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Conserved domains on  [gi|1709928|sp|P51583|]
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RecName: Full=Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase; Short=PAICS; Includes: RecName: Full=Phosphoribosylaminoimidazole carboxylase; AltName: Full=AIR carboxylase; Short=AIRC; Includes: RecName: Full=Phosphoribosylaminoimidazole succinocarboxamide synthetase; AltName: Full=SAICAR synthetase

Protein Classification

5-(carboxyamino)imidazole ribonucleotide mutase; phosphoribosylaminoimidazolesuccinocarboxamide synthase( domain architecture ID 10105473)

5-(carboxyamino)imidazole ribonucleotide mutase (PurE) catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR)| phosphoribosylaminoimidazolesuccinocarboxamide synthase catalyzes the conversion of 5-aminoimidazole-4-carboxyribonucleotide (CAIR) to 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) in the de novo biosynthesis of purine nucleotides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
7-258 0e+00

Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


:

Pssm-ID: 133471  Cd Length: 252  Bit Score: 511.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    7 LNIGRKLYEGKTKEVYELLDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAF 86
Cdd:cd01416   1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   87 IAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFCFAGLVIGQTEVDIMS 166
Cdd:cd01416  81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  167 HATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVK 246
Cdd:cd01416 161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                       250
                ....*....|..
gi 1709928  247 KNFEWVADRVEL 258
Cdd:cd01416 241 KNYEWVADKLEL 252
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
268-421 9.02e-68

phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


:

Pssm-ID: 273474  Cd Length: 156  Bit Score: 212.48  E-value: 9.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    268 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 347
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709928    348 ISCPPIT-ADWGAQDVWSSLRLPSGIGCSTILSPEG--SAQFAAQIFGLNNHLVWAKLRASKLNTWISLKQADKKIR 421
Cdd:TIGR01162  80 IGVPVPSkALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
 
Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
7-258 0e+00

Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


Pssm-ID: 133471  Cd Length: 252  Bit Score: 511.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    7 LNIGRKLYEGKTKEVYELLDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAF 86
Cdd:cd01416   1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   87 IAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFCFAGLVIGQTEVDIMS 166
Cdd:cd01416  81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  167 HATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVK 246
Cdd:cd01416 161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                       250
                ....*....|..
gi 1709928  247 KNFEWVADRVEL 258
Cdd:cd01416 241 KNYEWVADKLEL 252
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
12-240 6.35e-96

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 286.95  E-value: 6.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     12 KLYEGKTKEVYELLDsPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQC 91
Cdd:pfam01259   1 LLYEGKVKDVYETDD-PDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEIAGIPTHFIKSLSGREMLVKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     92 EMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFcfaglvIGQTEVDIMSHATQA 171
Cdd:pfam01259  80 KIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALGL------ATEEEAEEIRELALK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709928    172 IFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGD--RSQQK-DKQSYRD----LKEVTPE 240
Cdd:pfam01259 154 INEILKEYAAERGIILVDTKLEFGLD-SDGEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRDdlgdVEEAYQE 228
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
268-421 9.02e-68

phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273474  Cd Length: 156  Bit Score: 212.48  E-value: 9.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    268 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 347
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709928    348 ISCPPIT-ADWGAQDVWSSLRLPSGIGCSTILSPEG--SAQFAAQIFGLNNHLVWAKLRASKLNTWISLKQADKKIR 421
Cdd:TIGR01162  80 IGVPVPSkALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
10-261 2.20e-65

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 209.19  E-value: 2.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    10 GRKLYEGKTKEVYELlDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAP 89
Cdd:PRK09362   4 KELLYEGKAKIVYST-DDPDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEEAGIPTHFIEKLSDREQLVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    90 QCEMIPIEWVCRRIATGSFLKRNpGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKfcfaglVIGQTEVDIMSHAT 169
Cdd:PRK09362  83 KVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALG------WATPEELAEIKELA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   170 QAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEGLQMVKKN 248
Cdd:PRK09362 156 LKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETNEKLdKDRFRRDLGGVIEA 225
                        250
                 ....*....|...
gi 1709928   249 FEWVADRVELLLK 261
Cdd:PRK09362 226 YEEVLKRLGELLE 238
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
7-233 2.42e-63

Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole-succinocarboxamide synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439922  Cd Length: 245  Bit Score: 204.16  E-value: 2.42e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    7 LNIGRKLYEGKTKEVYELLDspGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAF 86
Cdd:COG0152   1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIGIPTHFIETLSGREM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   87 IAPQCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKfcfaglVIGQ 159
Cdd:COG0152  79 LVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALG------LATE 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709928  160 TEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGDRsQQKDKQSYRD 233
Cdd:COG0152 153 EEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFRD 224
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
268-408 1.54e-55

AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.


Pssm-ID: 459917  Cd Length: 147  Bit Score: 180.26  E-value: 1.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    268 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 347
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709928    348 ISCPPITADWGAQD-VWSSLRLPSGIGCST--ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLN 408
Cdd:pfam00731  80 IGVPVKSSALDGLDsLLSIVQMPSGVPVATvaIGGAKNAALLAAQILALSDPELAEKLKEYREE 143
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
266-413 2.50e-50

AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.


Pssm-ID: 214965  Cd Length: 152  Bit Score: 166.94  E-value: 2.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     266 CRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAY 345
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709928     346 PVISCPPITADW-GAQDVWSSLRLPSGIGCST----ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNTWISL 413
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATvaigIDGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
267-404 1.24e-13

Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439811  Cd Length: 161  Bit Score: 68.16  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  267 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 346
Cdd:COG0041   2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709928  347 VISCpPITAdwGAQDVWSSL----RLPSGIGCSTiLSPEGS---AQFAAQIFGLNNHLVWAKLRA 404
Cdd:COG0041  81 VIGV-PVKS--KALDGLDSLlsivQMPPGVPVAT-VAIGGAknaALLAAQILALKDPELAEKLKA 141
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
267-409 5.57e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 55.07  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   267 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 346
Cdd:PLN02948 412 LVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL-QVIIAGAGGAAHLPGMVASMTPLP 490
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709928   347 VISCP-PITADWGAQDVWSSLRLPSGIGCST--ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNT 409
Cdd:PLN02948 491 VIGVPvKTSHLDGLDSLLSIVQMPRGVPVATvaIGNATNAGLLAVRMLGASDPDLLDKMEAYQEDM 556
 
Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
7-258 0e+00

Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


Pssm-ID: 133471  Cd Length: 252  Bit Score: 511.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    7 LNIGRKLYEGKTKEVYELLDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAF 86
Cdd:cd01416   1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   87 IAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFCFAGLVIGQTEVDIMS 166
Cdd:cd01416  81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  167 HATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVK 246
Cdd:cd01416 161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                       250
                ....*....|..
gi 1709928  247 KNFEWVADRVEL 258
Cdd:cd01416 241 KNYEWVADKLEL 252
SAICAR_synt cd00476
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; SAICAR synthetase ...
12-257 4.92e-111

5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; SAICAR synthetase (the PurC gene product) catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


Pssm-ID: 133468  Cd Length: 230  Bit Score: 325.57  E-value: 4.92e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   12 KLYEGKTKEVYELLDspGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQC 91
Cdd:cd00476   1 TLYRGKTKIVYETKD--GVLLLEFKDDISAGDGARRNFLDEKGDITAKLTLFIFKYLSEAGIPTHFVERLGPRTLLVDKL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   92 EMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFcfaglvIGQTEVDIMSHATQA 171
Cdd:cd00476  79 K*IPLEVVVRNRATGSFVKRYGGFKEGREFPPPLVEFFYKDDAEHDPIVSEDQLERLGF------IGKVDVER*KELAVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  172 IFEILEKSWLPQNCTLVDMKIEFGVDVtTKEIVLADVIDNDSWRLWPSGDRSQQKDkqsyrdlKEVTPEGLQMVKKNFEW 251
Cdd:cd00476 153 INTVLKKLFSPAGLELWDFKLEFGLDE-EGEIVLGDEISPDSSRLWRKGGEPYDKD-------LFRRRASLGQIIEKYEE 224

                ....*.
gi 1709928  252 VADRVE 257
Cdd:cd00476 225 VAELVR 230
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
12-240 6.35e-96

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 286.95  E-value: 6.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     12 KLYEGKTKEVYELLDsPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQC 91
Cdd:pfam01259   1 LLYEGKVKDVYETDD-PDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEIAGIPTHFIKSLSGREMLVKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     92 EMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFcfaglvIGQTEVDIMSHATQA 171
Cdd:pfam01259  80 KIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALGL------ATEEEAEEIRELALK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709928    172 IFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGD--RSQQK-DKQSYRD----LKEVTPE 240
Cdd:pfam01259 154 INEILKEYAAERGIILVDTKLEFGLD-SDGEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRDdlgdVEEAYQE 228
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
268-421 9.02e-68

phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273474  Cd Length: 156  Bit Score: 212.48  E-value: 9.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    268 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 347
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709928    348 ISCPPIT-ADWGAQDVWSSLRLPSGIGCSTILSPEG--SAQFAAQIFGLNNHLVWAKLRASKLNTWISLKQADKKIR 421
Cdd:TIGR01162  80 IGVPVPSkALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
10-261 2.20e-65

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 209.19  E-value: 2.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    10 GRKLYEGKTKEVYELlDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAP 89
Cdd:PRK09362   4 KELLYEGKAKIVYST-DDPDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEEAGIPTHFIEKLSDREQLVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    90 QCEMIPIEWVCRRIATGSFLKRNpGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKfcfaglVIGQTEVDIMSHAT 169
Cdd:PRK09362  83 KVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALG------WATPEELAEIKELA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   170 QAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEGLQMVKKN 248
Cdd:PRK09362 156 LKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETNEKLdKDRFRRDLGGVIEA 225
                        250
                 ....*....|...
gi 1709928   249 FEWVADRVELLLK 261
Cdd:PRK09362 226 YEEVLKRLGELLE 238
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
7-233 2.42e-63

Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole-succinocarboxamide synthase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439922  Cd Length: 245  Bit Score: 204.16  E-value: 2.42e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    7 LNIGRKLYEGKTKEVYELLDspGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAF 86
Cdd:COG0152   1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIGIPTHFIETLSGREM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   87 IAPQCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKfcfaglVIGQ 159
Cdd:COG0152  79 LVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALG------LATE 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709928  160 TEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGDRsQQKDKQSYRD 233
Cdd:COG0152 153 EEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFRD 224
SAICAR_synt_PurC cd01415
bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) ...
12-258 1.66e-60

bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; A subfamily of SAICAR synthetases represented by the Thermotoga maritima (Tm) enzyme and E. coli PurC. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


Pssm-ID: 133470  Cd Length: 230  Bit Score: 196.13  E-value: 1.66e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   12 KLYEGKTKEVYELlDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQC 91
Cdd:cd01415   1 LLYEGKAKIVYAT-DDPDVLIVEFKDDATAFNGKKKDTIEGKGVLNNEISALIFKYLEENGIKTHFIEKLSDREQLVKKV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   92 EMIPIEWVCRRIATGSFLKRNpGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKfcfaglVIGQTEVDIMSHATQA 171
Cdd:cd01415  80 EIIPLEVVVRNIAAGSLVKRL-GIEEGTVLDPPIVEFYYKNDELGDPLINEDHILALG------LATEEELKEIKELALK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  172 IFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEGLQMVKKNFE 250
Cdd:cd01415 153 INEVLSEFFAEIGIILVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETGEKLdKDRFRRDLGDVIEAYE 222

                ....*...
gi 1709928  251 WVADRVEL 258
Cdd:cd01415 223 EVLKRLGE 230
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
268-408 1.54e-55

AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.


Pssm-ID: 459917  Cd Length: 147  Bit Score: 180.26  E-value: 1.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    268 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 347
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709928    348 ISCPPITADWGAQD-VWSSLRLPSGIGCST--ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLN 408
Cdd:pfam00731  80 IGVPVKSSALDGLDsLLSIVQMPSGVPVATvaIGGAKNAALLAAQILALSDPELAEKLKEYREE 143
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
266-413 2.50e-50

AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.


Pssm-ID: 214965  Cd Length: 152  Bit Score: 166.94  E-value: 2.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928     266 CRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAY 345
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709928     346 PVISCPPITADW-GAQDVWSSLRLPSGIGCST----ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNTWISL 413
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATvaigIDGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
SAICAR_synt_Sc cd01414
non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
12-233 1.01e-14

non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic, bacterial, and archaeal group of SAICAR synthetases represented by the Saccharomyces cerevisiae (Sc) enzyme, mostly absent in metazoans. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.


Pssm-ID: 133469 [Multi-domain]  Cd Length: 279  Bit Score: 74.12  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   12 KLYEGKTKEVYELLDspGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLqEAGIKTAFTKKCGET------- 84
Cdd:cd01414   1 LIYSGKVRDVYDLGD--GRLLFVATDRISAFDVILPPDIPGKGEVLTQISAFWFELT-EDIIPNHLISTDVEDlpeikep 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   85 ------AFIAPQCEMIPIEWVCRRIATGSFLKR------------NPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLI 146
Cdd:cd01414  78 edpdgrSMVVKKAKPIPIECIVRGYLTGSGWKEyqkggtvcgiklPEGLREAQKLPEPIFTPSTKAEEGHDENISFEEAV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  147 AakfcfaglVIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVtTKEIVLADVIDN-DSWRLWPSGDRSQQ 225
Cdd:cd01414 158 E--------IIGAELADELRELALALYERAAEYAAKRGLILADTKFEFGLDE-NGEIILIDEVLTpDSSRFWPADSYEPG 228
                       250
                ....*....|...
gi 1709928  226 K-----DKQSYRD 233
Cdd:cd01414 229 KeqpsfDKQFVRD 241
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
267-404 1.24e-13

Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439811  Cd Length: 161  Bit Score: 68.16  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928  267 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 346
Cdd:COG0041   2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709928  347 VISCpPITAdwGAQDVWSSL----RLPSGIGCSTiLSPEGS---AQFAAQIFGLNNHLVWAKLRA 404
Cdd:COG0041  81 VIGV-PVKS--KALDGLDSLlsivQMPPGVPVAT-VAIGGAknaALLAAQILALKDPELAEKLKA 141
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
267-409 5.57e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 55.07  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   267 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 346
Cdd:PLN02948 412 LVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL-QVIIAGAGGAAHLPGMVASMTPLP 490
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709928   347 VISCP-PITADWGAQDVWSSLRLPSGIGCST--ILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNT 409
Cdd:PLN02948 491 VIGVPvKTSHLDGLDSLLSIVQMPRGVPVATvaIGNATNAGLLAVRMLGASDPDLLDKMEAYQEDM 556
PRK12607 PRK12607
phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
13-255 3.93e-06

phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional


Pssm-ID: 183621 [Multi-domain]  Cd Length: 313  Bit Score: 48.35  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    13 LYEGKTKEVYELLDspGRVLLQSKDQITAGNAarknHLEG---KAAISNKITSCIFQllqeagiktaftkkcgETAFIAP 89
Cdd:PRK12607  18 VYRGKVRDNYDLPD--GRRVMVATDRISAFDR----VLPAipyKGQVLNQTAAFWFE----------------ATKDICP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928    90 ---------------QCEMIPIEWVCRRIATGSFL------KRN------P-GVKEGYRFYPPKVEMFFK-DDANNDPQW 140
Cdd:PRK12607  76 nhvlavpdpnvvvgkRCEPFPVEMVVRGYLAGSTWrlykagKREmygvtlPdGLRENQKLPEPIITPTTKaEEGGHDEPI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709928   141 SEEQLIAakfcfAGLViGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKeIVLADVIDN-DSWRLWps 219
Cdd:PRK12607 156 SPEEILA-----QGLL-TPEDWDELSKYALALFARGQEMAAERGLILVDTKYEFGKDADGR-IVLIDEIHTpDSSRYW-- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 1709928   220 gdrsqqkDKQSYRDL--KEVTPEGLQmvkKNF--EWVADR 255
Cdd:PRK12607 227 -------YADGYEERfaAGEPQEQLD---KEFvrQWLIER 256
 
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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