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Conserved domains on  [gi|1901086394|emb|CAD5323870|]
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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

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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 1.59e-156

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: 433.72  E-value: 1.59e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394   2 LAIFDKNVAKTPEALQGQEG-GSVCALKDRF--LPNHFSSVYPGAVTINLGSSGFIACSLEKQNPLLPRLFAVVDDMFCI 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFeeLAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  79 FQGHIENVPILKQQYGLTKTATEVTIVIEAYRTLRDRGPYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWG 158
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086394 159 TDAEGHLVVSDDVETVKKGCGKSFAPFPKGCFFTSSGGLRSYEHPSNELKPVPRVDSSGEVCGVTFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 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 1.59e-156

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: 433.72  E-value: 1.59e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394   2 LAIFDKNVAKTPEALQGQEG-GSVCALKDRF--LPNHFSSVYPGAVTINLGSSGFIACSLEKQNPLLPRLFAVVDDMFCI 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFeeLAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  79 FQGHIENVPILKQQYGLTKTATEVTIVIEAYRTLRDRGPYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWG 158
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086394 159 TDAEGHLVVSDDVETVKKGCGKSFAPFPKGCFFTSSGGLRSYEHPSNELKPVPRVDSSGEVCGVTFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-226 4.11e-147

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: 409.78  E-value: 4.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394   2 LAIFDKNVAKTPEALQgQEGGSVCALKDRFLPNHFSSVYPGAVTINLGSSGFIACSLEKQNPLLPRLFAVVDDMFCIFQG 81
Cdd:cd01910     1 LAVFSKAVAKPPEELV-SAGSRTPAKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  82 HIENVPILKQQYGLTKTATEVTIVIEAYRTLRDRGPYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDA 161
Cdd:cd01910    80 HLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901086394 162 EGHLVVSDDVETVKKGCGKSFAPFPKGCFFTSSGGLRSYEHPSNELKPVPRVDSSGEVCGVTFKV 226
Cdd:cd01910   160 DGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
asnB PRK09431
asparagine synthetase B; Provisional
78-203 5.16e-12

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 64.93  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  78 IFQGHIENVPILKQQYG-----LTKTATEVtiVIEAYRTLrdrGPysaeQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGS 152
Cdd:PRK09431   73 AVNGEIYNHQELRAELGdkyafQTGSDCEV--ILALYQEK---GP----DFLDDLDGMFAFALYDSEKDAYLIARDPIGI 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1901086394 153 VPLYWGTDAEGHLVVSDDVETVKKGCgKSFAPFPKGCFFTS-SGGLRSYEHP 203
Cdd:PRK09431  144 IPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSkDGEFVRYYQR 194
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
96-163 8.77e-03

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: 37.12  E-value: 8.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086394  96 TKTATEVtiVIEAYRtlrDRGpysaEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDAEG 163
Cdd:COG0367    96 THSDTEV--ILHAYE---EWG----EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGG 154
 
Name Accession Description Interval E-value
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
2-226 1.59e-156

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: 433.72  E-value: 1.59e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394   2 LAIFDKNVAKTPEALQGQEG-GSVCALKDRF--LPNHFSSVYPGAVTINLGSSGFIACSLEKQNPLLPRLFAVVDDMFCI 78
Cdd:pfam12481   1 LAVFDKAVAKPPEELNSPGSsTSSPALKKGFeeLAEHFLSAHPNAVSVNLGDSGFLAYSHHKQNPLLPRLFAVVDDIFCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  79 FQGHIENVPILKQQYGLTKTATEVTIVIEAYRTLRDRGPYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWG 158
Cdd:pfam12481  81 FQGHLENLASLKQQYGLSKGANEAMIVIEAYRTLRDRGPYPADQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086394 159 TDAEGHLVVSDDVETVKKGCGKSFAPFPKGCFFTSSGGLRSYEHPSNELKPVPRVDSSGEVCGVTFKV 226
Cdd:pfam12481 161 IDADGSLVFSDDIEIVKKGCGKSFAPFPKGCFFTSSGGLRSFEHPMNKVKAVPRVDSEGVVCGATFKV 228
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
2-226 4.11e-147

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: 409.78  E-value: 4.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394   2 LAIFDKNVAKTPEALQgQEGGSVCALKDRFLPNHFSSVYPGAVTINLGSSGFIACSLEKQNPLLPRLFAVVDDMFCIFQG 81
Cdd:cd01910     1 LAVFSKAVAKPPEELV-SAGSRTPAKTAEELLKRFLSANPSAVFVHLGAAGFLAYSHHNQSPLHPRLFAVKDDIFCLFQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  82 HIENVPILKQQYGLTKTATEVTIVIEAYRTLRDRGPYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDA 161
Cdd:cd01910    80 HLDNLGSLKQQYGLSKTANEAMLVIEAYRTLRDRGPYPADQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901086394 162 EGHLVVSDDVETVKKGCGKSFAPFPKGCFFTSSGGLRSYEHPSNELKPVPRVDSSGEVCGVTFKV 226
Cdd:cd01910   160 DGSVVFSDDVELVKASCGKSFAPFPKGCFFHSEGGLRSFEHPMNKLKAVPRVDSEGEMCGATFKV 224
asnB PRK09431
asparagine synthetase B; Provisional
78-203 5.16e-12

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 64.93  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  78 IFQGHIENVPILKQQYG-----LTKTATEVtiVIEAYRTLrdrGPysaeQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGS 152
Cdd:PRK09431   73 AVNGEIYNHQELRAELGdkyafQTGSDCEV--ILALYQEK---GP----DFLDDLDGMFAFALYDSEKDAYLIARDPIGI 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1901086394 153 VPLYWGTDAEGHLVVSDDVETVKKGCgKSFAPFPKGCFFTS-SGGLRSYEHP 203
Cdd:PRK09431  144 IPLYYGYDEHGNLYFASEMKALVPVC-KTIKEFPPGHYYWSkDGEFVRYYQR 194
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
81-216 2.65e-09

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 57.08  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  81 GHIENVPILKQQYGLTKTAT----EVtiVIEAYRtlrdrgpYSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLY 156
Cdd:PLN02549   76 GEIYNHKELREKLKLHKFRTgsdcEV--IAHLYE-------EHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLY 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1901086394 157 --WGTDaeGHLVVSDDVETVKKGCgKSFAPFPKGCFFTS-SGGLRSYEHPS--NELKPVPRVDSS 216
Cdd:PLN02549  147 igWGLD--GSVWFASEMKALCDDC-ERFEEFPPGHYYSSkAGGFRRWYNPPwfSESIPSTPYDPL 208
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
118-211 2.67e-06

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 47.79  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394 118 YSAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDAEGHLVVSDDVETVKKGCGKsFAPFPKGCFF---TSS 194
Cdd:PTZ00077  116 YGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVE-VKQFPPGHYYdqtKEK 194
                          90
                  ....*....|....*....
gi 1901086394 195 GGLRSYEHPS--NELKPVP 211
Cdd:PTZ00077  195 GEFVRYYNPNwhDFDHPIP 213
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
78-168 1.52e-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: 43.45  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901086394  78 IFQGHIENVPILKQQYGL------TKTATEVtiVIEAYRTLrdrgpysAEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDG 151
Cdd:pfam13522  42 VHNGEIYNYGELREELADlghafrSRSDTEV--LLALYEEW-------GEDCLERLRGMFAFAIWDRRRRTLFLARDRLG 112
                          90
                  ....*....|....*..
gi 1901086394 152 SVPLYWGTDaEGHLVVS 168
Cdd:pfam13522 113 IKPLYYGIL-GGGFVFA 128
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
96-168 7.43e-04

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: 38.27  E-value: 7.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901086394  96 TKTATEVtiVIEAYRtlRDRGpysaEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDAEGHLVVS 168
Cdd:pfam13537  51 THSDTEV--ILHLYE--AEWG----EDCVDRLNGMFAFAIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFA 115
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
100-163 1.06e-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: 39.08  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901086394 100 TEVtiVIEAYRtlrDRGpysaEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDAEG 163
Cdd:cd00712    99 TEV--ILHLYE---EWG----EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDGGG 153
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
96-163 8.77e-03

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: 37.12  E-value: 8.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901086394  96 TKTATEVtiVIEAYRtlrDRGpysaEQVVRDFQGKFGFMLYDCSTQNVFLAGDVDGSVPLYWGTDAEG 163
Cdd:COG0367    96 THSDTEV--ILHAYE---EWG----EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGG 154
 
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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