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Conserved domains on  [gi|695765324|ref|WP_032688358|]
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MULTISPECIES: asparaginase [Raoultella]

Protein Classification

asparaginase( domain architecture ID 10793270)

asparaginase catalyzes the formation of aspartate from asparagine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
1-335 0e+00

cytoplasmic asparaginase I; Provisional


:

Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 769.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   1 MQKKSIYVAYTGGTIGMQRSEHGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:PRK09461   1 MQKKSIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLIDSSDMTPEDWQHIADDIKANYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  81 EYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNR 160
Cdd:PRK09461  81 DYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 161 TTKAHADGFDAFASPNLAPLLEAGIHIRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILR 240
Cdd:PRK09461 161 TTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 241 SYGVGNAPQNGEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVD 320
Cdd:PRK09461 241 SYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQELSTE 320
                        330
                 ....*....|....*
gi 695765324 321 EIRNLMQENLRGELT 335
Cdd:PRK09461 321 EIRQAMQQNLRGELT 335
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
1-335 0e+00

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 769.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   1 MQKKSIYVAYTGGTIGMQRSEHGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:PRK09461   1 MQKKSIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLIDSSDMTPEDWQHIADDIKANYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  81 EYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNR 160
Cdd:PRK09461  81 DYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 161 TTKAHADGFDAFASPNLAPLLEAGIHIRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILR 240
Cdd:PRK09461 161 TTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 241 SYGVGNAPQNGEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVD 320
Cdd:PRK09461 241 SYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQELSTE 320
                        330
                 ....*....|....*
gi 695765324 321 EIRNLMQENLRGELT 335
Cdd:PRK09461 321 EIRQAMQQNLRGELT 335
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
3-336 2.18e-172

L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.


Pssm-ID: 129610 [Multi-domain]  Cd Length: 336  Bit Score: 482.01  E-value: 2.18e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    3 KKSIYVAYTGGTIGMQRSEH--GYIPVsGHLQRQLALMPEFHRPEMPDFtihEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:TIGR00519   1 LKDISIISTGGTIASKVDYRtgAVHPV-FTADELLSAVPELLDIANIDG---EALMNILSENMKPEYWVEIAEAVKKEYD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   81 EYDGFVILHGTDTMAFTASALSFMLEHlGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP------INEVTLFFNNR 154
Cdd:TIGR00519  77 DYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYIaevtvcMHGVTLDFNCR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  155 LYRGNRTTKAHADGFDAFASPNLAPLLEAGIH-IRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQP 233
Cdd:TIGR00519 156 LHRGVKVRKAHTSRRDAFASINAPPLAEINPDgIEYLNEVYRPRGEDELEVHDRLEEKVALIKIYPGISPDIIRNYLSKG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  234 VKALILRSYGVGNAPQNGefIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLL 313
Cdd:TIGR00519 236 YKGIVIEGTGLGHAPQNK--LQELQEASDRGVVVVMTTQCLNGRVNMNVYSTGRRLLQAGVIGGEDMLPEVALVKLMWLL 313
                         330       340
                  ....*....|....*....|...
gi 695765324  314 SQNLSVDEIRNLMQENLRGELTP 336
Cdd:TIGR00519 314 GQYSDPEEAKKMMSKNIAGEIEP 336
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
1-328 1.38e-140

L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];


Pssm-ID: 440022 [Multi-domain]  Cd Length: 325  Bit Score: 401.05  E-value: 1.38e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   1 MQKKSIYVAYTGGTIGMQRSEHGYIPV-SGHLQRQLALMPEFHRPEmpDFTIHEYEPLmDSSDMTPEDWQHIADDIRAHY 79
Cdd:COG0252    1 MMMPKILVLATGGTIAMRADPAGYAVApALSAEELLAAVPELAELA--DIEVEQFANI-DSSNMTPADWLALARRIEEAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  80 -DEYDGFVILHGTDTMAFTASALSFMLEhLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP--INEVTLFFNNRLY 156
Cdd:COG0252   78 aDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAASPEarGRGVLVVFNDEIH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 157 RGNRTTKAHADGFDAFASPNLAPLLEAGI-HIRRLGTPPAPHGiGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVK 235
Cdd:COG0252  157 RARRVTKTHTSRVDAFQSPNYGPLGEVDEgRVRFYRRPPRRPE-SELDLAPALLPRVAILKLYPGMDPALLDALLAAGVK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 236 ALILRSYGVGNAPQngEFIQVLAEASQRGIVVINLTQCMSGKVNmGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQ 315
Cdd:COG0252  236 GIVLEGTGAGNVPP--ALLPALKRAIERGVPVVVTSRCPEGRVN-GVYGGGRDLAEAGVISGGDLTPEKARIKLMLALGQ 312
                        330
                 ....*....|...
gi 695765324 316 NLSVDEIRNLMQE 328
Cdd:COG0252  313 GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
6-323 2.14e-138

Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.


Pssm-ID: 214873 [Multi-domain]  Cd Length: 323  Bit Score: 395.35  E-value: 2.14e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324     6 IYVAYTGGTIGMQRS-EHGYIPVSGHLQRQLALMPEFhrPEMPDFTIHEYEPLMDSSDMTPEDWQHIADDIRA--HYDEY 82
Cdd:smart00870   1 ILVLYTGGTIAMKADpSTGAVGPTAGAEELLALLPAL--PELADDIEVEQVANIDSSNMTPEDWLKLAKRINEalADDGY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    83 DGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP--INEVTLFFNNRLYRGNR 160
Cdd:smart00870  79 DGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPEarGRGVLVVFNDEIHRARR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   161 TTKAHADGFDAFASPNLAPL---LEAGIHIRRLGTPPAPHGIGELIVHPITPQP-IGVVTIYPGISADVVRNFLRQPVKA 236
Cdd:smart00870 159 VTKTHTSRVDAFQSPNFGPLgyvDEGGVVYYTRPTRRHTKRSPFLLDLKDALLPkVAIVKAYPGMDAELLDALLDSGAKG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   237 LILRSYGVGNAPQNgeFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQN 316
Cdd:smart00870 239 LVLEGTGAGNVPPD--LLEALKEALERGIPVVRTSRCLSGRVDPGYYATGRDLAKAGVISAGDLTPEKARIKLMLALGKG 316

                   ....*..
gi 695765324   317 LSVDEIR 323
Cdd:smart00870 317 LDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
4-323 3.22e-136

Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.


Pssm-ID: 199207 [Multi-domain]  Cd Length: 316  Bit Score: 389.63  E-value: 3.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   4 KSIYVAYTGGTIGMQRSEHGYIPVSGHLQRQLALMPEFHrpemPDFTIHEYEPLMDSSDMTPEDWQHIADDIRAHYDEYD 83
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLPELLE----DCFIEVEQLPNIDSSNMTPEDWLRIARAIAENYDGYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  84 GFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTK 163
Cdd:cd08963   77 GFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSIRGVYVAFNGKLIRGTRARK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 164 AHADGFDAFASPNLAPLLEAGIHIRRLGTPPAPHGIGELIVHPITPQpIGVVTIYPGISADVVRNFLRQPVKALILRSYG 243
Cdd:cd08963  157 VRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFYPDLDPN-VFLLKLIPGLLPAILDALLEKYPRGLILEGFG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 244 VGNAPQNGEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIR 323
Cdd:cd08963  236 AGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSVYAVGQALLEAGVIPGGDMTTEAAVAKLMWLLGQTDDAEEVR 315
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
6-188 1.64e-81

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 245.53  E-value: 1.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    6 IYVAYTGGTIGMQRSEHG-----YIPVSGHLQRQLALMpefhrpEMPDFTIhEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:pfam00710   1 VLILATGGTIASRADSSGgavvpALTGEELLAAVPELA------DIAEIEA-EQVANIDSSNMTPADWLRLARRIAEALD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   81 EYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANY--PINEVTLFFNNRLYRG 158
Cdd:pfam00710  74 DYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPaaRGPGVLVVFNDKLHRA 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 695765324  159 NRTTKAHADGFDAFASPNLAPLLE-AGIHIR 188
Cdd:pfam00710 154 RRVTKTHTSSLDAFDSPNFGPLGEvDGGQVE 184
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
1-335 0e+00

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 769.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   1 MQKKSIYVAYTGGTIGMQRSEHGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:PRK09461   1 MQKKSIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLIDSSDMTPEDWQHIADDIKANYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  81 EYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNR 160
Cdd:PRK09461  81 DYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEVTLFFNNKLFRGNR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 161 TTKAHADGFDAFASPNLAPLLEAGIHIRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILR 240
Cdd:PRK09461 161 TTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISAEVVRNFLRQPVKALILR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 241 SYGVGNAPQNGEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVD 320
Cdd:PRK09461 241 SYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGGYATGNALAHAGVISGADMTVEAALTKLHYLLSQELSTE 320
                        330
                 ....*....|....*
gi 695765324 321 EIRNLMQENLRGELT 335
Cdd:PRK09461 321 EIRQAMQQNLRGELT 335
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
3-336 2.18e-172

L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.


Pssm-ID: 129610 [Multi-domain]  Cd Length: 336  Bit Score: 482.01  E-value: 2.18e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    3 KKSIYVAYTGGTIGMQRSEH--GYIPVsGHLQRQLALMPEFHRPEMPDFtihEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:TIGR00519   1 LKDISIISTGGTIASKVDYRtgAVHPV-FTADELLSAVPELLDIANIDG---EALMNILSENMKPEYWVEIAEAVKKEYD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   81 EYDGFVILHGTDTMAFTASALSFMLEHlGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP------INEVTLFFNNR 154
Cdd:TIGR00519  77 DYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYIaevtvcMHGVTLDFNCR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  155 LYRGNRTTKAHADGFDAFASPNLAPLLEAGIH-IRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQP 233
Cdd:TIGR00519 156 LHRGVKVRKAHTSRRDAFASINAPPLAEINPDgIEYLNEVYRPRGEDELEVHDRLEEKVALIKIYPGISPDIIRNYLSKG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  234 VKALILRSYGVGNAPQNGefIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLL 313
Cdd:TIGR00519 236 YKGIVIEGTGLGHAPQNK--LQELQEASDRGVVVVMTTQCLNGRVNMNVYSTGRRLLQAGVIGGEDMLPEVALVKLMWLL 313
                         330       340
                  ....*....|....*....|...
gi 695765324  314 SQNLSVDEIRNLMQENLRGELTP 336
Cdd:TIGR00519 314 GQYSDPEEAKKMMSKNIAGEIEP 336
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
1-328 1.38e-140

L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];


Pssm-ID: 440022 [Multi-domain]  Cd Length: 325  Bit Score: 401.05  E-value: 1.38e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   1 MQKKSIYVAYTGGTIGMQRSEHGYIPV-SGHLQRQLALMPEFHRPEmpDFTIHEYEPLmDSSDMTPEDWQHIADDIRAHY 79
Cdd:COG0252    1 MMMPKILVLATGGTIAMRADPAGYAVApALSAEELLAAVPELAELA--DIEVEQFANI-DSSNMTPADWLALARRIEEAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  80 -DEYDGFVILHGTDTMAFTASALSFMLEhLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP--INEVTLFFNNRLY 156
Cdd:COG0252   78 aDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAASPEarGRGVLVVFNDEIH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 157 RGNRTTKAHADGFDAFASPNLAPLLEAGI-HIRRLGTPPAPHGiGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVK 235
Cdd:COG0252  157 RARRVTKTHTSRVDAFQSPNYGPLGEVDEgRVRFYRRPPRRPE-SELDLAPALLPRVAILKLYPGMDPALLDALLAAGVK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 236 ALILRSYGVGNAPQngEFIQVLAEASQRGIVVINLTQCMSGKVNmGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQ 315
Cdd:COG0252  236 GIVLEGTGAGNVPP--ALLPALKRAIERGVPVVVTSRCPEGRVN-GVYGGGRDLAEAGVISGGDLTPEKARIKLMLALGQ 312
                        330
                 ....*....|...
gi 695765324 316 NLSVDEIRNLMQE 328
Cdd:COG0252  313 GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
6-323 2.14e-138

Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.


Pssm-ID: 214873 [Multi-domain]  Cd Length: 323  Bit Score: 395.35  E-value: 2.14e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324     6 IYVAYTGGTIGMQRS-EHGYIPVSGHLQRQLALMPEFhrPEMPDFTIHEYEPLMDSSDMTPEDWQHIADDIRA--HYDEY 82
Cdd:smart00870   1 ILVLYTGGTIAMKADpSTGAVGPTAGAEELLALLPAL--PELADDIEVEQVANIDSSNMTPEDWLKLAKRINEalADDGY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    83 DGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYP--INEVTLFFNNRLYRGNR 160
Cdd:smart00870  79 DGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPEarGRGVLVVFNDEIHRARR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   161 TTKAHADGFDAFASPNLAPL---LEAGIHIRRLGTPPAPHGIGELIVHPITPQP-IGVVTIYPGISADVVRNFLRQPVKA 236
Cdd:smart00870 159 VTKTHTSRVDAFQSPNFGPLgyvDEGGVVYYTRPTRRHTKRSPFLLDLKDALLPkVAIVKAYPGMDAELLDALLDSGAKG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   237 LILRSYGVGNAPQNgeFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQN 316
Cdd:smart00870 239 LVLEGTGAGNVPPD--LLEALKEALERGIPVVRTSRCLSGRVDPGYYATGRDLAKAGVISAGDLTPEKARIKLMLALGKG 316

                   ....*..
gi 695765324   317 LSVDEIR 323
Cdd:smart00870 317 LDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
4-323 3.22e-136

Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.


Pssm-ID: 199207 [Multi-domain]  Cd Length: 316  Bit Score: 389.63  E-value: 3.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   4 KSIYVAYTGGTIGMQRSEHGYIPVSGHLQRQLALMPEFHrpemPDFTIHEYEPLMDSSDMTPEDWQHIADDIRAHYDEYD 83
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLPELLE----DCFIEVEQLPNIDSSNMTPEDWLRIARAIAENYDGYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  84 GFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTK 163
Cdd:cd08963   77 GFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSIRGVYVAFNGKLIRGTRARK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 164 AHADGFDAFASPNLAPLLEAGIHIRRLGTPPAPHGIGELIVHPITPQpIGVVTIYPGISADVVRNFLRQPVKALILRSYG 243
Cdd:cd08963  157 VRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFYPDLDPN-VFLLKLIPGLLPAILDALLEKYPRGLILEGFG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 244 VGNAPQNGEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIR 323
Cdd:cd08963  236 AGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSVYAVGQALLEAGVIPGGDMTTEAAVAKLMWLLGQTDDAEEVR 315
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
6-188 1.64e-81

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 245.53  E-value: 1.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324    6 IYVAYTGGTIGMQRSEHG-----YIPVSGHLQRQLALMpefhrpEMPDFTIhEYEPLMDSSDMTPEDWQHIADDIRAHYD 80
Cdd:pfam00710   1 VLILATGGTIASRADSSGgavvpALTGEELLAAVPELA------DIAEIEA-EQVANIDSSNMTPADWLRLARRIAEALD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   81 EYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANY--PINEVTLFFNNRLYRG 158
Cdd:pfam00710  74 DYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPaaRGPGVLVVFNDKLHRA 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 695765324  159 NRTTKAHADGFDAFASPNLAPLLE-AGIHIR 188
Cdd:pfam00710 154 RRVTKTHTSSLDAFDSPNFGPLGEvDGGQVE 184
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
44-336 2.09e-62

glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It is part of a heterodimer, with GatE (TIGR00134), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln). The analogous amidotransferase found in bacteria is the GatABC system, although GatABC homologs in the Archaea appear to act instead on Asp-tRNA(Asn). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 274001 [Multi-domain]  Cd Length: 404  Bit Score: 203.76  E-value: 2.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   44 PEMPDFTIHEYEPLMD--SSDMTPEDWQHIADDI-RAHYDEYDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQIP 120
Cdd:TIGR02153  99 PELLEIANIKARAVFNilSENMKPEYWIKIAEAVaKALKEGADGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRS 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  121 LAELRSDGQINLLNALYVAANyPINEVTLFFNNR-------LYRGNRTTKAHADGFDAFASPNLAPLLE----AGI---- 185
Cdd:TIGR02153 179 SDRPSSDAALNLICAVRAATS-PIAEVTVVMHGEtsdtyclVHRGVKVRKMHTSRRDAFQSINDIPIAKidpdEGIeklr 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  186 --HIRRlgtppaphGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQngEFIQVLAEASQR 263
Cdd:TIGR02153 258 idYRRR--------GEKELELDDKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVSE--DWIPSIKRATDD 327
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765324  264 GIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIRNLMQENLRGELTP 336
Cdd:TIGR02153 328 GVPVVMTSQCLYGRVNLNVYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTDDLEEVRKMMRTNIAGEINE 400
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
44-336 6.01e-62

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 203.15  E-value: 6.01e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  44 PEMPDFTIHEYEPLMD--SSDMTPEDWQHIADDIRAHYDE-YDGFVILHGTDTMAFTASALSFMLEhLGKPVIVTGSQip 120
Cdd:PRK04183 112 PELLDIANIRGRVLFNilSENMTPEYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFMLK-TPVPIVFVGAQ-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 121 laelRS------DGQINLLNALyVAANYPINEVTLFFNNR-------LYRGNRTTKAHADGFDAFASPNLAPLleAGIH- 186
Cdd:PRK04183 189 ----RSsdrpssDAAMNLICAV-LAATSDIAEVVVVMHGTtsddycaLHRGTRVRKMHTSRRDAFQSINDKPL--AKVDy 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 187 ----IRRLGTPPAPHGIGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQngEFIQVLAEASQ 262
Cdd:PRK04183 262 kegkIEFLRKDYRKRGEKELELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIEGTGLGHVST--DLIPSIKRATD 339
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765324 263 RGIVVINLTQCMSGKVNMGGYATGNALAQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIRNLMQENLRGELTP 336
Cdd:PRK04183 340 DGIPVVMTSQCLYGRVNMNVYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTYDLEEVRELMLTNLAGEINE 413
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
3-330 5.41e-60

GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain.


Pssm-ID: 199206 [Multi-domain]  Cd Length: 402  Bit Score: 197.46  E-value: 5.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   3 KKSIYVAYTGGTIGmqrSEHGYipVSGhlqrqlALMPEFHR-------PEMPDFTIHEYEPLMD--SSDMTPEDWQHIAD 73
Cdd:cd08962   70 LPKVSIISTGGTIA---SRVDY--RTG------AVSPAFTAeellraiPELLDIANIKAEVLFNilSENMTPEYWVKIAE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  74 DIRAHYDE-YDGFVILHGTDTMAFTASALSFMLEHLGKPVIVTGSQiplaelRS------DGQINLLNALYVAANyPINE 146
Cdd:cd08962  139 AVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQ------RSsdrpssDAAMNLIAAVLVAAS-DIAE 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 147 VTLFFNNR-------LYRGNRTTKAHADGFDAFASPNLAPLLE----AGI------HIRRlgtppaphGIGELIVHPITP 209
Cdd:cd08962  212 VVVVMHGTtsddyclLHRGTRVRKMHTSRRDAFQSINDEPLAKvdppGKIeklskdYRKR--------GDEELELNDKLE 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 210 QPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQngEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNAL 289
Cdd:cd08962  284 EKVALIKFYPGMDPEIIDFYVDKGYKGIVIEGTGLGHVSE--DLIPSIKKAIDDGIPVVMTSQCIYGRVNLNVYSTGREL 361
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 695765324 290 AQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIRNLMQENL 330
Cdd:cd08962  362 LKAGVIPGEDMLPETAYVKLMWVLGNTDDLEEVRKLMLTNL 402
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
58-323 4.83e-50

Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase.


Pssm-ID: 199205 [Multi-domain]  Cd Length: 320  Bit Score: 169.23  E-value: 4.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  58 MDSSDMTPEDWQHIADDIRAHYDE-YDGFVILHGTDTMAFTASALSFMLEHlGKPVIVTGSQIPLAELRSDGQINLLNAL 136
Cdd:cd00411   55 IASEDITPDDWLKLAKEVAKLLDSdVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 137 YVAAN--YPINEVTLFFNNRLYRGNRTTKAHADGFDAFASPNLAPLleAGIH---IRRLGTPPAPHGI-GELIVHPITPQ 210
Cdd:cd00411  134 RVAKDkdSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPL--GEIKdnkIYYQRKPARKHTDeSEFDVSDIKSL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 211 P-IGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNGefIQVLAEASQRGIVVINLTQCMSGKVNMGGYATgnaL 289
Cdd:cd00411  212 PkVDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPYDV--FPVLSSASKRGVAVVRSSQVIYGGVDLNAEKV---D 286
                        250       260       270
                 ....*....|....*....|....*....|....
gi 695765324 290 AQAGVISGFDMTVEATLTKLHYLLSQNLSVDEIR 323
Cdd:cd00411  287 LKAGVIPAGDLNPEKARVLLMWALTHTKDPEEVQ 320
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
4-323 2.41e-49

Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase.


Pssm-ID: 199208 [Multi-domain]  Cd Length: 319  Bit Score: 167.30  E-value: 2.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   4 KSIYVAYTGGTIGMQRSEHG-YIPVSGHLQRQLALMPEFhrpeMPDFTIhEYEPLM--DSSDMTPEDWQHIADDIRAHYD 80
Cdd:cd08964    1 PRIAVLATGGTIAGTADSSGaYAAPTLSGEELLAAVPGL----ADVADV-EVEQVSnlPSSDMTPADWLALAARVNEALA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  81 --EYDGFVILHGTDTMAFTASALSFMLEHlGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINE--VTLFFNNRLY 156
Cdd:cd08964   76 dpDVDGVVVTHGTDTLEETAYFLDLTLDS-DKPVVLTGAMRPADAPSADGPANLLDAVRVAASPEARGrgVLVVFNDEIH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 157 RGNRTTKAHADGFDAFASPNLAPL---LEAGIHIRRlgtPPAPHGIGELIVHPITPQpIGVVTIYPGISADVVRNFLRQP 233
Cdd:cd08964  155 AARDVTKTHTTSLDAFASPGFGPLgyvDGGKVRFYR---RPARPHTLPSEFDDELPR-VDIVYAYAGADGALLDAAVAAG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 234 VKALILRSYGVGNAPQngEFIQVLAEASQRGIVVINLTQCMSGKVNMG-GYATGNALAQAGVISGFDMTVE-ATLtKLHY 311
Cdd:cd08964  231 AKGIVIAGFGAGNVPP--ALVEALERAVAKGIPVVRSSRVGNGRVLPVyGYGGGADLAEAGAIFAGDLSPQkARI-LLML 307
                        330
                 ....*....|..
gi 695765324 312 LLSQNLSVDEIR 323
Cdd:cd08964  308 ALAAGLDPEEIQ 319
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
212-326 1.26e-40

Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of asparaginase enzymes.


Pssm-ID: 465490 [Multi-domain]  Cd Length: 114  Bit Score: 138.38  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  212 IGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQngEFIQVLAEASQRGIVVINLTQCMSGKVNMGGYATGNALAQ 291
Cdd:pfam17763   2 VDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVPS--ALLDALKEAVARGIPVVRSSRCGSGRVNLGYYETGRDLLE 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 695765324  292 AGVISGFDMTVEATLTKLHYLLSQNLSVDEIRNLM 326
Cdd:pfam17763  80 AGVISGGDLTPEKARIKLMLALGKGLDPEEIRELF 114
ansB PRK11096
L-asparaginase II; Provisional
60-288 1.59e-24

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 102.10  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  60 SSDMTPEDWQHIADDIRAHYDEYDGFVILHGTDTMAFTASALSfMLEHLGKPVIVTGSQIPLAELRSDGQINLLNALYVA 139
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 140 ANYPINE--VTLFFNNRLYRGNRTTKAHADGFDAFASPNLAPLleAGIH---IRRLGTPPAPHGIGELI-VHPITPQP-I 212
Cdd:PRK11096 158 ADKASANrgVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPL--GYIHngkVDYQRTPARKHTTDTPFdVSKLNELPkV 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324 213 GVVTIYPGISADvvrnflrqPVKALILRSY------GVGNAPQNGEFIQVLAEASQRGIVVINltqcmSGKVNMgGYATG 286
Cdd:PRK11096 236 GIVYNYANASDL--------PAKALVDAGYdgivsaGVGNGNLYKTVFDTLATAAKNGVAVVR-----SSRVPT-GATTQ 301

                 ..
gi 695765324 287 NA 288
Cdd:PRK11096 302 DA 303
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
44-338 1.19e-23

L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273115 [Multi-domain]  Cd Length: 349  Bit Score: 99.46  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324   44 PEMPDFTIHEYEPL--MDSSDMTPEDWQHIADDIRAHY--DEYDGFVILHGTDTMAFTASALSFMLEHlGKPVIVTGSQI 119
Cdd:TIGR00520  64 PELKKIANIKGEQVvnVGSQDMNEEVLLKLAKGINELLasDDYDGIVITHGTDTLEETAYFLDLTVKS-DKPVVIVGAMR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  120 PLAELRSDGQINLLNALYVAAN-YPINEVTLF-FNNRLYRGNRTTKAHADGFDAFASPNLAPLleAGIH---IRRLGTPP 194
Cdd:TIGR00520 143 PATSVSADGPMNLYNAVSVAANpKSAGRGVLVvLNDRIASGRYVTKTNTTSLDTFKSRNQGYL--GYIHngkIDYYYPPV 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765324  195 APHGIGEL--IVHPITPQP-IGVVTIYPGISADVVRNFLRQPVKALILRsyGVGNAPQNGEFIQVLAEASQRGIVVINLT 271
Cdd:TIGR00520 221 RKHTCDTPfsVSNLDEPLPkVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSS 298
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765324  272 QCMSGKVnmggyatgnalAQAGVISGFdmtveatltklhyLLSQNLSVDEIRNLMQENLRGELTPDE 338
Cdd:TIGR00520 299 RVGDGMV-----------TPDAEPDGF-------------IASGYLNPQKARVLLQLALTKTYDPEK 341
 
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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