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Conserved domains on  [gi|1002307734|ref|XP_015617262|]
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stem-specific protein TSJT1 [Oryza sativa Japonica Group]

Protein Classification

Wali7 domain-containing protein( domain architecture ID 10575738)

Wali7 domain-containing protein

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 ...
 2-226 1.77e-134

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: 377.48  E-value: 1.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734   2 LAVFSGAVVEVPAELVAAGSRTPSP--KTRASELVGRFLAAAEPAVSLQLGDLGHLAYSHANQSLLRPRSFASKDDIFCL 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSSTSSPalKKGFEELAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  80 FEGVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASFMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWG 159
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002307734 160 ITADGSVAFSNDIDLLKGSCGKSLAPFPQGCFYSNAlGGLKCYENPKNKVTAVPANEEE--ICGATFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSS-GGLRSFEHPMNKVKAVPRVDSEgvVCGATFKV 228
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-226 1.77e-134

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: 377.48  E-value: 1.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734   2 LAVFSGAVVEVPAELVAAGSRTPSP--KTRASELVGRFLAAAEPAVSLQLGDLGHLAYSHANQSLLRPRSFASKDDIFCL 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSSTSSPalKKGFEELAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  80 FEGVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASFMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWG 159
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002307734 160 ITADGSVAFSNDIDLLKGSCGKSLAPFPQGCFYSNAlGGLKCYENPKNKVTAVPANEEE--ICGATFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSS-GGLRSFEHPMNKVKAVPRVDSEgvVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-226 1.29e-132

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: 372.41  E-value: 1.29e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734   2 LAVFSGAVVEVPAELVAAGSRTPspKTRASELVGRFLAAAEPAVSLQLGDLGHLAYSHANQSLLRPRSFASKDDIFCLFE 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSRTP--AKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  82 GVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASFMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGIT 161
Cdd:cd01910    79 GHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002307734 162 ADGSVAFSNDIDLLKGSCGKSLAPFPQGCFYSNaLGGLKCYENPKNKVTAVPANEEE--ICGATFKV 226
Cdd:cd01910   159 ADGSVVFSDDVELVKASCGKSFAPFPKGCFFHS-EGGLRSFEHPMNKLKAVPRVDSEgeMCGATFKV 224
asnB PRK09431
asparagine synthetase B; Provisional
 124-219 3.88e-15

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 73.79  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFSNDIDLLKGSCgKSLAPFPQGCFYSNALGGLKCYE 203
Cdd:PRK09431  114 FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSKDGEFVRYY 192

                          90       100
                  ....*....|....*....|
gi 1002307734 204 NPK----NKVTAVPANEEEI 219
Cdd:PRK09431  193 QRDwfdyDAVKDNVTDKNEL 212
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 123-197 6.84e-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: 49.25  E-value: 6.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002307734 123 FMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITaDGSVAFSNDIDLLKGSCgkSLAPFPQGCFYSNALG 197
Cdd:TIGR01536 112 ECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASEIKALLAHP--NIKPFPDGAALAPGFG 183
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 124-187 2.44e-05

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: 44.83  E-value: 2.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITaDGSVAFSNDIdllkgscgKSLAPFP 187
Cdd:COG0367   114 CLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAED-GGGLAFASEL--------KALLAHP 168
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 2-226 1.77e-134

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: 377.48  E-value: 1.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734   2 LAVFSGAVVEVPAELVAAGSRTPSP--KTRASELVGRFLAAAEPAVSLQLGDLGHLAYSHANQSLLRPRSFASKDDIFCL 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSSTSSPalKKGFEELAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  80 FEGVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASFMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWG 159
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002307734 160 ITADGSVAFSNDIDLLKGSCGKSLAPFPQGCFYSNAlGGLKCYENPKNKVTAVPANEEE--ICGATFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSS-GGLRSFEHPMNKVKAVPRVDSEgvVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 2-226 1.29e-132

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: 372.41  E-value: 1.29e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734   2 LAVFSGAVVEVPAELVAAGSRTPspKTRASELVGRFLAAAEPAVSLQLGDLGHLAYSHANQSLLRPRSFASKDDIFCLFE 81
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSRTP--AKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  82 GVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASFMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGIT 161
Cdd:cd01910    79 GHLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002307734 162 ADGSVAFSNDIDLLKGSCGKSLAPFPQGCFYSNaLGGLKCYENPKNKVTAVPANEEE--ICGATFKV 226
Cdd:cd01910   159 ADGSVVFSDDVELVKASCGKSFAPFPKGCFFHS-EGGLRSFEHPMNKLKAVPRVDSEgeMCGATFKV 224
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 53-192 9.73e-19

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: 81.34  E-value: 9.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  53 GHLAYSHANQS--------LLRPRSFASkDDIFCLFEGVLDNLGRLSQQYGLSKGANEVLLVIEAYKTLRDRAPYPASF- 123
Cdd:cd00352    68 SGVALGHVRLAtnglpseaNAQPFRSED-GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGLf 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002307734 124 -----MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFSNDIDLLKGSCGKSLAPFPQGCFY 192
Cdd:cd00352   147 eavedALKRLDGPFAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
asnB PRK09431
asparagine synthetase B; Provisional
 124-219 3.88e-15

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 73.79  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFSNDIDLLKGSCgKSLAPFPQGCFYSNALGGLKCYE 203
Cdd:PRK09431  114 FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSKDGEFVRYY 192

                          90       100
                  ....*....|....*....|
gi 1002307734 204 NPK----NKVTAVPANEEEI 219
Cdd:PRK09431  193 QRDwfdyDAVKDNVTDKNEL 212
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 124-206 9.95e-14

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 69.79  E-value: 9.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFSNDIDLLKGSCgKSLAPFPQGCFYSNALGGLKCYE 203
Cdd:PLN02549  113 FVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDC-ERFEEFPPGHYYSSKAGGFRRWY 191


                  ...
gi 1002307734 204 NPK 206
Cdd:PLN02549  192 NPP 194
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 110-205 2.00e-12

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 65.89  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734 110 YKTLRDRAPYPASF-------MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFSNDIDLLKGSCGKs 182
Cdd:PTZ00077  100 FSSNSDCEIIGHLYkeygpkdFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE- 178

                          90       100
                  ....*....|....*....|....*
gi 1002307734 183 LAPFPQGCFYSNA--LGGLKCYENP 205
Cdd:PTZ00077  179 VKQFPPGHYYDQTkeKGEFVRYYNP 203
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 124-169 3.46e-08

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: 50.59  E-value: 3.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITADGSVAFS 169
Cdd:pfam13537  70 CVDRLNGMFAFAIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFA 115
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 124-188 1.45e-07

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: 50.25  E-value: 1.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITaDGSVAFSNDIdllkgscgKSLAPFPQ 188
Cdd:cd00712   113 CLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGLAFASEL--------KALLALPG 168
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 123-197 6.84e-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: 49.25  E-value: 6.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002307734 123 FMLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITaDGSVAFSNDIDLLKGSCgkSLAPFPQGCFYSNALG 197
Cdd:TIGR01536 112 ECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASEIKALLAHP--NIKPFPDGAALAPGFG 183
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 124-187 2.44e-05

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: 44.83  E-value: 2.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002307734 124 MLSQLTGSYAFVLFDKSTSSLLVASDPEGKVPLFWGITaDGSVAFSNDIdllkgscgKSLAPFP 187
Cdd:COG0367   114 CLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAED-GGGLAFASEL--------KALLAHP 168
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 80-169 9.13e-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: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 41.14  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002307734  80 FEGVLDNLGRLSQQYGLsKGAN-------EVLLVieAYKTLRDRApypasfmLSQLTGSYAFVLFDKSTSSLLVASDPEG 152
Cdd:pfam13522  43 HNGEIYNYGELREELAD-LGHAfrsrsdtEVLLA--LYEEWGEDC-------LERLRGMFAFAIWDRRRRTLFLARDRLG 112

                          90
                  ....*....|....*..
gi 1002307734 153 KVPLFWGITaDGSVAFS 169
Cdd:pfam13522 113 IKPLYYGIL-GGGFVFA 128
 
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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