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Conserved domains on  [gi|79328089|ref|NP_001031900|]
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aluminum induced protein with YGL and LRDR motifs [Arabidopsis thaliana]

Protein Classification

class II glutamine amidotransferase domain-containing protein( domain architecture ID 1025)

class II glutamine amidotransferase domain-containing protein may hydrolyze ammonia from glutamine and transfer the amino group to the appropriate substrate

EC:  2.4.2.-
Gene Ontology:  GO:0016740|GO:0006541
PubMed:  9559052|8430515
SCOP:  3000131

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gn_AT_II super family cl00319
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-214 1.04e-131

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.


The actual alignment was detected with superfamily member cd01910:

Pssm-ID: 469719 [Multi-domain]  Cd Length: 224  Bit Score: 369.72  E-value: 1.04e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089   2 LGIFSGAIVSPPEELVAAGSRTPspKTTGSTLVNRFVEKNPSAVSVQVGDYVQLAYSHHNESPLRPRSFGAKDEIFCLFQ 81
Cdd:cd01910   1 LAVFSKAVAKPPEELVSAGSRTP--AKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089  82 GSLDNLGSLKQQYGLAKNANEVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGIT 161
Cdd:cd01910  79 GHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79328089 162 ADGYVAFADDVDLLK------------GCYYSTaLGGLRSFENPKNKITAVPAN--EGEIWGATFKV 214
Cdd:cd01910 159 ADGSVVFSDDVELVKascgksfapfpkGCFFHS-EGGLRSFEHPMNKLKAVPRVdsEGEMCGATFKV 224
 
Name Accession Description Interval E-value
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-214 1.04e-131

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: 369.72  E-value: 1.04e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089   2 LGIFSGAIVSPPEELVAAGSRTPspKTTGSTLVNRFVEKNPSAVSVQVGDYVQLAYSHHNESPLRPRSFGAKDEIFCLFQ 81
Cdd:cd01910   1 LAVFSKAVAKPPEELVSAGSRTP--AKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089  82 GSLDNLGSLKQQYGLAKNANEVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGIT 161
Cdd:cd01910  79 GHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79328089 162 ADGYVAFADDVDLLK------------GCYYSTaLGGLRSFENPKNKITAVPAN--EGEIWGATFKV 214
Cdd:cd01910 159 ADGSVVFSDDVELVKascgksfapfpkGCFFHS-EGGLRSFEHPMNKLKAVPRVdsEGEMCGATFKV 224
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-214 1.13e-125

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: 354.37  E-value: 1.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089     2 LGIFSGAIVSPPEELVAAGSRTPSP--KTTGSTLVNRFVEKNPSAVSVQVGDYVQLAYSHHNESPLRPRSFGAKDEIFCL 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSSTSSPalKKGFEELAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089    80 FQGSLDNLGSLKQQYGLAKNANEVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWG 159
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79328089   160 ITADGYVAFADDVDLLK------------GCYYSTAlGGLRSFENPKNKITAVPAN--EGEIWGATFKV 214
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKkgcgksfapfpkGCFFTSS-GGLRSFEHPMNKVKAVPRVdsEGVVCGATFKV 228
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 82-194 8.37e-11

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 60.93  E-value: 8.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089   82 GSLDNLGSLKQQYGLAKNAN----EVLLviEAYKTLrdrapypANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLY 157
Cdd:PLN02549  76 GEIYNHKELREKLKLHKFRTgsdcEVIA--HLYEEH-------GEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLY 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 79328089  158 WGITADGYVAFADDVDLLK-----------GCYYSTALGGLRSFENPK 194
Cdd:PLN02549 147 IGWGLDGSVWFASEMKALCddcerfeefppGHYYSSKAGGFRRWYNPP 194
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 102-169 1.97e-09

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 56.77  E-value: 1.97e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79328089 102 EVLLviEAYKTLRDRApypanhvVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITaDGYVAFA 169
Cdd:COG0367 101 EVIL--HAYEEWGEDC-------LERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAED-GGGLAFA 158
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 123-169 1.38e-07

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 51.18  E-value: 1.38e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 79328089   123 HVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITaDGYVAFA 169
Cdd:TIGR01536 112 ECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFA 157
 
Name Accession Description Interval E-value
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-214 1.04e-131

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: 369.72  E-value: 1.04e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089   2 LGIFSGAIVSPPEELVAAGSRTPspKTTGSTLVNRFVEKNPSAVSVQVGDYVQLAYSHHNESPLRPRSFGAKDEIFCLFQ 81
Cdd:cd01910   1 LAVFSKAVAKPPEELVSAGSRTP--AKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089  82 GSLDNLGSLKQQYGLAKNANEVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGIT 161
Cdd:cd01910  79 GHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79328089 162 ADGYVAFADDVDLLK------------GCYYSTaLGGLRSFENPKNKITAVPAN--EGEIWGATFKV 214
Cdd:cd01910 159 ADGSVVFSDDVELVKascgksfapfpkGCFFHS-EGGLRSFEHPMNKLKAVPRVdsEGEMCGATFKV 224
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-214 1.13e-125

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: 354.37  E-value: 1.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089     2 LGIFSGAIVSPPEELVAAGSRTPSP--KTTGSTLVNRFVEKNPSAVSVQVGDYVQLAYSHHNESPLRPRSFGAKDEIFCL 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSSTSSPalKKGFEELAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089    80 FQGSLDNLGSLKQQYGLAKNANEVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWG 159
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79328089   160 ITADGYVAFADDVDLLK------------GCYYSTAlGGLRSFENPKNKITAVPAN--EGEIWGATFKV 214
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKkgcgksfapfpkGCFFTSS-GGLRSFEHPMNKVKAVPRVdsEGVVCGATFKV 228
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 67-176 1.72e-17

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: 77.87  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089  67 PRSFGaKDEIFCLFQGSLDNLGSLKQQYGLAKNAN------EVLLVIEAYKTLRDRAPYPANHVVAHLSGDFAFVVFDKS 140
Cdd:cd00352  90 PFRSE-DGRIALVHNGEIYNYRELREELEARGYRFegesdsEVILHLLERLGREGGLFEAVEDALKRLDGPFAFALWDGK 168

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 79328089 141 TSTLFVASDQVGKVPLYWGITADGYVAFADDVDLLK 176
Cdd:cd00352 169 PDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALL 204
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 102-169 5.39e-11

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: 59.88  E-value: 5.39e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79328089 102 EVLLviEAYKTLRDRApypanhvVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITADGyVAFA 169
Cdd:cd00712 100 EVIL--HLYEEWGEDC-------LERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGG-LAFA 157
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 82-194 8.37e-11

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 60.93  E-value: 8.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089   82 GSLDNLGSLKQQYGLAKNAN----EVLLviEAYKTLrdrapypANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLY 157
Cdd:PLN02549  76 GEIYNHKELREKLKLHKFRTgsdcEVIA--HLYEEH-------GEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLY 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 79328089  158 WGITADGYVAFADDVDLLK-----------GCYYSTALGGLRSFENPK 194
Cdd:PLN02549 147 IGWGLDGSVWFASEMKALCddcerfeefppGHYYSSKAGGFRRWYNPP 194
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 119-179 1.57e-10

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 60.11  E-value: 1.57e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328089  119 YPANHVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITADGYVAFADDVDLLK-GCY 179
Cdd:PTZ00077 116 YGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHdQCV 177
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 80-169 2.75e-10

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: 56.16  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328089    80 FQGSLDNLGSLKQQYGLAKNA------NEVLLVIeayktLRDRAPypanHVVAHLSGDFAFVVFDKSTSTLFVASDQVGK 153
Cdd:pfam13522  43 HNGEIYNYGELREELADLGHAfrsrsdTEVLLAL-----YEEWGE----DCLERLRGMFAFAIWDRRRRTLFLARDRLGI 113

                          90
                  ....*....|....*.
gi 79328089   154 VPLYWGITaDGYVAFA 169
Cdd:pfam13522 114 KPLYYGIL-GGGFVFA 128
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 123-169 2.81e-10

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: 55.99  E-value: 2.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 79328089   123 HVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITADGYVAFA 169
Cdd:pfam13537  69 DCVDRLNGMFAFAIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFA 115
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 102-169 1.97e-09

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 56.77  E-value: 1.97e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79328089 102 EVLLviEAYKTLRDRApypanhvVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITaDGYVAFA 169
Cdd:COG0367 101 EVIL--HAYEEWGEDC-------LERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAED-GGGLAFA 158
asnB PRK09431
asparagine synthetase B; Provisional
 128-188 3.01e-08

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 53.37  E-value: 3.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328089  128 LSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITADGYVAFADD----VDLLK-------GCYYSTALGGLR 188
Cdd:PRK09431 118 LDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEmkalVPVCKtikefppGHYYWSKDGEFV 189
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 123-169 1.38e-07

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 51.18  E-value: 1.38e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 79328089   123 HVVAHLSGDFAFVVFDKSTSTLFVASDQVGKVPLYWGITaDGYVAFA 169
Cdd:TIGR01536 112 ECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFA 157
 
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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