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Conserved domains on  [gi|499562249|ref|WP_011243032|]
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phosphoribosylformylglycinamidine synthase subunit PurQ [Synechococcus elongatus]

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;
1-217 6.32e-154

phosphoribosylformylglycinamidine synthase subunit PurQ;


:

Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 425.30  E-value: 6.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVQWVTAGLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGG 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  81 LVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEAN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249 161 GQVLFRYLD-NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLE 217
Cdd:PRK03619 161 GQVVFRYCDeNPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-217 6.32e-154

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 425.30  E-value: 6.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVQWVTAGLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGG 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  81 LVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEAN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249 161 GQVLFRYLD-NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLE 217
Cdd:PRK03619 161 GQVVFRYCDeNPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-217 6.41e-127

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: 357.83  E-value: 6.41e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEE--RDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEA 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAFE-RAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  79 GGLVLGICNGFQILTEVGLLPG---ALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLA 155
Cdd:COG0047   80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499562249 156 ALEANGQVLFRYLD---------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAG---SVDGLGLFAGLLE 217
Cdd:COG0047  160 ELEANGQVAFRYVDadgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVK 233
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-217 9.01e-114

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: 324.33  E-value: 9.01e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    1 MNVGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGG 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   81 LVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEAN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499562249  161 GQVLFRYLD---------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLE 217
Cdd:TIGR01737 160 DQVVFRYCDedgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVE 225
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-216 8.95e-100

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: 289.13  E-value: 8.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   3 VGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEE-----RDLSGLDLIVVPGGFSYGDYLRCGAIARFSP-AMQATVAFA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNDllagrKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  77 EAGGLVLGICNGFQILTEVGLLPGALVRNRDLHFRCET----TPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPA 152
Cdd:cd01740   80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWqnrfVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249 153 TLAALEANGQVLF----------RYLDNPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIA-----GSVDGLGLFAGLL 216
Cdd:cd01740  160 TLAELEENGQIAQyvdddgnvteRYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQwerllGGSDGLKLFRNAV 238
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-205 7.43e-49

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: 160.36  E-value: 7.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    2 NVGVIVFPGSNCDRDVQWV--TAGLLGQSTRM--IWHEERDLSGLDLIVVPGGFSYGDYLrcGA---IA---RFSPAMQA 71
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAfeRAGFDAVDVHMsdLLSGRVSLDDFQGLAAPGGFSYGDVL--GSgkgWAasiLFNPKLRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   72 TVA--FAEAGGLVLGICNGFQILTEVGLLPG----------ALVRNRDLHFRCETTPLRVErSDRPWSRTyQQGQILNLP 139
Cdd:pfam13507  81 AFEafFNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKIS-EKSPSVFL-RGMDGSGLP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249  140 IAHGEGR-YHADPATLAALEANGQVLFRYLD-----------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGS 205
Cdd:pfam13507 159 VAHGEGRfVFRSEEVLARLEANGQVALRYVDnagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWQWP 236
 
Name Accession Description Interval E-value
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
1-217 6.32e-154

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 425.30  E-value: 6.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVQWVTAGLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGG 80
Cdd:PRK03619   1 MKVAVIVFPGSNCDRDMARALRDLLGAEPEYVWHKETDLDGVDAVVLPGGFSYGDYLRCGAIAAFSPIMKAVKEFAEKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  81 LVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEAN 160
Cdd:PRK03619  81 PVLGICNGFQILTEAGLLPGALTRNASLKFICRDVHLRVENNDTPFTSGYEKGEVIRIPIAHGEGNYYADEETLKRLEGN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249 161 GQVLFRYLD-NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLE 217
Cdd:PRK03619 161 GQVVFRYCDeNPNGSVNDIAGIVNEKGNVLGMMPHPERAVEPLLGSTDGLKLFESLLK 218
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 1-217 6.41e-127

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: 357.83  E-value: 6.41e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEE--RDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEA 78
Cdd:COG0047    1 PKVAILVFPGSNCDRDMAAAFE-RAGAEAEDVWHSDlrTDLDDFDGLVLPGGFSYGDYLRAGAIAAFSPIMDAVREFARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  79 GGLVLGICNGFQILTEVGLLPG---ALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLA 155
Cdd:COG0047   80 GGLVLGICNGFQILTELGLLPGiwpALTRNRSLRFICRWVYLRVENNDSPFTSGMEAGEVIPIPIAHGEGRYVADEETLA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499562249 156 ALEANGQVLFRYLD---------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAG---SVDGLGLFAGLLE 217
Cdd:COG0047  160 ELEANGQVAFRYVDadgnvtypaNPNGSLNNIAGITNEDGNVLGMMPHPERAVEPLLGpgeSTDGLRIFRSAVK 233
FGAM_synth_I TIGR01737
phosphoribosylformylglycinamidine synthase I; In some species, ...
 1-217 9.01e-114

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: 324.33  E-value: 9.01e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    1 MNVGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEERDLSGLDLIVVPGGFSYGDYLRCGAIARFSPAMQATVAFAEAGG 80
Cdd:TIGR01737   1 MKVAVIRFPGTNCDRDTVYALR-LLGVDAEIVWYEDGSLPDYDGVVLPGGFSYGDYLRAGAIAAASPIMQEVREFAEKGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   81 LVLGICNGFQILTEVGLLPGALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPATLAALEAN 160
Cdd:TIGR01737  80 PVLGICNGFQILVEAGLLPGALLPNDSLRFICRWVYLRVENADTIFTKNYKKGEVIRIPIAHGEGRYYADDETLARLESN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499562249  161 GQVLFRYLD---------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGSVDGLGLFAGLLE 217
Cdd:TIGR01737 160 DQVVFRYCDedgdvaeeaNPNGSVGNIAGIVNERGNVLGMMPHPERASEKLLGGDDGLKLFESLVE 225
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 3-216 8.95e-100

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: 289.13  E-value: 8.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   3 VGVIVFPGSNCDRDVQWVTAgLLGQSTRMIWHEE-----RDLSGLDLIVVPGGFSYGDYLRCGAIARFSP-AMQATVAFA 76
Cdd:cd01740    1 VAVLRFPGSNCDRDMAYAFE-LAGFEAEDVWHNDllagrKDLDDYDGVVLPGGFSYGDYLRAGAIAAASPlLMEEVKEFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  77 EAGGLVLGICNGFQILTEVGLLPGALVRNRDLHFRCET----TPLRVERSDRPWSRTYQQGQILNLPIAHGEGRYHADPA 152
Cdd:cd01740   80 ERGGLVLGICNGFQILVELGLLPGALIRNKGLKFICRWqnrfVTLRVENNDSPFTKGYMEGEVLRIPVAHGEGRFYADDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249 153 TLAALEANGQVLF----------RYLDNPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIA-----GSVDGLGLFAGLL 216
Cdd:cd01740  160 TLAELEENGQIAQyvdddgnvteRYPANPNGSLDGIAGICNEDGRVLGMMPHPERAVEPWQwerllGGSDGLKLFRNAV 238
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-198 2.33e-53

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 172.25  E-value: 2.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   1 MNVGVIVFPGSNCDRDVqwVTA-GLLGQSTRMIwH------EERDLSGLDLIVVPGGFSYGDYLRCGAI--ARFSP-AMQ 70
Cdd:PRK01175   4 IRVAVLRMEGTNCEDET--VKAfRRLGVEPEYV-HindlaaERKSVSDYDCLVIPGGFSAGDYIRAGAIfaARLKAvLRK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  71 ATVAFAEAGGLVLGICNGFQILTEVGLLPG----------ALVRNRDLHFRCETTPLRVERSDRPWSRTYQQGqILNLPI 140
Cdd:PRK01175  81 DIEEFIDEGYPIIGICNGFQVLVELGLLPGfdeiaekpemALTVNESNRFECRPTYLKKENRKCIFTKLLKKD-VFQVPV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249 141 AHGEGR-YHADPATLAALEANGQVLFRYLD----------NPNGSCNDIAGITNVAGNVLGMMPHPERA 198
Cdd:PRK01175 160 AHAEGRvVFSEEEILERLIENDQIVFRYVDengnyagypwNPNGSIYNIAGITNEKGNVIGLMPHPERA 228
GATase_5 pfam13507
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ...
 2-205 7.43e-49

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: 160.36  E-value: 7.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    2 NVGVIVFPGSNCDRDVQWV--TAGLLGQSTRM--IWHEERDLSGLDLIVVPGGFSYGDYLrcGA---IA---RFSPAMQA 71
Cdd:pfam13507   3 RVAILREPGTNGEYEMAAAfeRAGFDAVDVHMsdLLSGRVSLDDFQGLAAPGGFSYGDVL--GSgkgWAasiLFNPKLRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   72 TVA--FAEAGGLVLGICNGFQILTEVGLLPG----------ALVRNRDLHFRCETTPLRVErSDRPWSRTyQQGQILNLP 139
Cdd:pfam13507  81 AFEafFNRPDTFSLGICNGCQLLSKLGLIPGgegdlaerwpTLTRNDSGRFESRWVNVKIS-EKSPSVFL-RGMDGSGLP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249  140 IAHGEGR-YHADPATLAALEANGQVLFRYLD-----------NPNGSCNDIAGITNVAGNVLGMMPHPERAAEAIAGS 205
Cdd:pfam13507 159 VAHGEGRfVFRSEEVLARLEANGQVALRYVDnagnpteeypfNPNGSPLGIAGICSPDGRVLGLMPHPERVFRPWQWP 236
FGAM_synt TIGR01735
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ...
 37-205 2.87e-31

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: 120.66  E-value: 2.87e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    37 RDLSGLDLIVVPGGFSYGDYLRCG----AIARFSPAMQATVA--FAEAGGLVLGICNGFQILTEV-GLLPG-----ALVR 104
Cdd:TIGR01735 1096 VHLDEFRGLAACGGFSYGDVLGAGkgwaKSILFNPRLRDQFQafFKRPDTFSLGVCNGCQMLSNLlEWIPGtenwpHFVR 1175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   105 NRDLHFRCETTPLRVERSDRPWSRTyQQGQILNLPIAHGEGR-YHADPATLAALEANGQVLFRYLD-----------NPN 172
Cdd:TIGR01735 1176 NNSERFEARVASVRVGESPSIMLRG-MAGSRLPVAVAHGEGYaAFSSPELQAQADASGLAALRYIDddgnpteayplNPN 1254

                          170       180       190
                   ....*....|....*....|....*....|...
gi 499562249   173 GSCNDIAGITNVAGNVLGMMPHPERAAEAIAGS 205
Cdd:TIGR01735 1255 GSPGGIAGITSCDGRVTIMMPHPERVFRAWQNS 1287
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
 45-197 1.74e-27

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 109.50  E-value: 1.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   45 IVVPGGFSYGDYLRCG-----AIaRFSPAMQATVA--FAEAGGLVLGICNGFQILTEVGLL-PGA-----LVRNRDLHFR 111
Cdd:PRK05297 1084 LVACGGFSYGDVLGAGegwakSI-LFNPRLRDQFEafFARPDTFALGVCNGCQMMSNLKEIiPGAehwprFVRNRSEQFE 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  112 CETTPLRVERSDrpwSRTYQ--QGQILNLPIAHGEGRYHADPATLAALEANGQVLFRYLD-----------NPNGSCNDI 178
Cdd:PRK05297 1163 ARFSLVEVQESP---SIFLQgmAGSRLPIAVAHGEGRAEFPDAHLAALEAKGLVALRYVDnhgqvtetypaNPNGSPNGI 1239

                         170
                  ....*....|....*....
gi 499562249  179 AGITNVAGNVLGMMPHPER 197
Cdd:PRK05297 1240 TGLTTADGRVTIMMPHPER 1258
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 3-198 2.80e-19

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 85.97  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249    3 VGVIVFPGSNCDRDV--QWVTAGLlgqstrmiwhEERDLSGLDL------------IVVPGGFSYGDYLRCG----AIAR 64
Cdd:PLN03206 1040 VAIIREEGSNGDREMaaAFYAAGF----------EPWDVTMSDLlngrislddfrgIVFVGGFSYADVLDSAkgwaGSIR 1109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   65 FS-PAMQATVAF-AEAGGLVLGICNGFQILTEVGLLPGA----------------LVRNRDLHFRCETTPLRVERSdrPw 126
Cdd:PLN03206 1110 FNePLLQQFQEFyNRPDTFSLGVCNGCQLMALLGWVPGPqvggglgaggdpsqprFVHNESGRFECRFTSVTIEDS--P- 1186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  127 SRTYQ--QGQILNLPIAHGEGRYH-ADPATLAALEANGQVLFRYLD-----------NPNGSCNDIAGITNVAGNVLGMM 192
Cdd:PLN03206 1187 AIMLKgmEGSTLGVWAAHGEGRAYfPDESVLDEVLKSNLAPVRYCDddgepteqypfNPNGSPLGIAALCSPDGRHLAMM 1266


                  ....*.
gi 499562249  193 PHPERA 198
Cdd:PLN03206 1267 PHPERC 1272
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-92 5.68e-09

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: 52.22  E-value: 5.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   3 VGVIVFPGSNCDRDVQWVTA-GLLGQSTRMIWHEE------RDLSGLDLIVVPGGFSYGDYLRcgaiaRFSPAMQATVAF 75
Cdd:cd01653    1 VAVLLFPGFEELELASPLDAlREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLA-----RDEALLALLREA 75

                         90
                 ....*....|....*..
gi 499562249  76 AEAGGLVLGICNGFQIL 92
Cdd:cd01653   76 AAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-92 2.40e-08

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: 49.89  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   3 VGVIVFPGSNCDRDVQWVTA-GLLGQSTRMIWHEE------RDLSGLDLIVVPGGFSYGDYLRcgaiaRFSPAMQATVAF 75
Cdd:cd03128    1 VAVLLFGGSEELELASPLDAlREAGAEVDVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLA-----WDEALLALLREA 75

                         90
                 ....*....|....*..
gi 499562249  76 AEAGGLVLGICNGFQIL 92
Cdd:cd03128   76 AAAGKPVLGICLGAQLL 92
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 35-100 1.43e-06

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: 46.64  E-value: 1.43e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499562249  35 EERDLSGLDLIVVPGGFSYGDYLRcgaiarFSPAMQATV-AFAEAGGLVLGICNGFQILTEVGLLPG 100
Cdd:COG0693   58 DDVDPDDYDALVLPGGHGAPDDLR------EDPDVVALVrEFYEAGKPVAAICHGPAVLAAAGLLKG 118
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 43-100 9.88e-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: 44.17  E-value: 9.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249   43 DLIVVPGGFSYGDYLRcgaiaRFSPAMQATVAFAEAGGLVLGICNGFQILTEVGLLPG 100
Cdd:pfam01965  63 DALVLPGGRAGPERLR-----DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKG 115
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
43-99 1.09e-05

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 44.54  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249   43 DLIVVPGGFSYGDYLrcgAIARFSPAMQATVAFAEAGGLVLGICNGFQILTE------------VGLLP 99
Cdd:pfam07685  44 DLIILPGGKPTIQDL---ALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGEtiedpegvriegLGLLD 109
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 43-100 1.32e-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: 43.69  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249  43 DLIVVPGGFSyGDYLRCgaiarfSPAMQATV-AFAEAGGLVLGICNGFQILTEVGLLPG 100
Cdd:cd03134   64 DALVIPGGTN-PDKLRR------DPDAVAFVrAFAEAGKPVAAICHGPWVLISAGVVRG 115
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 38-92 2.07e-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: 43.77  E-value: 2.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499562249  38 DLSGLDLIVVPGGFSYG---DYLRCGAIARfspamqATVAFAEAGGLVLGICNGFQIL 92
Cdd:cd01750   34 GLGDADLIILPGSKDTIqdlAWLRKRGLAE------AIKNYARAGGPVLGICGGYQML 85
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 16-92 3.86e-04

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: 40.81  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  16 DVQWVTAGllgqstrmiwheeRDLSGLDLIVVPGgfS---YGD--YLRCGAIArfspamQATVAFAEAGGLVLGICNGFQ 90
Cdd:COG1492  278 RLRYVRPP-------------EELGDADLVILPG--SkntIADlaWLRESGLD------DAIRAHARRGGPVLGICGGYQ 336


                 ..
gi 499562249  91 IL 92
Cdd:COG1492  337 ML 338
PRK00784 PRK00784
cobyric acid synthase;
2-92 4.71e-04

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 40.45  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249   2 NVGVIVFPG-SN----------CDRDVQWVTAGllgqstrmiwheeRDLSGLDLIVVPGgfS---YGD--YLRCGAIARf 65
Cdd:PRK00784 253 RIAVIRLPRiSNftdfdplraePGVDVRYVRPG-------------EPLPDADLVILPG--SkntIADlaWLRESGWDE- 316

                         90       100
                 ....*....|....*....|....*..
gi 499562249  66 spamqATVAFAEAGGLVLGICNGFQIL 92
Cdd:PRK00784 317 -----AIRAHARRGGPVLGICGGYQML 338
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 38-201 1.83e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 38.19  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  38 DLSGLDLIVVPGgfsygdylrCGAiarFSPAMQ---------ATVAFAEAGGLVLGICNGFQILTE----------VGLL 98
Cdd:PRK13141  34 EILAADGVILPG---------VGA---FPDAMAnlrergldeVIKEAVASGKPLLGICLGMQLLFEsseefgetegLGLL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499562249  99 PGALVRnrdlhFRCEtTPLRVersdrP---WSRtyqqgqiLNLpiahgegryHADPATLAALEANGQVLF---RYLDNPN 172
Cdd:PRK13141 102 PGRVRR-----FPPE-EGLKV-----PhmgWNQ-------LEL---------KKESPLLKGIPDGAYVYFvhsYYADPCD 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 499562249 173 GScnDIAGITN--------VA-GNVLGMMPHPERAAEA 201
Cdd:PRK13141 155 EE--YVAATTDygvefpaaVGkDNVFGAQFHPEKSGDV 190
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 36-101 3.14e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 37.53  E-value: 3.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499562249  36 ERDLSGLDLIVVPGGFSYgdylrcgaiaRFSPAMQATVAFAEAGGL-VLGICNGFQILT-----EVGLLPGA 101
Cdd:cd01746   50 EEALKGADGILVPGGFGI----------RGVEGKILAIKYARENNIpFLGICLGMQLAViefarNVLGLPDA 111
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 43-100 5.38e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which 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.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 36.47  E-value: 5.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499562249  43 DLIVVPGGfsygdylRCGAIARFSPAMQATVA-FAEAGGLVLGICNGFQILTEVGLLPG 100
Cdd:cd03169   78 DALVIPGG-------RAPEYLRLDEKVLAIVRhFAEANKPVAAICHGPQILAAAGVLKG 129
 
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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