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Conserved domains on  [gi|1969806676|ref|NP_001378940|]
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bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase isoform 4 [Homo sapiens]

Protein Classification

SAICAR_synt_Ade5 and purE domain-containing protein( domain architecture ID 10619781)

protein containing domains Myb_DNA-bind_4, SAICAR_synt_Ade5, and purE

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; ...
361-619 1.52e-172

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: 496.04  E-value: 1.52e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 361 LNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAvtsyksnRIKTAFTR 440
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEA-------GIKTHFVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQ 520
Cdd:cd01416    74 QCSPTAFIARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 521 TEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTP 600
Cdd:cd01416   154 KEVDIMTKSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTD 233
                         250
                  ....*....|....*....
gi 1969806676 601 EGLQMVKKNFEWVAERVEL 619
Cdd:cd01416   234 EALQEVKKNYEWVADKLEL 252
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782 6.73e-63

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: 207.86  E-value: 6.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 629 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 708
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1969806676 709 ISCP-PLTPDWGVQDVWSSLRLPSGLGCSTVLSPEG--SAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIR 782
Cdd:TIGR01162  80 IGVPvPSKALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235 1.59e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 80.77  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 151 GKHWTVPEVRALIDIWSDKSIQRQLEGTVRNKRIFQQIAAKLQKFGIDRDWKQCRTKYKNLKHEYKIVRtAQDLGMTKSM 230
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 1969806676 231 KFFTE 235
Cdd:pfam13837  80 PFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91 4.39e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 73.84  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676   6 GKHWTEEEVKALLSVWAEknIRKQLYG--TLRNKGIFIYIAKRLQSLGVYRDWKQCWAKYKNLKYEYRTVKyaHNSGDSS 83
Cdd:pfam13837   1 RNKWTEEETLALIEIWGE--RLELRFQesKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK--EGNNGSG 76

                  ....*...
gi 1969806676  84 KTMKFFHD 91
Cdd:pfam13837  77 SSWPFFEE 84
 
Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
361-619 1.52e-172

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: 496.04  E-value: 1.52e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 361 LNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAvtsyksnRIKTAFTR 440
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEA-------GIKTHFVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQ 520
Cdd:cd01416    74 QCSPTAFIARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 521 TEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTP 600
Cdd:cd01416   154 KEVDIMTKSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTD 233
                         250
                  ....*....|....*....
gi 1969806676 601 EGLQMVKKNFEWVAERVEL 619
Cdd:cd01416   234 EALQEVKKNYEWVADKLEL 252
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
366-601 6.12e-88

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 276.94  E-value: 6.12e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 366 KLYEGKTKEVYELLDsPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEavtsyksNRIKTAFTRKCGET 445
Cdd:pfam01259   1 LLYEGKVKDVYETDD-PDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEI-------AGIPTHFIKSLSGR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 446 AFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcfaglLIGQTEVDI 525
Cdd:pfam01259  73 EMLVKKVKIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALG------LATEEEAEE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 526 MSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGD--RSQQK-DKQSYRD----LKEV 598
Cdd:pfam01259 147 IRELALKINEILKEYAAERGIILVDTKLEFGLD-SDGEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRDdlgdVEEA 225

                  ...
gi 1969806676 599 TPE 601
Cdd:pfam01259 226 YQE 228
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782 6.73e-63

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: 207.86  E-value: 6.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 629 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 708
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1969806676 709 ISCP-PLTPDWGVQDVWSSLRLPSGLGCSTVLSPEG--SAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIR 782
Cdd:TIGR01162  80 IGVPvPSKALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
364-622 3.45e-59

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 200.72  E-value: 3.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 364 GKKLYEGKTKEVYELlDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEavtsyksNRIKTAFTRKCG 443
Cdd:PRK09362    4 KELLYEGKAKIVYST-DDPDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEE-------AGIPTHFIEKLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 444 ETAFIAPQCEMIPIEWVCRRIATGSFLKRNpGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcfaglLIGQTEV 523
Cdd:PRK09362   76 DREQLVKKVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALG------WATPEEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 524 DIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEG 602
Cdd:PRK09362  149 AEIKELALKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETNEKLdKDRFRRD 218
                         250       260
                  ....*....|....*....|
gi 1969806676 603 LQMVKKNFEWVAERVELLLK 622
Cdd:PRK09362  219 LGGVIEAYEEVLKRLGELLE 238
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
361-594 1.86e-57

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: 196.07  E-value: 1.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 361 LNIGKKLYEGKTKEVYELLDspGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAVtsyksnrIKTAFTR 440
Cdd:COG0152     1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIG-------IPTHFIE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcf 513
Cdd:COG0152    72 TLSGREMLVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALG--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 514 aglLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGDRsQQKDKQSYR 593
Cdd:COG0152   149 ---LATEEEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFR 223

                  .
gi 1969806676 594 D 594
Cdd:COG0152   224 D 224
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
629-765 2.88e-53

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: 181.03  E-value: 2.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 629 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 708
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 709 ISCPPLTPDW-GVQDVWSSLRLPSGLGCSTVL--SPEGSAQFAAQIFGLSNHLVWSKLRA 765
Cdd:pfam00731  80 IGVPVKSSALdGLDSLLSIVQMPSGVPVATVAigGAKNAALLAAQILALSDPELAEKLKE 139
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
627-774 1.22e-47

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: 165.78  E-value: 1.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676  627 CRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAY 706
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1969806676  707 PVISCPPLTPDW-GVQDVWSSLRLPSGLGCSTVL----SPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISL 774
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATVAigidGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235 1.59e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 80.77  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 151 GKHWTVPEVRALIDIWSDKSIQRQLEGTVRNKRIFQQIAAKLQKFGIDRDWKQCRTKYKNLKHEYKIVRtAQDLGMTKSM 230
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 1969806676 231 KFFTE 235
Cdd:pfam13837  80 PFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91 4.39e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 73.84  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676   6 GKHWTEEEVKALLSVWAEknIRKQLYG--TLRNKGIFIYIAKRLQSLGVYRDWKQCWAKYKNLKYEYRTVKyaHNSGDSS 83
Cdd:pfam13837   1 RNKWTEEETLALIEIWGE--RLELRFQesKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK--EGNNGSG 76

                  ....*...
gi 1969806676  84 KTMKFFHD 91
Cdd:pfam13837  77 SSWPFFEE 84
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
628-712 3.07e-12

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: 65.08  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 628 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 707
Cdd:COG0041     2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80

                  ....*
gi 1969806676 708 VISCP 712
Cdd:COG0041    81 VIGVP 85
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
152-219 7.79e-11

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 58.06  E-value: 7.79e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1969806676 152 KHWTVPEVRALIdiwsdkSIQRQLE----GTVRNKRIFQQIAAKLQKFGIDRDWKQCRTKYKNLKHEYKIVR 219
Cdd:cd12203     1 KRWPREETLSLI------RLRREMEsrfqETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
613-765 4.45e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 56.61  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 613 VAERVELLLKSES-QC--------RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIp 683
Cdd:PLN02948  388 VEARLDQLLAEESaDPdalpkgtpLVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL- 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 684 TVFVAVAGRSNGLGPVMSGNTAYPVISCP-PLTPDWGVQDVWSSLRLPSGLGCSTVL--SPEGSAQFAAQIFGLSNHLVW 760
Cdd:PLN02948  467 QVIIAGAGGAAHLPGMVASMTPLPVIGVPvKTSHLDGLDSLLSIVQMPRGVPVATVAigNATNAGLLAVRMLGASDPDLL 546

                  ....*
gi 1969806676 761 SKLRA 765
Cdd:PLN02948  547 DKMEA 551
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
7-74 1.30e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 49.20  E-value: 1.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1969806676   7 KHWTEEEVKALLSVWAEKNIRKQlyGTLRNKGIFIYIAKRLQSLGVYRDWKQCWAKYKNLKYEYRTVK 74
Cdd:cd12203     1 KRWPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
 
Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
361-619 1.52e-172

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: 496.04  E-value: 1.52e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 361 LNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAvtsyksnRIKTAFTR 440
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEA-------GIKTHFVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQ 520
Cdd:cd01416    74 QCSPTAFIARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 521 TEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTP 600
Cdd:cd01416   154 KEVDIMTKSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTD 233
                         250
                  ....*....|....*....
gi 1969806676 601 EGLQMVKKNFEWVAERVEL 619
Cdd:cd01416   234 EALQEVKKNYEWVADKLEL 252
SAICAR_synt cd00476
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; SAICAR synthetase ...
366-618 2.98e-104

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: 319.79  E-value: 2.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 366 KLYEGKTKEVYELLDspGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAvtsyksnRIKTAFTRKCGET 445
Cdd:cd00476     1 TLYRGKTKIVYETKD--GVLLLEFKDDISAGDGARRNFLDEKGDITAKLTLFIFKYLSEA-------GIPTHFVERLGPR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 446 AFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFcfagllIGQTEVDI 525
Cdd:cd00476    72 TLLVDKLK*IPLEVVVRNRATGSFVKRYGGFKEGREFPPPLVEFFYKDDAEHDPIVSEDQLERLGF------IGKVDVER 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 526 MSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVtTKEIVLADVIDNDSWRLWPSGDRSQQKDkqsyrdlKEVTPEGLQM 605
Cdd:cd00476   146 *KELAVKINTVLKKLFSPAGLELWDFKLEFGLDE-EGEIVLGDEISPDSSRLWRKGGEPYDKD-------LFRRRASLGQ 217
                         250
                  ....*....|...
gi 1969806676 606 VKKNFEWVAERVE 618
Cdd:cd00476   218 IIEKYEEVAELVR 230
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
366-601 6.12e-88

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 276.94  E-value: 6.12e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 366 KLYEGKTKEVYELLDsPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEavtsyksNRIKTAFTRKCGET 445
Cdd:pfam01259   1 LLYEGKVKDVYETDD-PDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEI-------AGIPTHFIKSLSGR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 446 AFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcfaglLIGQTEVDI 525
Cdd:pfam01259  73 EMLVKKVKIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALG------LATEEEAEE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 526 MSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGD--RSQQK-DKQSYRD----LKEV 598
Cdd:pfam01259 147 IRELALKINEILKEYAAERGIILVDTKLEFGLD-SDGEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRDdlgdVEEA 225

                  ...
gi 1969806676 599 TPE 601
Cdd:pfam01259 226 YQE 228
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782 6.73e-63

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: 207.86  E-value: 6.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 629 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 708
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1969806676 709 ISCP-PLTPDWGVQDVWSSLRLPSGLGCSTVLSPEG--SAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIR 782
Cdd:TIGR01162  80 IGVPvPSKALSGLDSLLSIVQMPSGVPVATVAIGNAgnAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
364-622 3.45e-59

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 200.72  E-value: 3.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 364 GKKLYEGKTKEVYELlDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEavtsyksNRIKTAFTRKCG 443
Cdd:PRK09362    4 KELLYEGKAKIVYST-DDPDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEE-------AGIPTHFIEKLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 444 ETAFIAPQCEMIPIEWVCRRIATGSFLKRNpGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcfaglLIGQTEV 523
Cdd:PRK09362   76 DREQLVKKVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALG------WATPEEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 524 DIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEG 602
Cdd:PRK09362  149 AEIKELALKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETNEKLdKDRFRRD 218
                         250       260
                  ....*....|....*....|
gi 1969806676 603 LQMVKKNFEWVAERVELLLK 622
Cdd:PRK09362  219 LGGVIEAYEEVLKRLGELLE 238
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
361-594 1.86e-57

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: 196.07  E-value: 1.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 361 LNIGKKLYEGKTKEVYELLDspGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAVtsyksnrIKTAFTR 440
Cdd:COG0152     1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIG-------IPTHFIE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcf 513
Cdd:COG0152    72 TLSGREMLVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALG--- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 514 aglLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWPSGDRsQQKDKQSYR 593
Cdd:COG0152   149 ---LATEEEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFR 223

                  .
gi 1969806676 594 D 594
Cdd:COG0152   224 D 224
SAICAR_synt_PurC cd01415
bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) ...
366-619 9.32e-55

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: 188.43  E-value: 9.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 366 KLYEGKTKEVYELlDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEavtsyksNRIKTAFTRKCGET 445
Cdd:cd01415     1 LLYEGKAKIVYAT-DDPDVLIVEFKDDATAFNGKKKDTIEGKGVLNNEISALIFKYLEE-------NGIKTHFIEKLSDR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 446 AFIAPQCEMIPIEWVCRRIATGSFLKRNpGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKfcfaglLIGQTEVDI 525
Cdd:cd01415    73 EQLVKKVEIIPLEVVVRNIAAGSLVKRL-GIEEGTVLDPPIVEFYYKNDELGDPLINEDHILALG------LATEEELKE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 526 MSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDvTTKEIVLADVIDNDSWRLWpsgdrsqqkDKQSYRDL-KEVTPEGLQ 604
Cdd:cd01415   146 IKELALKINEVLSEFFAEIGIILVDFKLEFGRD-KDGEIVLADEISPDTCRLW---------DKETGEKLdKDRFRRDLG 215
                         250
                  ....*....|....*
gi 1969806676 605 MVKKNFEWVAERVEL 619
Cdd:cd01415   216 DVIEAYEEVLKRLGE 230
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
629-765 2.88e-53

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: 181.03  E-value: 2.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 629 VVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYPV 708
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 709 ISCPPLTPDW-GVQDVWSSLRLPSGLGCSTVL--SPEGSAQFAAQIFGLSNHLVWSKLRA 765
Cdd:pfam00731  80 IGVPVKSSALdGLDSLLSIVQMPSGVPVATVAigGAKNAALLAAQILALSDPELAEKLKE 139
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
627-774 1.22e-47

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: 165.78  E-value: 1.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676  627 CRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAY 706
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1969806676  707 PVISCPPLTPDW-GVQDVWSSLRLPSGLGCSTVL----SPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISL 774
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATVAigidGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235 1.59e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 80.77  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 151 GKHWTVPEVRALIDIWSDKSIQRQLEGTVRNKRIFQQIAAKLQKFGIDRDWKQCRTKYKNLKHEYKIVRtAQDLGMTKSM 230
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 1969806676 231 KFFTE 235
Cdd:pfam13837  80 PFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91 4.39e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 73.84  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676   6 GKHWTEEEVKALLSVWAEknIRKQLYG--TLRNKGIFIYIAKRLQSLGVYRDWKQCWAKYKNLKYEYRTVKyaHNSGDSS 83
Cdd:pfam13837   1 RNKWTEEETLALIEIWGE--RLELRFQesKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK--EGNNGSG 76

                  ....*...
gi 1969806676  84 KTMKFFHD 91
Cdd:pfam13837  77 SSWPFFEE 84
SAICAR_synt_Sc cd01414
non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
366-594 3.56e-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: 73.74  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 366 KLYEGKTKEVYELLDspGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAVTS-----YKSNRIKTAFTR 440
Cdd:cd01414     1 LIYSGKVRDVYDLGD--GRLLFVATDRISAFDVILPPDIPGKGEVLTQISAFWFELTEDIIPNhlistDVEDLPEIKEPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 441 KCGETAFIAPQCEMIPIEWVCRRIATGSFLKR------------NPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIA 508
Cdd:cd01414    79 DPDGRSMVVKKAKPIPIECIVRGYLTGSGWKEyqkggtvcgiklPEGLREAQKLPEPIFTPSTKAEEGHDENISFEEAVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 509 akfcfaglLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVtTKEIVLADVIDN-DSWRLWPSGDRSQQK 587
Cdd:cd01414   159 --------IIGAELADELRELALALYERAAEYAAKRGLILADTKFEFGLDE-NGEIILIDEVLTpDSSRFWPADSYEPGK 229
                         250
                  ....*....|..
gi 1969806676 588 -----DKQSYRD 594
Cdd:cd01414   230 eqpsfDKQFVRD 241
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
628-712 3.07e-12

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: 65.08  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 628 RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIpTVFVAVAGRSNGLGPVMSGNTAYP 707
Cdd:COG0041     2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80

                  ....*
gi 1969806676 708 VISCP 712
Cdd:COG0041    81 VIGVP 85
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
152-219 7.79e-11

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 58.06  E-value: 7.79e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1969806676 152 KHWTVPEVRALIdiwsdkSIQRQLE----GTVRNKRIFQQIAAKLQKFGIDRDWKQCRTKYKNLKHEYKIVR 219
Cdd:cd12203     1 KRWPREETLSLI------RLRREMEsrfqETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
613-765 4.45e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 56.61  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 613 VAERVELLLKSES-QC--------RVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIp 683
Cdd:PLN02948  388 VEARLDQLLAEESaDPdalpkgtpLVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL- 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 684 TVFVAVAGRSNGLGPVMSGNTAYPVISCP-PLTPDWGVQDVWSSLRLPSGLGCSTVL--SPEGSAQFAAQIFGLSNHLVW 760
Cdd:PLN02948  467 QVIIAGAGGAAHLPGMVASMTPLPVIGVPvKTSHLDGLDSLLSIVQMPRGVPVATVAigNATNAGLLAVRMLGASDPDLL 546

                  ....*
gi 1969806676 761 SKLRA 765
Cdd:PLN02948  547 DKMEA 551
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
7-74 1.30e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 49.20  E-value: 1.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1969806676   7 KHWTEEEVKALLSVWAEKNIRKQlyGTLRNKGIFIYIAKRLQSLGVYRDWKQCWAKYKNLKYEYRTVK 74
Cdd:cd12203     1 KRWPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
PRK12607 PRK12607
phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
448-616 9.97e-06

phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional


Pssm-ID: 183621 [Multi-domain]  Cd Length: 313  Bit Score: 48.35  E-value: 9.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 448 IAPQCEMIPIEWVCRRIATGSFL------KRN------P-GVKEGYKFYPPKVELFFK-DDANNDPQWSEEQLIAakfcf 513
Cdd:PRK12607   88 VGKRCEPFPVEMVVRGYLAGSTWrlykagKREmygvtlPdGLRENQKLPEPIITPTTKaEEGGHDEPISPEEILA----- 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806676 514 AGLLiGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKeIVLADVIDN-DSWRLWpsgdrsqqkDKQSY 592
Cdd:PRK12607  163 QGLL-TPEDWDELSKYALALFARGQEMAAERGLILVDTKYEFGKDADGR-IVLIDEIHTpDSSRYW---------YADGY 231
                         170       180
                  ....*....|....*....|....*...
gi 1969806676 593 RDL--KEVTPEGLQmvkKNF--EWVAER 616
Cdd:PRK12607  232 EERfaAGEPQEQLD---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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