NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1789582616|emb|CAA0382529|]
View 

unnamed protein product [Arabidopsis thaliana]

Protein Classification

DUF3700 domain-containing protein( domain architecture ID 10575738)

DUF3700 domain-containing protein may belong to the family of class II glutamine amidotransferase, which hydrolyzes ammonia from glutamine and transfers the amino group to the appropriate substrate; similar to Elaeis guineensis stem-specific protein TSJT1-like

CATH:  3.60.20.10
PubMed:  8430515|9559052
SCOP:  3000131

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 ...
2-229 3.71e-148

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: 412.53  E-value: 3.71e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616   2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMFHSETGLKSFDHPTNMMKAMPRIDSEGVLCGASFKV 229
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 ...
2-229 3.71e-148

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: 412.53  E-value: 3.71e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616   2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMFHSETGLKSFDHPTNMMKAMPRIDSEGVLCGASFKV 229
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-229 1.21e-127

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: 360.47  E-value: 1.21e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616   2 LAIFQKAFAHPPEELNSPASHfsgKTPKLPGETLSDFLSHHQNNAFSMnFGDSAVLAY-ARQETSLRQRLFCGLDGIYCM 80
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSR---TPAKTAEELLKRFLSANPSAVFVH-LGAAGFLAYsHHNQSPLHPRLFAVKDDIFCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  81 FLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLYW 160
Cdd:cd01910    77 FQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789582616 161 GISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMFHSETGLKSFDHPTNMMKAMPRIDSEGVLCGASFKV 229
Cdd:cd01910   156 GIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
130-199 1.97e-07

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 51.30  E-value: 1.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNGCMFHSETG 199
Cdd:PLN02549  117 LDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDCER-FEEFPPGHYYSSKAG 185
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
2-229 3.71e-148

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: 412.53  E-value: 3.71e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616   2 LAIFQKAFAHPPEELNSPAS-HFSGKTPKLPGETLSDFLSHHQNnAFSMNFGDSAVLAYARQETS-LRQRLFCGLDGIYC 79
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFEELAEHFLSAHPN-AVSVNLGDSGFLAYSHHKQNpLLPRLFAVVDDIFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  80 MFLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLY 159
Cdd:pfam12481  80 LFQGHLENLASLKQQYGLS-KGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLY 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 160 WGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMFHSETGLKSFDHPTNMMKAMPRIDSEGVLCGASFKV 229
Cdd:pfam12481 159 WGIDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-229 1.21e-127

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: 360.47  E-value: 1.21e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616   2 LAIFQKAFAHPPEELNSPASHfsgKTPKLPGETLSDFLSHHQNNAFSMnFGDSAVLAY-ARQETSLRQRLFCGLDGIYCM 80
Cdd:cd01910     1 LAVFSKAVAKPPEELVSAGSR---TPAKTAEELLKRFLSANPSAVFVH-LGAAGFLAYsHHNQSPLHPRLFAVKDDIFCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  81 FLGRLNNLCTLNRQYGLSgKNSNEAMFVIEAYRTLRDRGPYPADQVLRGLEGSFAFVVYDTQTSSVFSALSSDGGESLYW 160
Cdd:cd01910    77 FQGHLDNLGSLKQQYGLS-KTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYW 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789582616 161 GISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMFHSETGLKSFDHPTNMMKAMPRIDSEGVLCGASFKV 229
Cdd:cd01910   156 GIAADGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
70-194 3.44e-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: 77.49  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616  70 LFCGLDGIYCMFLGRLNNLCTLNRQYGLSGKNsNEAMFVIEAYRTLRDRGPY------PADQVLRGLEGSFAFVVYDTQT 143
Cdd:cd00352    91 FRSEDGRIALVHNGEIYNYRELREELEARGYR-FEGESDSEVILHLLERLGRegglfeAVEDALKRLDGPFAFALWDGKP 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1789582616 144 SSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKSFAPFPNGCMF 194
Cdd:cd00352   170 DRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
130-199 1.97e-07

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 51.30  E-value: 1.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNGCMFHSETG 199
Cdd:PLN02549  117 LDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALCDDCER-FEEFPPGHYYSSKAG 185
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
130-198 2.68e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 47.79  E-value: 2.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789582616 130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCAKsFAPFPNGcMFHSET 198
Cdd:PTZ00077  125 LDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPG-HYYDQT 191
asnB PRK09431
asparagine synthetase B; Provisional
130-199 4.52e-06

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 47.21  E-value: 4.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789582616 130 LEGSFAFVVYDTQTSSVFSALSSDGGESLYWGISGDGSVVMSDDIQIIKQGCaKSFAPFPNGCMFHSETG 199
Cdd:PRK09431  118 LDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSKDG 186
 
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