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Conserved domains on  [gi|171095|gb|AAA34438|]
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asparaginase II precursor [Saccharomyces cerevisiae]

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List of domain hits

Name Accession Description Interval E-value
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
33-242 5.25e-95

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  Cd Length: 319  Bit Score: 284.40  E-value: 5.25e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    33 PSIKIFGTGGTIASKGSTSatTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDD 112
Cdd:cd08964   1 PRIAVLATGGTIAGTADSS--GAYAAPTLSGEELLAAVPGLADVADVEVEQVSNLPSSDMTPADWLALAARVNEALADPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   113 YAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFW 192
Cdd:cd08964  79 VDGVVVTHGTDTLEETAYFLDLTLDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAASPEARGRGVLVVFNDEIHAARD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 171095   193 TTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTD 242
Cdd:cd08964 159 VTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDELPR 208
 
Name Accession Description Interval E-value
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
33-242 5.25e-95

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  Cd Length: 319  Bit Score: 284.40  E-value: 5.25e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    33 PSIKIFGTGGTIASKGSTSatTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDD 112
Cdd:cd08964   1 PRIAVLATGGTIAGTADSS--GAYAAPTLSGEELLAAVPGLADVADVEVEQVSNLPSSDMTPADWLALAARVNEALADPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   113 YAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFW 192
Cdd:cd08964  79 VDGVVVTHGTDTLEETAYFLDLTLDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAASPEARGRGVLVVFNDEIHAARD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 171095   193 TTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTD 242
Cdd:cd08964 159 VTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDELPR 208
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
9-242 4.57e-139

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: 129611  Cd Length: 349  Bit Score: 398.00  E-value: 4.57e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095       9 LSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAEKANLDYLQVSNV 87
Cdd:TIGR00520   1 MELFKKSANAAVVLSGSAAQARSLPNIKILATGGTIAGKGQSSASTAGYKVGeLGIEDLIEAVPSLKDIANIKGEQIVNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      88 GSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVS 167
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLASDDYDGIVITHGTDTLEETAYFLDLTVKSDKPVVIVGAMRPSTSVSADGPMNLYNAVS 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171095     168 IAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQ-FFDISNLTD 242
Cdd:TIGR00520 161 VAANPKSAGRGVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIHNGKIDYYYPPVRKHTCDtPFSVSNLDE 236
AnsB COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Amino acid transport and ...
1-244 2.71e-83

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


Pssm-ID: 223330  Cd Length: 351  Bit Score: 255.68  E-value: 2.71e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     1 MRSLNTLLLSLFVamssgapllkireEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAEKANL 79
Cdd:COG0252   1 MNVLNAGLATLSA-------------SPNSKLPKILILATGGTIASGTDSSTGAVTPTSGaLEILALLPAVPALNIAANI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    80 DYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGP 159
Cdd:COG0252  68 EGEQVLNIDSSDMTPEDWLRLAEAINEALDDGDVDGVVITHGTDTMEETAFFLSLTLNTPKPVVLTGAMRPADAPSSDGP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   160 MNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKpNGWQFFDISN 239
Cdd:COG0252 148 ANLRNAVSVAADPKSRGVGVLVVFNDRIHRGVRVTKTHTSRFDAFESPNLGPLGEIDRGKVSFFRDPYR-RGDSGFDVSP 226

                ....*
gi 171095   240 LTDLR 244
Cdd:COG0252 227 LTEPK 231
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
35-242 9.15e-82

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  Cd Length: 323  Bit Score: 250.51  E-value: 9.15e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095       35 IKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAekANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDY 113
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPTAGaEELLALLPALPELA--DDIEVEQVANIDSSNMTPEDWLKLAKRINEALADDGY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      114 AGAVVTHGTDTMEETAFFLDLTI-NSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFW 192
Cdd:smart00870  79 DGVVVTHGTDTLEETAYFLSLTLdSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPEARGRGVLVVFNDEIHRARR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 171095      193 TTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTD 242
Cdd:smart00870 159 VTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPFLLDLKD 208
Asparaginase pfam00710
Asparaginase;
35-229 5.48e-76

Asparaginase;


Pssm-ID: 250074  Cd Length: 318  Bit Score: 235.52  E-value: 5.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      35 IKIFGTGGTIASKGSTSATTAGYsvgLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALasDDYA 114
Cdd:pfam00710   2 ILILYTGGTIAMVADPSGGAVAP---LSGEDLLAAVPELADIADIEVEQLFNIDSSNMTPADWLRLAERINEAL--DDYD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     115 GAVVTHGTDTMEETAFFLDLTI-NSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWT 193
Cdd:pfam00710  77 GVVVTHGTDTLEETASFLSLMLeSLDKPVVLTGAQRPASAPSSDGPMNLLDALRVAASPDARGRGVLVVFNDKIHRGRRV 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 171095     194 TKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKP 229
Cdd:pfam00710 157 TKTHTSSLDAFASPNFGPLGEVGGGRVKYFRDPLRR 192
ansB PRK11096
L-asparaginase II; Provisional
8-245 1.10e-71

L-asparaginase II; Provisional


Pssm-ID: 182958  Cd Length: 347  Bit Score: 225.37  E-value: 1.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      8 LLSLFVAMSSGAPLlkireeknsSLPSIKIFGTGGTIASKGStSATTAGYSVG-LTVNDLIEAVPSLAEKANLDYLQVSN 86
Cdd:PRK11096   7 ALAALVMGFSGAAF---------ALPNITILATGGTIAGGGD-SATKSNYTAGkVGVENLVNAVPQLKDIANVKGEQVVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     87 VGSNSLNYTHLIPLYHGISEALASDDyaGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAV 166
Cdd:PRK11096  77 IGSQDMNDEVWLTLAKKINTDCDKTD--GFVITHGTDTMEETAYFLDLTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    167 SIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQF-FDISNLTDLRK 245
Cdd:PRK11096 155 VTAADKASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIHNGKVDYQRTPARKHTTDTpFDVSKLNELPK 234
ansA PRK09461
cytoplasmic asparaginase I; Provisional
111-204 3.41e-09

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 54.98  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    111 DDYAGAVVTHGTDTMEETA----FFLDltiNSEKPVCIAGAMRPATATSADGPMNLYQAVSIAA----SEKSLgrgtmiT 182
Cdd:PRK09461  80 DDYDGFVILHGTDTMAYTAsalsFMLE---NLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAnypiNEVTL------F 150
                         90       100
                 ....*....|....*....|..
gi 171095    183 LNDRIASGFWTTKMNANSLDTF 204
Cdd:PRK09461 151 FNNKLFRGNRTTKAHADGFDAF 172
 
Name Accession Description Interval E-value
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
33-242 5.25e-95

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  Cd Length: 319  Bit Score: 284.40  E-value: 5.25e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    33 PSIKIFGTGGTIASKGSTSatTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDD 112
Cdd:cd08964   1 PRIAVLATGGTIAGTADSS--GAYAAPTLSGEELLAAVPGLADVADVEVEQVSNLPSSDMTPADWLALAARVNEALADPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   113 YAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFW 192
Cdd:cd08964  79 VDGVVVTHGTDTLEETAYFLDLTLDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAASPEARGRGVLVVFNDEIHAARD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 171095   193 TTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTD 242
Cdd:cd08964 159 VTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFDDELPR 208
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
9-242 4.57e-139

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: 129611  Cd Length: 349  Bit Score: 398.00  E-value: 4.57e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095       9 LSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAEKANLDYLQVSNV 87
Cdd:TIGR00520   1 MELFKKSANAAVVLSGSAAQARSLPNIKILATGGTIAGKGQSSASTAGYKVGeLGIEDLIEAVPSLKDIANIKGEQIVNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      88 GSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVS 167
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLASDDYDGIVITHGTDTLEETAYFLDLTVKSDKPVVIVGAMRPSTSVSADGPMNLYNAVS 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171095     168 IAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQ-FFDISNLTD 242
Cdd:TIGR00520 161 VAANPKSAGRGVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIHNGKIDYYYPPVRKHTCDtPFSVSNLDE 236
AnsB COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Amino acid transport and ...
1-244 2.71e-83

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


Pssm-ID: 223330  Cd Length: 351  Bit Score: 255.68  E-value: 2.71e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     1 MRSLNTLLLSLFVamssgapllkireEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAEKANL 79
Cdd:COG0252   1 MNVLNAGLATLSA-------------SPNSKLPKILILATGGTIASGTDSSTGAVTPTSGaLEILALLPAVPALNIAANI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    80 DYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGP 159
Cdd:COG0252  68 EGEQVLNIDSSDMTPEDWLRLAEAINEALDDGDVDGVVITHGTDTMEETAFFLSLTLNTPKPVVLTGAMRPADAPSSDGP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   160 MNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKpNGWQFFDISN 239
Cdd:COG0252 148 ANLRNAVSVAADPKSRGVGVLVVFNDRIHRGVRVTKTHTSRFDAFESPNLGPLGEIDRGKVSFFRDPYR-RGDSGFDVSP 226

                ....*
gi 171095   240 LTDLR 244
Cdd:COG0252 227 LTEPK 231
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
35-242 9.15e-82

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  Cd Length: 323  Bit Score: 250.51  E-value: 9.15e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095       35 IKIFGTGGTIASKGSTSATTAGYSVG-LTVNDLIEAVPSLAekANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDY 113
Cdd:smart00870   1 ILVLYTGGTIAMKADPSTGAVGPTAGaEELLALLPALPELA--DDIEVEQVANIDSSNMTPEDWLKLAKRINEALADDGY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      114 AGAVVTHGTDTMEETAFFLDLTI-NSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFW 192
Cdd:smart00870  79 DGVVVTHGTDTLEETAYFLSLTLdSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAASPEARGRGVLVVFNDEIHRARR 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 171095      193 TTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTD 242
Cdd:smart00870 159 VTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPFLLDLKD 208
Asparaginase pfam00710
Asparaginase;
35-229 5.48e-76

Asparaginase;


Pssm-ID: 250074  Cd Length: 318  Bit Score: 235.52  E-value: 5.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      35 IKIFGTGGTIASKGSTSATTAGYsvgLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALasDDYA 114
Cdd:pfam00710   2 ILILYTGGTIAMVADPSGGAVAP---LSGEDLLAAVPELADIADIEVEQLFNIDSSNMTPADWLRLAERINEAL--DDYD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     115 GAVVTHGTDTMEETAFFLDLTI-NSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWT 193
Cdd:pfam00710  77 GVVVTHGTDTLEETASFLSLMLeSLDKPVVLTGAQRPASAPSSDGPMNLLDALRVAASPDARGRGVLVVFNDKIHRGRRV 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 171095     194 TKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKP 229
Cdd:pfam00710 157 TKTHTSSLDAFASPNFGPLGEVGGGRVKYFRDPLRR 192
ansB PRK11096
L-asparaginase II; Provisional
8-245 1.10e-71

L-asparaginase II; Provisional


Pssm-ID: 182958  Cd Length: 347  Bit Score: 225.37  E-value: 1.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      8 LLSLFVAMSSGAPLlkireeknsSLPSIKIFGTGGTIASKGStSATTAGYSVG-LTVNDLIEAVPSLAEKANLDYLQVSN 86
Cdd:PRK11096   7 ALAALVMGFSGAAF---------ALPNITILATGGTIAGGGD-SATKSNYTAGkVGVENLVNAVPQLKDIANVKGEQVVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     87 VGSNSLNYTHLIPLYHGISEALASDDyaGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAV 166
Cdd:PRK11096  77 IGSQDMNDEVWLTLAKKINTDCDKTD--GFVITHGTDTMEETAYFLDLTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    167 SIAASEKSLGRGTMITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQF-FDISNLTDLRK 245
Cdd:PRK11096 155 VTAADKASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIHNGKVDYQRTPARKHTTDTpFDVSKLNELPK 234
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
33-245 1.01e-62

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  Cd Length: 320  Bit Score: 201.59  E-value: 1.01e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    33 PSIKIFGTGGTIASKGStSATTAGYSVG-LTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASD 111
Cdd:cd00411   1 PNITILATGGTIAGVGD-SATYSAYVAGaLGVEKLIKAVPELKELANVKGEQLMNIASEDITPDDWLKLAKEVAKLLDSD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   112 DYaGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGF 191
Cdd:cd00411  80 VD-GIVITHGTDT*EETAYFLSLTLKNDKPVVLVGAMRPSTAMSADGPFNLYNAVRVAKDKDSRGRGVLVVMNDKVHSGR 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 171095   192 WTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQ-FFDISNLTDLRK 245
Cdd:cd00411 159 DVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDEsEFDVSDIKSLPK 213
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
32-231 6.28e-31

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  Cd Length: 336  Bit Score: 117.61  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      32 LPSIKIFGTGGTIASKgsTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALasD 111
Cdd:TIGR00519   1 LKDISIISTGGTIASK--VDYRTGAVHPVFTADELLSAVPELLDIANIDGEALMNILSENMKPEYWVEIAEAVKKEY--D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     112 DYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASE----KSLGRGTMITLNDRI 187
Cdd:TIGR00519  77 DYDGFVITHGTDTMAYTAAALSFMLETPKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYiaevTVCMHGVTLDFNCRL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 171095     188 ASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNG 231
Cdd:TIGR00519 157 HRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRG 200
PRK04183 PRK04183
glutamyl-tRNA(Gln) amidotransferase subunit D; Validated
20-172 2.06e-27

glutamyl-tRNA(Gln) amidotransferase subunit D; Validated


Pssm-ID: 235245  Cd Length: 419  Bit Score: 108.39  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095     20 PLLKIREEKNSSLPSIKIFGTGGTIASK--GSTSATTAGysvgLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHL 97
Cdd:PRK04183  63 EPPPKEIEKDPGLPNVSILSTGGTIASKvdYRTGAVTPA----FTAEDLLRAVPELLDIANIRGRVLFNILSENMTPEYW 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 171095     98 IPLYHGISEALaSDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASE 172
Cdd:PRK04183 139 VEIAEAVYEEI-KNGADGVVVAHGTDTMHYTAAALSFMLKTPVPIVFVGAQRSSDRPSSDAAMNLICAVLAATSD 212
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
33-214 7.48e-27

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  Cd Length: 316  Bit Score: 105.74  E-value: 7.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    33 PSIKIFGTGGTIASKgstsATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALasDD 112
Cdd:cd08963   1 KKILLLYTGGTIASV----KTEGGLAPALTAEELLSYLPELLEDCFIEVEQLPNIDSSNMTPEDWLRIARAIAENY--DG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095   113 YAGAVVTHGTDTMEETAFFLDLTI-NSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSlgRGTMITLNDRIASGF 191
Cdd:cd08963  75 YDGFVITHGTDTMAYTAAALSFLLqNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGSI--RGVYVAFNGKLIRGT 152
                       170       180
                ....*....|....*....|...
gi 171095   192 WTTKMNANSLDTFRADEQGYLGY 214
Cdd:cd08963 153 RARKVRTTSFDAFESINYPLLAE 175
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
20-172 6.85e-25

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: 233752  Cd Length: 404  Bit Score: 100.92  E-value: 6.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095      20 PLLKIREEKNSSLPSIKIFGTGGTIASKgsTSATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIP 99
Cdd:TIGR02153  50 VPPPAEIEKKPGLPKVSIISTGGTIASR--VDYETGAVYPAFTAEELARAVPELLEIANIKARAVFNILSENMKPEYWIK 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171095     100 LYHGISEALaSDDYAGAVVTHGTDTMEETAFFLDLTINSE-KPVCIAGAMRPATATSADGPMNLYQAVSIAASE 172
Cdd:TIGR02153 128 IAEAVAKAL-KEGADGVVVAHGTDTMAYTAAALSFMFETLpVPVVLVGAQRSSDRPSSDAALNLICAVRAATSP 200
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
16-172 1.69e-24

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  Cd Length: 402  Bit Score: 99.61  E-value: 1.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    16 SSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSaTTAGYSVgLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYT 95
Cdd:cd08962  54 EKPKPELGEEIEKKPGLPKVSIISTGGTIASRVDYR-TGAVSPA-FTAEELLRAIPELLDIANIKAEVLFNILSENMTPE 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171095    96 HLIPLYHGISEALaSDDYAGAVVTHGTDTMEETAFFLDLTINSE-KPVCIAGAMRPATATSADGPMNLYQAVSIAASE 172
Cdd:cd08962 132 YWVKIAEAVYKEI-KEGADGVVVAHGTDTMHYTASALSFMLETLpVPVVFVGAQRSSDRPSSDAAMNLIAAVLVAASD 208
ansA PRK09461
cytoplasmic asparaginase I; Provisional
111-204 3.41e-09

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 54.98  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171095    111 DDYAGAVVTHGTDTMEETA----FFLDltiNSEKPVCIAGAMRPATATSADGPMNLYQAVSIAA----SEKSLgrgtmiT 182
Cdd:PRK09461  80 DDYDGFVILHGTDTMAYTAsalsFMLE---NLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAnypiNEVTL------F 150
                         90       100
                 ....*....|....*....|..
gi 171095    183 LNDRIASGFWTTKMNANSLDTF 204
Cdd:PRK09461 151 FNNKLFRGNRTTKAHADGFDAF 172
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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