NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1229773311|ref|XP_022139643|]
View 

stem-specific protein TSJT1-like [Momordica charantia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-230 2.00e-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: 408.29  E-value: 2.00e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311   2 LAIFHKTFAHPPEELNSPAS-FSGSKTPKLPEETLKEFLSRHPhNTFSVNFGEAAVLAYVPPDRPfSLHQRLFCGFDEIY 80
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN-PLLPRLFAVVDDIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  81 CLFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPYPADQVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLY 160
Cdd:pfam12481  79 CLFQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311 161 WGIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMFHSEGGLMSFEHPLNKMKPMPRIDSEGAMCGANFKV 230
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-230 2.00e-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: 408.29  E-value: 2.00e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311   2 LAIFHKTFAHPPEELNSPAS-FSGSKTPKLPEETLKEFLSRHPhNTFSVNFGEAAVLAYVPPDRPfSLHQRLFCGFDEIY 80
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN-PLLPRLFAVVDDIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  81 CLFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPYPADQVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLY 160
Cdd:pfam12481  79 CLFQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311 161 WGIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMFHSEGGLMSFEHPLNKMKPMPRIDSEGAMCGANFKV 230
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-230 2.09e-141

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: 395.52  E-value: 2.09e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311   2 LAIFHKTFAHPPEELNSPASfsgSKTPKLPEETLKEFLSRHPHNTFsVNFGEAAVLAYVPpDRPFSLHQRLFCGFDEIYC 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGS---RTPAKTAEELLKRFLSANPSAVF-VHLGAAGFLAYSH-HNQSPLHPRLFAVKDDIFC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  82 LFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPYPADQVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLYW 161
Cdd:cd01910    76 LFQGHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229773311 162 GIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMFHSEGGLMSFEHPLNKMKPMPRIDSEGAMCGANFKV 230
Cdd:cd01910   156 GIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 126-207 9.47e-10

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 58.24  E-value: 9.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311 126 QVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLYWGIAADGSVVISDDVEVIKEGCAKsYAPFPTGCMFHS-EGGLMSF 204
Cdd:PLN02549  112 EFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDCER-FEEFPPGHYYSSkAGGFRRW 190


                  ...
gi 1229773311 205 EHP 207
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 ...
 2-230 2.00e-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: 408.29  E-value: 2.00e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311   2 LAIFHKTFAHPPEELNSPAS-FSGSKTPKLPEETLKEFLSRHPhNTFSVNFGEAAVLAYVPPDRPfSLHQRLFCGFDEIY 80
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHP-NAVSVNLGDSGFLAYSHHKQN-PLLPRLFAVVDDIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  81 CLFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPYPADQVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLY 160
Cdd:pfam12481  79 CLFQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311 161 WGIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMFHSEGGLMSFEHPLNKMKPMPRIDSEGAMCGANFKV 230
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-230 2.09e-141

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: 395.52  E-value: 2.09e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311   2 LAIFHKTFAHPPEELNSPASfsgSKTPKLPEETLKEFLSRHPHNTFsVNFGEAAVLAYVPpDRPFSLHQRLFCGFDEIYC 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGS---RTPAKTAEELLKRFLSANPSAVF-VHLGAAGFLAYSH-HNQSPLHPRLFAVKDDIFC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  82 LFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPYPADQVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLYW 161
Cdd:cd01910    76 LFQGHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229773311 162 GIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMFHSEGGLMSFEHPLNKMKPMPRIDSEGAMCGANFKV 230
Cdd:cd01910   156 GIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 67-195 9.88e-20

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: 84.42  E-value: 9.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311  67 SLHQRLFCGFDEIYCLFLGSLSNLCALNKQYGLSKGSNEAMFLIEAYRTLRDRGPY------PADQVLKDLDGSFAFVVY 140
Cdd:cd00352    86 ANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRegglfeAVEDALKRLDGPFAFALW 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1229773311 141 DSRAGAVFAALGADGGVKLYWGIAADGSVVISDDVEVIKEGCAKSYAPFPTGCMF 195
Cdd:cd00352   166 DGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 126-207 9.47e-10

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 58.24  E-value: 9.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229773311 126 QVLKDLDGSFAFVVYDSRAGAVFAALGADGGVKLYWGIAADGSVVISDDVEVIKEGCAKsYAPFPTGCMFHS-EGGLMSF 204
Cdd:PLN02549  112 EFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDCER-FEEFPPGHYYSSkAGGFRRW 190


                  ...
gi 1229773311 205 EHP 207
Cdd:PLN02549  191 YNP 193
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 131-192 1.67e-09

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 57.80  E-value: 1.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229773311 131 LDGSFAFVVYDSRAGAVFAALGADGGVKLYWGIAADGSVVISDDVEVIKEGCAKsYAPFPTG 192
Cdd:PTZ00077  125 LDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPG 185
asnB PRK09431
asparagine synthetase B; Provisional
 128-202 2.10e-08

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 54.14  E-value: 2.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229773311 128 LKDLDGSFAFVVYDSRAGAVFAALGADGGVKLYWGIAADGSVVISDDVEVIKEGCaKSYAPFPTGCMFHSEGGLM 202
Cdd:PRK09431  115 LDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSKDGEF 188
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 126-170 2.54e-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: 42.51  E-value: 2.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1229773311 126 QVLKDLDGSFAFVVYDSRAGAVFAA---LgadgGVK-LYWGIAADGSVV 170
Cdd:pfam13537  69 DCVDRLNGMFAFAIWDRRRQRLFLArdrF----GIKpLYYGRDDGGRLL 113
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 128-167 3.18e-03

Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.


Pssm-ID: 238364 [Multi-domain]  Cd Length: 220  Bit Score: 37.92  E-value: 3.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1229773311 128 LKDLDGSFAFVVYDSRAGAVFAA---LgadgGVK-LYWGIAADG 167
Cdd:cd00712   114 LERLNGMFAFALWDKRKRRLFLArdrF----GIKpLYYGRDGGG 153
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 124-173 7.59e-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: 35.74  E-value: 7.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1229773311 124 ADQVLKDLDGSFAFVVYDSRAGAVFaaLGADG-GVK-LYWGIAADGSVVISD 173
Cdd:pfam13522  81 GEDCLERLRGMFAFAIWDRRRRTLF--LARDRlGIKpLYYGILGGGFVFASE 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH