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Conserved domains on  [gi|1494874620|ref|WP_121616448|]
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asparaginase [Virgibacillus halodenitrificans]

Protein Classification

asparaginase( domain architecture ID 10008560)

asparaginase catalyzes the hydrolysis of L-asparagine to form L-aspartic acid and ammonia

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AnsA2 COG4448
L-asparaginase II [Amino acid transport and metabolism];
1-333 2.39e-169

L-asparaginase II [Amino acid transport and metabolism];


:

Pssm-ID: 443547  Cd Length: 336  Bit Score: 474.28  E-value: 2.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620   1 MERNNV--VNVKRGTSIESSHQVHLAVVDSNGDLLHYVGEPNGKVYARSSMKPIQAIPIVETGAADYYQFSDADLSLCTA 78
Cdd:COG4448     1 MTMAAVvlVEVTRGGLVESRHRGSAVVVDADGRVVASLGDPDAPVFPRSSAKPLQALPLLESGAADAFGLTDEELALACA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620  79 SHNGEAMHTERVLSILKRIGIEDTTLQCGTHIPRWQDTYKNLILNNKEVTPLYNNCSGKHTGMLATAKFMGESLEDYYAK 158
Cdd:COG4448    81 SHSGEPEHVEAVRSMLAKAGLDEDALRCGPHWPLDEAARDALIRAGEGPTRLHNNCSGKHAGMLATCVHLGWPTDGYLDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 159 DHPVQQRIVQAVSEVCDYPqEEIEIGIDGCGVPVHGLPLERLAYGFARMATHEILGEKRSSAVSRITNAMMEAPEMVGGT 238
Cdd:COG4448   161 DHPLQQAIRETVEELTGEP-VADATGVDGCGAPVFALPLTGLARAFARLATAEGGSPARATAARRVADAMRAHPELVAGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 239 NRFCSDFMKAGQGRFFGKAGAEGVYCIGDTKTGLGIAAKVADGNGRAVYPAVMEAITQLGLLTNDQIEQLKEYHHPKLRN 318
Cdd:COG4448   240 GRFDTDLMRAVPGRLVAKTGAEGVYAAALPPDGLGVALKIDDGATRAAEPVVAALLRRLGVLDAEEPAALAALARPPVLN 319
                         330
                  ....*....|....*
gi 1494874620 319 ARDEIIGELVPVFQL 333
Cdd:COG4448   320 GGGEVVGEIRPAFAL 334
 
Name Accession Description Interval E-value
AnsA2 COG4448
L-asparaginase II [Amino acid transport and metabolism];
1-333 2.39e-169

L-asparaginase II [Amino acid transport and metabolism];


Pssm-ID: 443547  Cd Length: 336  Bit Score: 474.28  E-value: 2.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620   1 MERNNV--VNVKRGTSIESSHQVHLAVVDSNGDLLHYVGEPNGKVYARSSMKPIQAIPIVETGAADYYQFSDADLSLCTA 78
Cdd:COG4448     1 MTMAAVvlVEVTRGGLVESRHRGSAVVVDADGRVVASLGDPDAPVFPRSSAKPLQALPLLESGAADAFGLTDEELALACA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620  79 SHNGEAMHTERVLSILKRIGIEDTTLQCGTHIPRWQDTYKNLILNNKEVTPLYNNCSGKHTGMLATAKFMGESLEDYYAK 158
Cdd:COG4448    81 SHSGEPEHVEAVRSMLAKAGLDEDALRCGPHWPLDEAARDALIRAGEGPTRLHNNCSGKHAGMLATCVHLGWPTDGYLDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 159 DHPVQQRIVQAVSEVCDYPqEEIEIGIDGCGVPVHGLPLERLAYGFARMATHEILGEKRSSAVSRITNAMMEAPEMVGGT 238
Cdd:COG4448   161 DHPLQQAIRETVEELTGEP-VADATGVDGCGAPVFALPLTGLARAFARLATAEGGSPARATAARRVADAMRAHPELVAGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 239 NRFCSDFMKAGQGRFFGKAGAEGVYCIGDTKTGLGIAAKVADGNGRAVYPAVMEAITQLGLLTNDQIEQLKEYHHPKLRN 318
Cdd:COG4448   240 GRFDTDLMRAVPGRLVAKTGAEGVYAAALPPDGLGVALKIDDGATRAAEPVVAALLRRLGVLDAEEPAALAALARPPVLN 319
                         330
                  ....*....|....*
gi 1494874620 319 ARDEIIGELVPVFQL 333
Cdd:COG4448   320 GGGEVVGEIRPAFAL 334
Asparaginase_II pfam06089
L-asparaginase II; This family consists of several bacterial L-asparaginase II proteins. ...
9-329 3.73e-158

L-asparaginase II; This family consists of several bacterial L-asparaginase II proteins. L-asparaginase (EC:3.5.1.1) catalyzes the hydrolysis of L-asparagine to L-aspartate and ammonium. Rhizobium etli possesses two asparaginases: asparaginase I, which is thermostable and constitutive, and asparaginase II, which is thermolabile, induced by asparagine and repressed by the carbon source.


Pssm-ID: 461825  Cd Length: 320  Bit Score: 445.39  E-value: 3.73e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620   9 VKRGTSIESSHQVHLAVVDSNGDLLHYVGEPNGKVYARSSMKPIQAIPIVETGAADYYQFSDADLSLCTASHNGEAMHTE 88
Cdd:pfam06089   1 VVRGGLVESVHRGHAVVVDADGRVLASAGDPDRPTFPRSAAKPFQALALLESGAAERFGLDDEELALACASHSGEPFHVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620  89 RVLSILKRIGIEDTTLQCGTHIPRWQDTYKNLILNNKEVTPLYNNCSGKHTGMLATAKFMGESLEDYYAKDHPVQQRIVQ 168
Cdd:pfam06089  81 RVRSILAKAGLDESALRCGPHLPLDEAARRALIRAGGKPSPLHNNCSGKHAGMLAACVALGWPLDGYLDPDHPLQQLIRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 169 AVSEVCDYPQEEIEIGIDGCGVPVHGLPLERLAYGFARMATHEILGEkRSSAVSRITNAMMEAPEMVGGTNRFCSDFMKA 248
Cdd:pfam06089 161 TVEELTGEPPDEIIVGVDGCGAPTFALPLTGLARAYARLAAAGDGLE-RAEALERIARAMTAHPELVAGTGRFDTELMRA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 249 GQGRFFGKAGAEGVYCIGDTKTGLGIAAKVADGNGRAVYPAVMEAITQLGLLTNDQIEQLKEYHHPKLRNARDEIIGELV 328
Cdd:pfam06089 240 TPGRLVAKGGAEGVYCVGLPDGGLGIAVKIEDGSTRARYAVAAALLRQLGVLTPEEAEALAEFARPPVLNGRGEVVGEVR 319

                  .
gi 1494874620 329 P 329
Cdd:pfam06089 320 P 320
 
Name Accession Description Interval E-value
AnsA2 COG4448
L-asparaginase II [Amino acid transport and metabolism];
1-333 2.39e-169

L-asparaginase II [Amino acid transport and metabolism];


Pssm-ID: 443547  Cd Length: 336  Bit Score: 474.28  E-value: 2.39e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620   1 MERNNV--VNVKRGTSIESSHQVHLAVVDSNGDLLHYVGEPNGKVYARSSMKPIQAIPIVETGAADYYQFSDADLSLCTA 78
Cdd:COG4448     1 MTMAAVvlVEVTRGGLVESRHRGSAVVVDADGRVVASLGDPDAPVFPRSSAKPLQALPLLESGAADAFGLTDEELALACA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620  79 SHNGEAMHTERVLSILKRIGIEDTTLQCGTHIPRWQDTYKNLILNNKEVTPLYNNCSGKHTGMLATAKFMGESLEDYYAK 158
Cdd:COG4448    81 SHSGEPEHVEAVRSMLAKAGLDEDALRCGPHWPLDEAARDALIRAGEGPTRLHNNCSGKHAGMLATCVHLGWPTDGYLDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 159 DHPVQQRIVQAVSEVCDYPqEEIEIGIDGCGVPVHGLPLERLAYGFARMATHEILGEKRSSAVSRITNAMMEAPEMVGGT 238
Cdd:COG4448   161 DHPLQQAIRETVEELTGEP-VADATGVDGCGAPVFALPLTGLARAFARLATAEGGSPARATAARRVADAMRAHPELVAGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 239 NRFCSDFMKAGQGRFFGKAGAEGVYCIGDTKTGLGIAAKVADGNGRAVYPAVMEAITQLGLLTNDQIEQLKEYHHPKLRN 318
Cdd:COG4448   240 GRFDTDLMRAVPGRLVAKTGAEGVYAAALPPDGLGVALKIDDGATRAAEPVVAALLRRLGVLDAEEPAALAALARPPVLN 319
                         330
                  ....*....|....*
gi 1494874620 319 ARDEIIGELVPVFQL 333
Cdd:COG4448   320 GGGEVVGEIRPAFAL 334
Asparaginase_II pfam06089
L-asparaginase II; This family consists of several bacterial L-asparaginase II proteins. ...
9-329 3.73e-158

L-asparaginase II; This family consists of several bacterial L-asparaginase II proteins. L-asparaginase (EC:3.5.1.1) catalyzes the hydrolysis of L-asparagine to L-aspartate and ammonium. Rhizobium etli possesses two asparaginases: asparaginase I, which is thermostable and constitutive, and asparaginase II, which is thermolabile, induced by asparagine and repressed by the carbon source.


Pssm-ID: 461825  Cd Length: 320  Bit Score: 445.39  E-value: 3.73e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620   9 VKRGTSIESSHQVHLAVVDSNGDLLHYVGEPNGKVYARSSMKPIQAIPIVETGAADYYQFSDADLSLCTASHNGEAMHTE 88
Cdd:pfam06089   1 VVRGGLVESVHRGHAVVVDADGRVLASAGDPDRPTFPRSAAKPFQALALLESGAAERFGLDDEELALACASHSGEPFHVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620  89 RVLSILKRIGIEDTTLQCGTHIPRWQDTYKNLILNNKEVTPLYNNCSGKHTGMLATAKFMGESLEDYYAKDHPVQQRIVQ 168
Cdd:pfam06089  81 RVRSILAKAGLDESALRCGPHLPLDEAARRALIRAGGKPSPLHNNCSGKHAGMLAACVALGWPLDGYLDPDHPLQQLIRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 169 AVSEVCDYPQEEIEIGIDGCGVPVHGLPLERLAYGFARMATHEILGEkRSSAVSRITNAMMEAPEMVGGTNRFCSDFMKA 248
Cdd:pfam06089 161 TVEELTGEPPDEIIVGVDGCGAPTFALPLTGLARAYARLAAAGDGLE-RAEALERIARAMTAHPELVAGTGRFDTELMRA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494874620 249 GQGRFFGKAGAEGVYCIGDTKTGLGIAAKVADGNGRAVYPAVMEAITQLGLLTNDQIEQLKEYHHPKLRNARDEIIGELV 328
Cdd:pfam06089 240 TPGRLVAKGGAEGVYCVGLPDGGLGIAVKIEDGSTRARYAVAAALLRQLGVLTPEEAEALAEFARPPVLNGRGEVVGEVR 319

                  .
gi 1494874620 329 P 329
Cdd:pfam06089 320 P 320
 
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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