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Conserved domains on  [gi|1002263223|ref|XP_015635960|]
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stem-specific protein TSJT1 [Oryza sativa Japonica Group]

Protein Classification

class II glutamine amidotransferase domain-containing protein; asparagine synthetase domain-containing protein( domain architecture ID 10575738)

class II glutamine amidotransferase domain-containing protein may hydrolyze ammonia from glutamine and transfer the amino group to the appropriate substrate; asparagine synthetase domain-containing protein (ASNSD) such as ASNSD1 contains an N-terminal class-II glutamine amidotransferase domain and a C-terminal asparagine synthase B domain belonging to the adenine nucleotide alpha hydrolase (AANH) superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
2-231 7.99e-146

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


:

Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 407.14  E-value: 7.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223   2 LAIFQKQVAHAPAELNSPRS---SAAKPKNPDEILRDFHALHPiEAFSTSFGGGAALACVAGHARnglSGYERMFCGLDD 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSstsSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN---PLLPRLFAVVDD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  79 IYCVFMGRLDNLSSLIRQYGLcSRSTNEALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEV 158
Cdd:pfam12481  77 IFCLFQGHLENLASLKQQYGL-SKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002263223 159 PLYWGIAADGSVVICDEREIVKGGCGKSYAPFPVGCMFHSEGGLKSFEHPMNRLKAMPRVDSEGVMCGATFKV 231
Cdd:pfam12481 156 PLYWGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
2-231 7.99e-146

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 407.14  E-value: 7.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223   2 LAIFQKQVAHAPAELNSPRS---SAAKPKNPDEILRDFHALHPiEAFSTSFGGGAALACVAGHARnglSGYERMFCGLDD 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSstsSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN---PLLPRLFAVVDD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  79 IYCVFMGRLDNLSSLIRQYGLcSRSTNEALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEV 158
Cdd:pfam12481  77 IFCLFQGHLENLASLKQQYGL-SKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002263223 159 PLYWGIAADGSVVICDEREIVKGGCGKSYAPFPVGCMFHSEGGLKSFEHPMNRLKAMPRVDSEGVMCGATFKV 231
Cdd:pfam12481 156 PLYWGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-231 9.25e-142

This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.


Pssm-ID: 238891 [Multi-domain]  Cd Length: 224  Bit Score: 396.68  E-value: 9.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223   2 LAIFQKQVAHAPAELNSPRSSAAKpKNPDEILRDFHALHPIEAFSTsfggGAALACVAGHARNGLSGYERMFCGLDDIYC 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSRTPA-KTAEELLKRFLSANPSAVFVH----LGAAGFLAYSHHNQSPLHPRLFAVKDDIFC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  82 VFMGRLDNLSSLIRQYGLCsRSTNEALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLY 161
Cdd:cd01910    76 LFQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLY 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223 162 WGIAADGSVVICDEREIVKGGCGKSYAPFPVGCMFHSEGGLKSFEHPMNRLKAMPRVDSEGVMCGATFKV 231
Cdd:cd01910   155 WGIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
127-208 1.34e-08

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 55.16  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223 127 QVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVVICDEREIVKGGCgKSYAPFPVGCMFHS-EGGLKSF 205
Cdd:PLN02549  112 EFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDC-ERFEEFPPGHYYSSkAGGFRRW 190

                  ...
gi 1002263223 206 EHP 208
Cdd:PLN02549  191 YNP 193
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
2-231 7.99e-146

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 407.14  E-value: 7.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223   2 LAIFQKQVAHAPAELNSPRS---SAAKPKNPDEILRDFHALHPiEAFSTSFGGGAALACVAGHARnglSGYERMFCGLDD 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSstsSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN---PLLPRLFAVVDD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  79 IYCVFMGRLDNLSSLIRQYGLcSRSTNEALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEV 158
Cdd:pfam12481  77 IFCLFQGHLENLASLKQQYGL-SKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002263223 159 PLYWGIAADGSVVICDEREIVKGGCGKSYAPFPVGCMFHSEGGLKSFEHPMNRLKAMPRVDSEGVMCGATFKV 231
Cdd:pfam12481 156 PLYWGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-231 9.25e-142

This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.


Pssm-ID: 238891 [Multi-domain]  Cd Length: 224  Bit Score: 396.68  E-value: 9.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223   2 LAIFQKQVAHAPAELNSPRSSAAKpKNPDEILRDFHALHPIEAFSTsfggGAALACVAGHARNGLSGYERMFCGLDDIYC 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSRTPA-KTAEELLKRFLSANPSAVFVH----LGAAGFLAYSHHNQSPLHPRLFAVKDDIFC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  82 VFMGRLDNLSSLIRQYGLCsRSTNEALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLY 161
Cdd:cd01910    76 LFQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLY 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223 162 WGIAADGSVVICDEREIVKGGCGKSYAPFPVGCMFHSEGGLKSFEHPMNRLKAMPRVDSEGVMCGATFKV 231
Cdd:cd01910   155 WGIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
28-196 9.98e-22

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 89.82  E-value: 9.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  28 NPDEILRDFHALHPIEAFSTSFGGGAALACVAGHAR---NGLSGYER---MFCGLDDIYCVFMGRLDNLSSLIRQY---G 98
Cdd:cd00352    41 DGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRlatNGLPSEANaqpFRSEDGRIALVHNGEIYNYRELREELearG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  99 LCSRSTN--EALLVIEAYRTLRDRGPYPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVVICDER 176
Cdd:cd00352   121 YRFEGESdsEVILHLLERLGREGGLFEAVEDALKRLDGPFAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEP 200
                         170       180
                  ....*....|....*....|
gi 1002263223 177 EIVKGGCGKSYAPFPVGCMF 196
Cdd:cd00352   201 KALLALPFKGVRRLPPGELL 220
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
127-208 1.34e-08

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 55.16  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223 127 QVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVVICDEREIVKGGCgKSYAPFPVGCMFHS-EGGLKSF 205
Cdd:PLN02549  112 EFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDC-ERFEEFPPGHYYSSkAGGFRRW 190

                  ...
gi 1002263223 206 EHP 208
Cdd:PLN02549  191 YNP 193
asnB PRK09431
asparagine synthetase B; Provisional
129-201 2.54e-08

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 54.14  E-value: 2.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002263223 129 VKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVVICDEREIVKGGCgKSYAPFPVGCMFHSEGG 201
Cdd:PRK09431  115 LDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSKDG 186
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
123-193 1.15e-07

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 52.02  E-value: 1.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002263223 123 YPADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVVICDEREIVKGGCGKsYAPFPVG 193
Cdd:PTZ00077  116 YGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPG 185
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
82-171 1.54e-05

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.


Pssm-ID: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 43.28  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  82 VFMGRLDNLSSLIRQY---GLCSRSTNEALLVIEAYRtlRDRGPypadQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEV 158
Cdd:pfam13537  27 VFNGEIYNYRELRAELeakGYRFRTHSDTEVILHLYE--AEWGE----DCVDRLNGMFAFAIWDRRRQRLFLARDRFGIK 100
                          90
                  ....*....|...
gi 1002263223 159 PLYWGIAADGSVV 171
Cdd:pfam13537 101 PLYYGRDDGGRLL 113
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
43-171 1.53e-03

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 37.67  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002263223  43 EAFSTSFGGGAALacvaGHAR---NGLS--GYERMFCGLDDIYCVFMGRLDNLSSLIRQYGL-----CSRSTNEALLVie 112
Cdd:pfam13522   2 DFSGIWVEGGVAL----GHVRlaiVDLPdaGNQPMLSRDGRLVLVHNGEIYNYGELREELADlghafRSRSDTEVLLA-- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002263223 113 AYRTLrdrgpypADQVVKDLSGSFAFVVFDNKSGAVFAALSTDGEVPLYWGIAADGSVV 171
Cdd:pfam13522  76 LYEEW-------GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVF 127
 
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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