ is part of the complex that catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate; subunit PurQ produces an ammonia molecule by converting glutamine to glutamate

CATH:  3.40.50.880
EC:  6.3.5.3|3.5.1.2
Gene Ontology:  GO:0005524|GO:0004642
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-225 1.43e-124

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 351.34  E-value: 1.43e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALE-KMQFKNQMVWHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSGC 79
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRdLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  80 LILGICNGFQILTETGLLKGTLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNELKEK 159
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519726848 160 NLIAIKYCNAkgnidensNPNGSLENIAGIFNDNKNILGIMPHPERMVDEIISNRDGENLFSSILS 225
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-225 1.43e-124

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 351.34  E-value: 1.43e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALE-KMQFKNQMVWHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSGC 79
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRdLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  80 LILGICNGFQILTETGLLKGTLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNELKEK 159
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519726848 160 NLIAIKYCNAkgnidensNPNGSLENIAGIFNDNKNILGIMPHPERMVDEIISNRDGENLFSSILS 225
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-224 7.40e-118

Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 335.10  E-value: 7.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALEKMQFKNQMVWHKE--TKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSG 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  79 CLILGICNGFQILTETGLLKG---TLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNE 155
Cdd:COG0047    81 GLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519726848 156 LKEKNLIAIKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVDEII---SNRDGENLFSSIL 224
Cdd:COG0047   161 LEANGQVAFRYVDADGNVTYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLgpgESTDGLRIFRSAV 232
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-225 2.86e-106

phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273782 [Multi-domain]  Cd Length: 227  Bit Score: 305.46  E-value: 2.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALEKMQFKNQMVWHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSGCL 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  81 ILGICNGFQILTETGLLKGTLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNELKEKN 160
Cdd:TIGR01737  81 VLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESND 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519726848 161 LIAIKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVDEIISNRDGENLFSSILS 225
Cdd:TIGR01737 161 QVVFRYCDEDGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVE 225
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 5-224 8.20e-96

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 279.50  E-value: 8.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCDRDIAVALEKMQFKNQMVWHKET-----KLPKSDLIVIPGGFSYGDYLRSGAIAGKS-LIIDEVIKAANSG 78
Cdd:cd01740     3 VLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFAERG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  79 CLILGICNGFQILTETGLLKGTLLRNKNLKFI----NKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLN 154
Cdd:cd01740    83 GLVLGICNGFQILVELGLLPGALIRNKGLKFIcrwqNRFVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDETLA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519726848 155 ELKEKNLIA-IKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVD-----EIISNRDGENLFSSIL 224
Cdd:cd01740   163 ELEENGQIAqYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEpwqweRLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 5-208 5.02e-50

CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.


Pssm-ID: 463904 [Multi-domain]  Cd Length: 260  Bit Score: 163.44  E-value: 5.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCDRDIAVALEKMQFKNQMVwH------KETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAA--- 75
Cdd:pfam13507   6 ILREPGTNGEYEMAAAFERAGFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRDAfea 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  76 ---NSGCLILGICNGFQILTETGLLKG----------TLLRNKNLKFINKDVHVKIMN-SKTKFTnryKKDQILKINIAH 141
Cdd:pfam13507  85 ffnRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEkSPSVFL---RGMDGSGLPVAH 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848 142 NEGN-YFTDSAHLNELKEKNLIAIKYCNAKGNIDENS--NPNGSLENIAGIFNDNKNILGIMPHPERMVD 208
Cdd:pfam13507 162 GEGRfVFRSEEVLARLEANGQVALRYVDNAGNPTEEYpfNPNGSPLGIAGICSPDGRVLGLMPHPERVFR 231
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-225 1.43e-124

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 351.34  E-value: 1.43e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALE-KMQFKNQMVWHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSGC 79
Cdd:PRK03619    1 MKVAVIVFPGSNCDRDMARALRdLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  80 LILGICNGFQILTETGLLKGTLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNELKEK 159
Cdd:PRK03619   81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519726848 160 NLIAIKYCNAkgnidensNPNGSLENIAGIFNDNKNILGIMPHPERMVDEIISNRDGENLFSSILS 225
Cdd:PRK03619  161 GQVVFRYCDE--------NPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-224 7.40e-118

Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 335.10  E-value: 7.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALEKMQFKNQMVWHKE--TKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSG 78
Cdd:COG0047     1 PKVAILVFPGSNCDRDMAAAFERAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  79 CLILGICNGFQILTETGLLKG---TLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNE 155
Cdd:COG0047    81 GLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519726848 156 LKEKNLIAIKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVDEII---SNRDGENLFSSIL 224
Cdd:COG0047   161 LEANGQVAFRYVDADGNVTYPANPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLgpgESTDGLRIFRSAV 232
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-225 2.86e-106

phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273782 [Multi-domain]  Cd Length: 227  Bit Score: 305.46  E-value: 2.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALEKMQFKNQMVWHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAANSGCL 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALRLLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  81 ILGICNGFQILTETGLLKGTLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLNELKEKN 160
Cdd:TIGR01737  81 VLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESND 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519726848 161 LIAIKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVDEIISNRDGENLFSSILS 225
Cdd:TIGR01737 161 QVVFRYCDEDGDVAEEANPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVE 225
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 5-224 8.20e-96

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 279.50  E-value: 8.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCDRDIAVALEKMQFKNQMVWHKET-----KLPKSDLIVIPGGFSYGDYLRSGAIAGKS-LIIDEVIKAANSG 78
Cdd:cd01740     3 VLRFPGSNCDRDMAYAFELAGFEAEDVWHNDLlagrkDLDDYDGVVLPGGFSYGDYLRAGAIAAASpLLMEEVKEFAERG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  79 CLILGICNGFQILTETGLLKGTLLRNKNLKFI----NKDVHVKIMNSKTKFTNRYKKDQILKINIAHNEGNYFTDSAHLN 154
Cdd:cd01740    83 GLVLGICNGFQILVELGLLPGALIRNKGLKFIcrwqNRFVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDETLA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519726848 155 ELKEKNLIA-IKYCNAKGNIDENSNPNGSLENIAGIFNDNKNILGIMPHPERMVD-----EIISNRDGENLFSSIL 224
Cdd:cd01740   163 ELEENGQIAqYVDDDGNVTERYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEpwqweRLLGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 5-208 5.02e-50

CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230.


Pssm-ID: 463904 [Multi-domain]  Cd Length: 260  Bit Score: 163.44  E-value: 5.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCDRDIAVALEKMQFKNQMVwH------KETKLPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKAA--- 75
Cdd:pfam13507   6 ILREPGTNGEYEMAAAFERAGFDAVDV-HmsdllsGRVSLDDFQGLAAPGGFSYGDVLGSGKGWAASILFNPKLRDAfea 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  76 ---NSGCLILGICNGFQILTETGLLKG----------TLLRNKNLKFINKDVHVKIMN-SKTKFTnryKKDQILKINIAH 141
Cdd:pfam13507  85 ffnRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKISEkSPSVFL---RGMDGSGLPVAH 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848 142 NEGN-YFTDSAHLNELKEKNLIAIKYCNAKGNIDENS--NPNGSLENIAGIFNDNKNILGIMPHPERMVD 208
Cdd:pfam13507 162 GEGRfVFRSEEVLARLEANGQVALRYVDNAGNPTEEYpfNPNGSPLGIAGICSPDGRVLGLMPHPERVFR 231
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-225 1.95e-46

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 154.53  E-value: 1.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   1 MKSSVIVFPGSNCDRDIAVALEKMQFKNQMVWHKETK-----LPKSDLIVIPGGFSYGDYLRSGAIAG---KSLIIDEVI 72
Cdd:PRK01175    4 IRVAVLRMEGTNCEDETVKAFRRLGVEPEYVHINDLAaerksVSDYDCLVIPGGFSAGDYIRAGAIFAarlKAVLRKDIE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  73 KAANSGCLILGICNGFQILTETGLLKG----------TLLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDqILKINIAHN 142
Cdd:PRK01175   84 EFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLLKKD-VFQVPVAHA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848 143 EGN-YFTDSAHLNELKEKNLIAIKYCNAKGNIDENS-NPNGSLENIAGIFNDNKNILGIMPHPER-------MVDEIISN 213
Cdd:PRK01175  163 EGRvVFSEEEILERLIENDQIVFRYVDENGNYAGYPwNPNGSIYNIAGITNEKGNVIGLMPHPERafygyqhPYWEKEED 242

                         250
                  ....*....|...
gi 1519726848 214 R-DGENLFSSILS 225
Cdd:PRK01175  243 YgDGKIFFDSLIN 255
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 10-207 2.66e-23

phosphoribosylformylglycinamidine synthase, single chain form; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 188163 [Multi-domain]  Cd Length: 1310  Bit Score: 97.55  E-value: 2.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   10 GSNCDRDIAVALEKMQFKnqmVWhketKLPKSDL------------IVIPGGFSYGDYLRSGAIAGKSLIIDEVIKA--- 74
Cdd:TIGR01735 1065 GVNGDREMAAAFDRAGFE---AW----DVHMSDLlagrvhldefrgLAACGGFSYGDVLGAGKGWAKSILFNPRLRDqfq 1137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   75 ---ANSGCLILGICNGFQILTE-TGLLKGT-----LLRNKNLKFINKDVHVKIMNSKTKFTNRYKKDQiLKINIAHNEGN 145
Cdd:TIGR01735 1138 affKRPDTFSLGVCNGCQMLSNlLEWIPGTenwphFVRNNSERFEARVASVRVGESPSIMLRGMAGSR-LPVAVAHGEGY 1216

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519726848  146 -YFTDSAHLNELKEKNLIAIKYCNAKGNIDEN--SNPNGSLENIAGIFNDNKNILGIMPHPERMV 207
Cdd:TIGR01735 1217 aAFSSPELQAQADASGLAALRYIDDDGNPTEAypLNPNGSPGGIAGITSCDGRVTIMMPHPERVF 1281
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 48-205 3.01e-21

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 91.78  E-value: 3.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   48 GGFSYGDYLrsGAIAG--KSLIIDEVIKAANSG------CLILGICNGFQILTETGLL------KGTLLRNKNLKFINKD 113
Cdd:PRK05297  1088 GGFSYGDVL--GAGEGwaKSILFNPRLRDQFEAffarpdTFALGVCNGCQMMSNLKEIipgaehWPRFVRNRSEQFEARF 1165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  114 VHVKIMNSKTKFTNRYKkDQILKINIAHNEGNYFTDSAHLNELKEKNLIAIKYCNAKGNIDEN--SNPNGSLENIAGIFN 191
Cdd:PRK05297  1166 SLVEVQESPSIFLQGMA-GSRLPIAVAHGEGRAEFPDAHLAALEAKGLVALRYVDNHGQVTETypANPNGSPNGITGLTT 1244

                          170
                   ....*....|....
gi 1519726848  192 DNKNILGIMPHPER 205
Cdd:PRK05297  1245 ADGRVTIMMPHPER 1258
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 2-205 1.57e-19

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 86.75  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848    2 KSSVIVFPGSNCDRDIAVALEKMQFKNqmvWhketKLPKSDL------------IVIPGGFSYGDYLRSG-AIAG----- 63
Cdd:PLN03206  1039 KVAIIREEGSNGDREMAAAFYAAGFEP---W----DVTMSDLlngrislddfrgIVFVGGFSYADVLDSAkGWAGsirfn 1111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   64 KSLI--IDEVIKAANSgcLILGICNGFQILTETGLLKGT----------------LLRNKNLKFINKDVHVKIMNSKTKF 125
Cdd:PLN03206  1112 EPLLqqFQEFYNRPDT--FSLGVCNGCQLMALLGWVPGPqvggglgaggdpsqprFVHNESGRFECRFTSVTIEDSPAIM 1189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  126 tnrYK--KDQILKINIAHNEGN-YFTDSAHLNELKEKNLIAIKYCNAKGNIDEN--SNPNGSLENIAGIFNDNKNILGIM 200
Cdd:PLN03206  1190 ---LKgmEGSTLGVWAAHGEGRaYFPDESVLDEVLKSNLAPVRYCDDDGEPTEQypFNPNGSPLGIAALCSPDGRHLAMM 1266


                   ....*
gi 1519726848  201 PHPER 205
Cdd:PLN03206  1267 PHPER 1271
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-91 1.01e-10

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 56.44  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCD--RDIAVALEKMQFKNQMVWHKE------TKLPKSDLIVIPGGFSYGDYLRSGAiagksLIIDEVIKAAN 76
Cdd:cd03128     3 VLLFGGSEELelASPLDALREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLAWDE-----ALLALLREAAA 77

                          90
                  ....*....|....*
gi 1519726848  77 SGCLILGICNGFQIL 91
Cdd:cd03128    78 AGKPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-91 1.41e-10

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.84  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848   5 VIVFPGSNCD--RDIAVALEKMQFKNQMVWHKE------TKLPKSDLIVIPGGFSYGDYLRSGAiagksLIIDEVIKAAN 76
Cdd:cd01653     3 VLLFPGFEELelASPLDALREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLARDE-----ALLALLREAAA 77

                          90
                  ....*....|....*
gi 1519726848  77 SGCLILGICNGFQIL 91
Cdd:cd01653    78 AGKPILGICLGAQLL 92
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 42-99 2.17e-06

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 46.10  E-value: 2.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519726848  42 DLIVIPGGFSYGDYLRsgaiaGKSLIIDEVIKAANSGCLILGICNGFQILTETGLLKG 99
Cdd:pfam01965  63 DALVLPGGRAGPERLR-----DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
34-94 7.95e-06

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 44.92  E-value: 7.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519726848  34 KETKLPKS-DLIVIPGGFsygDYLRSGAIAGKSLIIDEVIKAANSGCLILGICNGFQILTET 94
Cdd:pfam07685  35 PDESLGPDaDLIILPGGK---PTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGET 93
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 38-94 1.37e-05

Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441101 [Multi-domain]  Cd Length: 493  Bit Score: 45.05  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519726848  38 LPKSDLIVIPGgfS---YGD--YLR-SGaiagksliIDEVIKA-ANSGCLILGICNGFQILTET 94
Cdd:COG1492   288 LGDADLVILPG--SkntIADlaWLReSG--------LDDAIRAhARRGGPVLGICGGYQMLGRR 341
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 42-116 2.12e-05

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 43.30  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  42 DLIVIPGGFSyGDYLRSGAIAgksliIDEVIKAANSGCLILGICNGFQILTETGLLKG-TL---------LRNKNLKFIN 111
Cdd:cd03134    64 DALVIPGGTN-PDKLRRDPDA-----VAFVRAFAEAGKPVAAICHGPWVLISAGVVRGrKLtsypsikddLINAGANWVD 137


                  ....*
gi 1519726848 112 KDVHV 116
Cdd:cd03134   138 EEVVV 142
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 15-103 2.85e-05

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 43.26  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  15 RDIAVALEKMQFKNQMVwHKETKLPKSDLIVIPGGFSYGDYLRSGAIAGkslIIDEVIKAANSGCLILGICNGFQILTET 94
Cdd:cd01748    12 RSVANALERLGAEVIIT-SDPEEILSADKLILPGVGAFGDAMANLRERG---LIEALKEAIASGKPFLGICLGMQLLFES 87

                          90
                  ....*....|....*....
gi 1519726848  95 ----------GLLKGTLLR 103
Cdd:cd01748    88 seegggtkglGLIPGKVVR 106
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 42-91 2.90e-05

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 43.39  E-value: 2.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519726848  42 DLIVIPGGFSYG---DYLRSGAIAgksliiDEVIKAANSGCLILGICNGFQIL 91
Cdd:cd01750    39 DLIILPGSKDTIqdlAWLRKRGLA------EAIKNYARAGGPVLGICGGYQML 85
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 42-116 7.38e-05

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 41.63  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  42 DLIVIPGGFSYGDYLRSGAIAgksliIDEVIKAANSGCLILGICNGFQILTETGLLKG----------TLLRNKNLKFIN 111
Cdd:COG0693    66 DALVLPGGHGAPDDLREDPDV-----VALVREFYEAGKPVAAICHGPAVLAAAGLLKGrkvtsfpnieDDLKNAGATYVD 140


                  ....*
gi 1519726848 112 KDVHV 116
Cdd:COG0693   141 EEVVV 145
PRK00784 PRK00784
cobyric acid synthase;
38-91 8.02e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 42.76  E-value: 8.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1519726848  38 LPKSDLIVIPGgfS---YGD--YLRSGAIAgksliiDEVIKAANSGCLILGICNGFQIL 91
Cdd:PRK00784  288 LPDADLVILPG--SkntIADlaWLRESGWD------EAIRAHARRGGPVLGICGGYQML 338
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 20-108 8.88e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 42.04  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  20 ALEKMQFKNQMVWHKEtKLPKSDLIVIPGGFSYGDylrsgAIAG-KSLIIDEVIK-AANSGCLILGICNGFQILTET--- 94
Cdd:PRK13141   18 ALERLGAEAVITSDPE-EILAADGVILPGVGAFPD-----AMANlRERGLDEVIKeAVASGKPLLGICLGMQLLFESsee 91

                          90       100
                  ....*....|....*....|....
gi 1519726848  95 -------GLLKGTLLR---NKNLK 108
Cdd:PRK13141   92 fgeteglGLLPGRVRRfppEEGLK 115
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 38-99 4.62e-03

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 37.44  E-value: 4.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519726848  38 LPKSDLIVIPGGFSYGDYLRSGAIAGksliideVIKAANSGCLILGICNGFQILTETGLLKG 99
Cdd:COG4977    64 LAAADTLIVPGGLDPAAAADPALLAW-------LRRAAARGARLASICTGAFLLAAAGLLDG 118
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 42-99 5.94e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 36.38  E-value: 5.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519726848  42 DLIVIPGGFSYGDYLRSgaiagKSLIIDEVIKAANSGCLILGICNGFQILTETGLLKG 99
Cdd:cd03135    62 DAIVIPGGLPGAQNLAD-----NEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKG 114
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 40-109 7.94e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 36.00  E-value: 7.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519726848  40 KSDLIVIPGGFSYGD---YLRSgaiagkslIIDEVIKAANSGCLILGICNGFQIL----TETGLLKG-TLLRNKNLKF 109
Cdd:PRK13143   38 DADGIVLPGVGAFGAameNLSP--------LRDVILEAARSGKPFLGICLGMQLLfessEEGGGVRGlGLFPGRVVRF 107
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 15-95 9.00e-03

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 36.15  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519726848  15 RDIAVALEKMQFKNQMVwhKETK-LPKSDLIVIPGGFSYGDYLRSGAIAGKSLIIDEVIKaanSGCLILGICNGFQILTE 93
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVV--KDSKeAELADKLILPGVGAFGAAMARLRENGLDLFVELVVR---LGKPVLGICLGMQLLFE 86


                  ..
gi 1519726848  94 TG 95
Cdd:TIGR01855  87 RS 88
 
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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