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Conserved domains on  [gi|2038121376|ref|XP_041417948|]
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multifunctional protein ADE2-like isoform X1 [Xenopus laevis]

Protein Classification

5-(carboxyamino)imidazole ribonucleotide mutase; phosphoribosylaminoimidazolesuccinocarboxamide synthase( domain architecture ID 10619781)

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; ...
565-816 2.64e-179

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: 519.93  E-value: 2.64e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 565 LKLGKKLNEGKTKEVYELPEHPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAF 644
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 645 IATHCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLSCAGLVIGQAEVDIMT 724
Cdd:cd01416    81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 725 HSTAAIFEILEKAWMTQECTLVDMKIEFGVDVTKKEIVLADVIDNDSWRLWPAGDKSQQKDKQTYRELKEVTPEALQMVK 804
Cdd:cd01416   161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                         250
                  ....*....|..
gi 2038121376 805 RNFEWVADRVEL 816
Cdd:cd01416   241 KNYEWVADKLEL 252
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
826-979 1.64e-51

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: 177.81  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 826 VVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYPV 905
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038121376 906 INCP-PLTADWGAQDVWSSLRMPSGLGCSTVLSPEAAAQFAAQIF--GLNNHLVWCKLRSCTLNTWISLKQADMKLR 979
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 ...
6-90 2.88e-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: 74.61  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376   6 GRYWTEDEVRALISIWSEKNIRKQLHGTLRNKGLFLYIAKRMQQLGVSRDWKQCRAKYKNLKYEYRAIKcGHAIEDDAKM 85
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 2038121376  86 RFYNE 90
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 ...
310-395 8.47e-15

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: 70.37  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 310 GKHWTTEETQALITIWSEESIRKQLEGVVRNRQIFEHIASLLQKQGIDRGWRQCRTKYKNLKHDYivaKKAMDSGFKRKT 389
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*..
gi 2038121376 390 T-KFFHE 395
Cdd:pfam13837  78 SwPFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
148-231 6.96e-14

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: 67.68  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 148 GKHWTSREINALINIWSDRNICRQLKGTVRNQKIFEHIAKLLKEAGIDRDWRQCRTKYKNLKHEYvvvKKAQECGNDSKR 227
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*
gi 2038121376 228 M-KYF 231
Cdd:pfam13837  78 SwPFF 82
 
Name Accession Description Interval E-value
SAICAR_synt_Ade5 cd01416
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
565-816 2.64e-179

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: 519.93  E-value: 2.64e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 565 LKLGKKLNEGKTKEVYELPEHPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAF 644
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 645 IATHCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLSCAGLVIGQAEVDIMT 724
Cdd:cd01416    81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 725 HSTAAIFEILEKAWMTQECTLVDMKIEFGVDVTKKEIVLADVIDNDSWRLWPAGDKSQQKDKQTYRELKEVTPEALQMVK 804
Cdd:cd01416   161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                         250
                  ....*....|..
gi 2038121376 805 RNFEWVADRVEL 816
Cdd:cd01416   241 KNYEWVADKLEL 252
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
570-798 5.45e-86

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 275.39  E-value: 5.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 570 KLNEGKTKEVYELpEHPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIATHC 649
Cdd:pfam01259   1 LLYEGKVKDVYET-DDPDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEIAGIPTHFIKSLSGREMLVKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 650 EMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQAEVDIMTHSTAA 729
Cdd:pfam01259  80 KIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALGL------ATEEEAEEIRELALK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038121376 730 IFEILEKAWMTQECTLVDMKIEFGVDVTkKEIVLADVIDNDSWRLWPAGD--KSQQK-DKQTYR----ELKEVTPE 798
Cdd:pfam01259 154 INEILKEYAAERGIILVDTKLEFGLDSD-GEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRddlgDVEEAYQE 228
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
565-790 1.76e-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: 198.00  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 565 LKLGKKLNEGKTKEVYELPEhpGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAF 644
Cdd:COG0152     1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIGIPTHFIETLSGREM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 645 IATHCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQ 717
Cdd:COG0152    79 LVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALGL------ATE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376 718 AEVDIMTHSTAAIFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDNDSWRLWPAGDKsQQKDKQTYR 790
Cdd:COG0152   153 EEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFR 223
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
568-819 2.10e-55

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 191.86  E-value: 2.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 568 GKKLNEGKTKEVYELPEhPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIAT 647
Cdd:PRK09362    4 KELLYEGKAKIVYSTDD-PDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEEAGIPTHFIEKLSDREQLVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 648 HCEMIPIEWVCRRIATGSFLKRNpGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQAEVDIMTHST 727
Cdd:PRK09362   83 KVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALGW------ATPEELAEIKELA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 728 AAIFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDNDSWRLWpagDKSQQK--DKQTYR-ELKEVTpEAlqmvk 804
Cdd:PRK09362  156 LKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---DKETNEklDKDRFRrDLGGVI-EA----- 225
                         250
                  ....*....|....*
gi 2038121376 805 rnFEWVADRVELLLK 819
Cdd:PRK09362  226 --YEEVLKRLGELLE 238
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
826-979 1.64e-51

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: 177.81  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 826 VVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYPV 905
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038121376 906 INCP-PLTADWGAQDVWSSLRMPSGLGCSTVLSPEAAAQFAAQIF--GLNNHLVWCKLRSCTLNTWISLKQADMKLR 979
Cdd:TIGR01162  80 IGVPvPSKALSGLDSLLSIVQMPSGVPVATVAIGNAGNAALLAAQilGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
826-936 6.55e-45

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: 158.69  E-value: 6.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 826 VVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYPV 905
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2038121376 906 INCPPLTADWGAQD-VWSSLRMPSGLGCSTVL 936
Cdd:pfam00731  80 IGVPVKSSALDGLDsLLSIVQMPSGVPVATVA 111
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
824-961 5.33e-39

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: 141.90  E-value: 5.33e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376  824 GRVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAY 903
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376  904 PVINCPPLTADW-GAQDVWSSLRMPSGLGCSTVL----SPEAAAQFAAQIFGLNNHLVWCKLR 961
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATVAigidGAFNAALLAAQILALNDPELAAKLA 142
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-90 2.88e-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: 74.61  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376   6 GRYWTEDEVRALISIWSEKNIRKQLHGTLRNKGLFLYIAKRMQQLGVSRDWKQCRAKYKNLKYEYRAIKcGHAIEDDAKM 85
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 2038121376  86 RFYNE 90
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 ...
310-395 8.47e-15

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: 70.37  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 310 GKHWTTEETQALITIWSEESIRKQLEGVVRNRQIFEHIASLLQKQGIDRGWRQCRTKYKNLKHDYivaKKAMDSGFKRKT 389
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*..
gi 2038121376 390 T-KFFHE 395
Cdd:pfam13837  78 SwPFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
148-231 6.96e-14

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: 67.68  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 148 GKHWTSREINALINIWSDRNICRQLKGTVRNQKIFEHIAKLLKEAGIDRDWRQCRTKYKNLKHEYvvvKKAQECGNDSKR 227
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*
gi 2038121376 228 M-KYF 231
Cdd:pfam13837  78 SwPFF 82
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
825-909 1.30e-11

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: 63.54  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 825 RVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYP 904
Cdd:COG0041     2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80

                  ....*
gi 2038121376 905 VINCP 909
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 ...
9-74 4.10e-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: 59.22  E-value: 4.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038121376   9 WTEDEVRALISIWSEKNIRKQlhGTLRNKGLFLYIAKRMQQLGVSRDWKQCRAKYKNLKYEYRAIK 74
Cdd:cd12203     3 WPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
311-374 3.43e-08

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: 51.13  E-value: 3.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038121376 311 KHWTTEETQALITIWSEESIRKQleGVVRNRQIFEHIASLLQKQGIDRGWRQCRTKYKNLKHDY 374
Cdd:cd12203     1 KRWPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYY 62
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
825-935 3.64e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 57.38  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 825 RVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYP 904
Cdd:PLN02948  412 LVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL-QVIIAGAGGAAHLPGMVASMTPLP 490
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2038121376 905 VINCP-PLTADWGAQDVWSSLRMPSGLGCSTV 935
Cdd:PLN02948  491 VIGVPvKTSHLDGLDSLLSIVQMPRGVPVATV 522
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
149-216 4.29e-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: 48.05  E-value: 4.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038121376 149 KHWTSREINALINIWSD---RNIcrqlkGTVRNQKIFEHIAKLLKEAGIDRDWRQCRTKYKNLKHEYVVVK 216
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; ...
565-816 2.64e-179

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: 519.93  E-value: 2.64e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 565 LKLGKKLNEGKTKEVYELPEHPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAF 644
Cdd:cd01416     1 LKLGKKLIEGKTKIVYELPDQPGLVLIQSKDRITAGDGARKDEIEGKAAISNKTTSNVFELLQEAGIKTHFVKQCSPTAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 645 IATHCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLSCAGLVIGQAEVDIMT 724
Cdd:cd01416    81 IARKCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFSPPKLEFFYKDDANHDPQWSEEQLLEAKLNCGGLKIGKKEVDIMT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 725 HSTAAIFEILEKAWMTQECTLVDMKIEFGVDVTKKEIVLADVIDNDSWRLWPAGDKSQQKDKQTYRELKEVTPEALQMVK 804
Cdd:cd01416   161 KSTIAIFEILEKAWATQDCTLVDMKIEFGVDVTTGEILLADVIDNDSWRLWPSGDKRLMKDKQVYRNLKEVTDEALQEVK 240
                         250
                  ....*....|..
gi 2038121376 805 RNFEWVADRVEL 816
Cdd:cd01416   241 KNYEWVADKLEL 252
SAICAR_synt cd00476
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; SAICAR synthetase ...
570-815 2.10e-87

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: 279.35  E-value: 2.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 570 KLNEGKTKEVYELPEhpGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIATHC 649
Cdd:cd00476     1 TLYRGKTKIVYETKD--GVLLLEFKDDISAGDGARRNFLDEKGDITAKLTLFIFKYLSEAGIPTHFVERLGPRTLLVDKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 650 EMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKlscaglVIGQAEVDIMTHSTAA 729
Cdd:cd00476    79 K*IPLEVVVRNRATGSFVKRYGGFKEGREFPPPLVEFFYKDDAEHDPIVSEDQLERLG------FIGKVDVER*KELAVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 730 IFEILEKAWMTQECTLVDMKIEFGVDVtKKEIVLADVIDNDSWRLWPAGDKSQQKDkqtyrelKEVTPEALQMVKRNFEW 809
Cdd:cd00476   153 INTVLKKLFSPAGLELWDFKLEFGLDE-EGEIVLGDEISPDSSRLWRKGGEPYDKD-------LFRRRASLGQIIEKYEE 224

                  ....*.
gi 2038121376 810 VADRVE 815
Cdd:cd00476   225 VAELVR 230
SAICAR_synt pfam01259
SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.
570-798 5.45e-86

SAICAR synthetase; Also known as Phosphoribosylaminoimidazole-succinocarboxamide synthase.


Pssm-ID: 460140  Cd Length: 228  Bit Score: 275.39  E-value: 5.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 570 KLNEGKTKEVYELpEHPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIATHC 649
Cdd:pfam01259   1 LLYEGKVKDVYET-DDPDTLLVVAKDRISAFDGVKKGTIPGKGAVNNQISAFWFELLEIAGIPTHFIKSLSGREMLVKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 650 EMIPIEWVCRRIATGSFLKRNPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQAEVDIMTHSTAA 729
Cdd:pfam01259  80 KIIPLEVVVRNYAAGSLGKRLPGLKEGTKLPEPIFEPSTKADALGDPNINEEHIVALGL------ATEEEAEEIRELALK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038121376 730 IFEILEKAWMTQECTLVDMKIEFGVDVTkKEIVLADVIDNDSWRLWPAGD--KSQQK-DKQTYR----ELKEVTPE 798
Cdd:pfam01259 154 INEILKEYAAERGIILVDTKLEFGLDSD-GEIVLADEITPDSSRFWDADTyeKSQESlDKDRFRddlgDVEEAYQE 228
PurC COG0152
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
565-790 1.76e-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: 198.00  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 565 LKLGKKLNEGKTKEVYELPEhpGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAF 644
Cdd:COG0152     1 MPKLELLYEGKVKDVYATDD--DTLLMVFKDRISAFDGVKPDPIPGKGEVLNQISAFWFELLEDIGIPTHFIETLSGREM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 645 IATHCEMIPIEWVCRRIATGSFLKR-------NPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQ 717
Cdd:COG0152    79 LVKKLEMIPVEVVVRNYAAGSLWKRyqagialPLGLEEGTKLPEPIFEPSTKADEGHDPNISEEHIVALGL------ATE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376 718 AEVDIMTHSTAAIFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDNDSWRLWPAGDKsQQKDKQTYR 790
Cdd:COG0152   153 EEAEELRELALKINERLSELAAERGIILVDTKLEFGRD-ADGEIVLADEITPDSSRLWDADTY-ESLDKDRFR 223
PRK09362 PRK09362
phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed
568-819 2.10e-55

phosphoribosylaminoimidazole-succinocarboxamide synthase; Reviewed


Pssm-ID: 181800  Cd Length: 238  Bit Score: 191.86  E-value: 2.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 568 GKKLNEGKTKEVYELPEhPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIAT 647
Cdd:PRK09362    4 KELLYEGKAKIVYSTDD-PDLLIVEFKDDATAFNGEKKEQIDGKGVLNNQISSFIFKKLEEAGIPTHFIEKLSDREQLVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 648 HCEMIPIEWVCRRIATGSFLKRNpGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQAEVDIMTHST 727
Cdd:PRK09362   83 KVEIIPLEVVVRNVAAGSLVKRL-GIEEGTVLPPPIVEFYYKNDALGDPMINEDHILALGW------ATPEELAEIKELA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 728 AAIFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDNDSWRLWpagDKSQQK--DKQTYR-ELKEVTpEAlqmvk 804
Cdd:PRK09362  156 LKINDVLKGLFAGAGIRLVDFKLEFGRD-KDGEIVLADEISPDTCRLW---DKETNEklDKDRFRrDLGGVI-EA----- 225
                         250
                  ....*....|....*
gi 2038121376 805 rnFEWVADRVELLLK 819
Cdd:PRK09362  226 --YEEVLKRLGELLE 238
SAICAR_synt_PurC cd01415
bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) ...
570-790 1.57e-52

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: 183.42  E-value: 1.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 570 KLNEGKTKEVYELPEhPGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLQEAGIKTAFVRKCSDAAFIATHC 649
Cdd:cd01415     1 LLYEGKAKIVYATDD-PDVLIVEFKDDATAFNGKKKDTIEGKGVLNNEISALIFKYLEENGIKTHFIEKLSDREQLVKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 650 EMIPIEWVCRRIATGSFLKRNpGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLISAKLscaglvIGQAEVDIMTHSTAA 729
Cdd:cd01415    80 EIIPLEVVVRNIAAGSLVKRL-GIEEGTVLDPPIVEFYYKNDELGDPLINEDHILALGL------ATEEELKEIKELALK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376 730 IFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDNDSWRLWpagDKSQQK--DKQTYR 790
Cdd:cd01415   153 INEVLSEFFAEIGIILVDFKLEFGRD-KDGEIVLADEISPDTCRLW---DKETGEklDKDRFR 211
purE TIGR01162
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
826-979 1.64e-51

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: 177.81  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 826 VVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYPV 905
Cdd:TIGR01162   1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGI-KVIIAGAGGAAHLPGMVAALTPLPV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038121376 906 INCP-PLTADWGAQDVWSSLRMPSGLGCSTVLSPEAAAQFAAQIF--GLNNHLVWCKLRSCTLNTWISLKQADMKLR 979
Cdd:TIGR01162  80 IGVPvPSKALSGLDSLLSIVQMPSGVPVATVAIGNAGNAALLAAQilGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
AIRC pfam00731
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
826-936 6.55e-45

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: 158.69  E-value: 6.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 826 VVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYPV 905
Cdd:pfam00731   1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGL-KVIIAGAGGAAHLPGMVAALTTLPV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2038121376 906 INCPPLTADWGAQD-VWSSLRMPSGLGCSTVL 936
Cdd:pfam00731  80 IGVPVKSSALDGLDsLLSIVQMPSGVPVATVA 111
AIRC smart01001
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
824-961 5.33e-39

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: 141.90  E-value: 5.33e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376  824 GRVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAY 903
Cdd:smart01001   1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGI-KVIIAGAGGAAHLPGVVAALTTL 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376  904 PVINCPPLTADW-GAQDVWSSLRMPSGLGCSTVL----SPEAAAQFAAQIFGLNNHLVWCKLR 961
Cdd:smart01001  80 PVIGVPVSSGYLgGLDSLLSIVQMPSGIPVATVAigidGAFNAALLAAQILALNDPELAAKLA 142
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-90 2.88e-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: 74.61  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376   6 GRYWTEDEVRALISIWSEKNIRKQLHGTLRNKGLFLYIAKRMQQLGVSRDWKQCRAKYKNLKYEYRAIKcGHAIEDDAKM 85
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEK-EGNNGSGSSW 79

                  ....*
gi 2038121376  86 RFYNE 90
Cdd:pfam13837  80 PFFEE 84
SAICAR_synt_Sc cd01414
non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; ...
570-787 4.57e-15

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: 76.82  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 570 KLNEGKTKEVYELPEhpGCVLMKSKDLITAGDAVRKDHMEGKASISNKTTSCVFKLLqEAGIKTAFV------------- 636
Cdd:cd01414     1 LIYSGKVRDVYDLGD--GRLLFVATDRISAFDVILPPDIPGKGEVLTQISAFWFELT-EDIIPNHLIstdvedlpeikep 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 637 RKCSDAAFIATHCEMIPIEWVCRRIATGSFLKR------------NPGVKEGYKFLPPKVETFFKDDANHDPQWSEEQLI 704
Cdd:cd01414    78 EDPDGRSMVVKKAKPIPIECIVRGYLTGSGWKEyqkggtvcgiklPEGLREAQKLPEPIFTPSTKAEEGHDENISFEEAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 705 SaklscaglVIGQAEVDIMTHSTAAIFEILEKAWMTQECTLVDMKIEFGVDVtKKEIVLADVIDN-DSWRLWPAGDKSQQ 783
Cdd:cd01414   158 E--------IIGAELADELRELALALYERAAEYAAKRGLILADTKFEFGLDE-NGEIILIDEVLTpDSSRFWPADSYEPG 228

                  ....*....
gi 2038121376 784 K-----DKQ 787
Cdd:cd01414   229 KeqpsfDKQ 237
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
310-395 8.47e-15

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: 70.37  E-value: 8.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 310 GKHWTTEETQALITIWSEESIRKQLEGVVRNRQIFEHIASLLQKQGIDRGWRQCRTKYKNLKHDYivaKKAMDSGFKRKT 389
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*..
gi 2038121376 390 T-KFFHE 395
Cdd:pfam13837  78 SwPFFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
148-231 6.96e-14

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: 67.68  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 148 GKHWTSREINALINIWSDRNICRQLKGTVRNQKIFEHIAKLLKEAGIDRDWRQCRTKYKNLKHEYvvvKKAQECGNDSKR 227
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKY---RKEKEGNNGSGS 77

                  ....*
gi 2038121376 228 M-KYF 231
Cdd:pfam13837  78 SwPFF 82
PurE COG0041
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
825-909 1.30e-11

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: 63.54  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 825 RVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYP 904
Cdd:COG0041     2 KVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGL-KVIIAGAGGAAHLPGMVAAKTTLP 80

                  ....*
gi 2038121376 905 VINCP 909
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 ...
9-74 4.10e-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: 59.22  E-value: 4.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038121376   9 WTEDEVRALISIWSEKNIRKQlhGTLRNKGLFLYIAKRMQQLGVSRDWKQCRAKYKNLKYEYRAIK 74
Cdd:cd12203     3 WPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
311-374 3.43e-08

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: 51.13  E-value: 3.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038121376 311 KHWTTEETQALITIWSEESIRKQleGVVRNRQIFEHIASLLQKQGIDRGWRQCRTKYKNLKHDY 374
Cdd:cd12203     1 KRWPREETLSLIRLRREMESRFQ--ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYY 62
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
825-935 3.64e-08

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 57.38  E-value: 3.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 825 RVVVLMGSISDLAHCEKIKKSCANYGIPCELRVTSAHKGPDETLRIKSEYDGDGIpTVFIAVAGRSNGLGPVMSGNTAYP 904
Cdd:PLN02948  412 LVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGL-QVIIAGAGGAAHLPGMVASMTPLP 490
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2038121376 905 VINCP-PLTADWGAQDVWSSLRMPSGLGCSTV 935
Cdd:PLN02948  491 VIGVPvKTSHLDGLDSLLSIVQMPRGVPVATV 522
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
149-216 4.29e-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: 48.05  E-value: 4.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038121376 149 KHWTSREINALINIWSD---RNIcrqlkGTVRNQKIFEHIAKLLKEAGIDRDWRQCRTKYKNLKHEYVVVK 216
Cdd:cd12203     1 KRWPREETLSLIRLRREmesRFQ-----ETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
PRK12607 PRK12607
phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional
574-777 5.64e-07

phosphoribosylaminoimidazole-succinocarboxamide synthase; Provisional


Pssm-ID: 183621 [Multi-domain]  Cd Length: 313  Bit Score: 52.58  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 574 GKTKEVYELPEhpGCVLMKSKDLITAGDAVrkdhMEG---KASISNKTTSCVFKllQEAGIKTAFVRKCSDAAF-IATHC 649
Cdd:PRK12607   21 GKVRDNYDLPD--GRRVMVATDRISAFDRV----LPAipyKGQVLNQTAAFWFE--ATKDICPNHVLAVPDPNVvVGKRC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 650 EMIPIEWVCRRIATGSFL------KRN------P-GVKEGYKFLPPKVETFFK-DDANHDPQWSEEQLISaklscAGLVi 715
Cdd:PRK12607   93 EPFPVEMVVRGYLAGSTWrlykagKREmygvtlPdGLRENQKLPEPIITPTTKaEEGGHDEPISPEEILA-----QGLL- 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038121376 716 GQAEVDIMTHSTAAIFEILEKAWMTQECTLVDMKIEFGVDVTKKeIVLADVIDN-DSWRLWPA 777
Cdd:PRK12607  167 TPEDWDELSKYALALFARGQEMAAERGLILVDTKYEFGKDADGR-IVLIDEIHTpDSSRYWYA 228
PLN02544 PLN02544
phosphoribosylaminoimidazole-succinocarboxamide synthase
567-778 5.57e-06

phosphoribosylaminoimidazole-succinocarboxamide synthase


Pssm-ID: 178159 [Multi-domain]  Cd Length: 370  Bit Score: 49.82  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 567 LGKKLnEGKTKEVYELPEHpgcVLMKSKDLITAGDAVRKdHMEGKASISNKTTSCVFKLLQEAgIKTAFVRKCSDAAFIA 646
Cdd:PLN02544   75 LGSRR-RGKVRDIYDLGDY---LVLVTTDRQSAFDRVLA-SIPFKGQVLNQTSAWWFNNTKHI-TPNALVSSPDPNVTIA 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038121376 647 THCEMIPIEWVCRRIATGS-----FLKRNPGVKE--GYKF---------LPPKVETFFKDDANHDPQWSEEQLISAKLsc 710
Cdd:PLN02544  149 KKCSVFPVEFVVRGYMTGStstslWTVYNKGVRNycGNDLpdgmvknqkLPANILTPTTKAADHDVPISPEEIVEEGL-- 226
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038121376 711 aglvIGQAEVDIMTHSTAAIFEILEKAWMTQECTLVDMKIEFGVDvTKKEIVLADVIDN-DSWRLWPAG 778
Cdd:PLN02544  227 ----MTQEDFDEVSSKALALFAFGQEVAAEHGLILVDTKYEFGKD-ADGTILLIDEVHTpDSSRYWLAD 290
 
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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