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Conserved domains on  [gi|1631970745|ref|NP_001357127|]
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dipeptidase 3 isoform c precursor [Homo sapiens]

Protein Classification

dipeptidase( domain architecture ID 10472453)

M19 family dipeptidase is a metal-dependent dimeric enzyme belonging to the amidohydrolase superfamily

CATH:  3.20.20.140
EC:  3.4.13.19
Gene Ontology:  GO:0006508|GO:0070573|GO:0046872
MEROPS:  M19
SCOP:  4002206

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
87-407 1.22e-138

Membrane dipeptidase (Peptidase family M19);


:

Pssm-ID: 395996  Cd Length: 317  Bit Score: 401.62  E-value: 1.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  87 LMRSFPLVDGHNDLPQVLRQRYKNVLQDvnlrNFSHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHR 166
Cdd:pfam01244   1 LHRDSPVIDGHNDLPLRLRQEGDNILFD----GDSGLQTDLPRLREGGVGAQFWAIFVPCDAQYDDAVQATLEQIDLFYR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 167 MCASYSE-LELVTSAEGLNSSQ---KLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHmyt 242
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWADGAYERKDR--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 243 nVSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTL 322
Cdd:pfam01244 154 -DGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 323 SMGVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLL 402
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADIEKILGGNWL 312

                  ....*
gi 1631970745 403 RVFRQ 407
Cdd:pfam01244 313 RVLRE 317
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
87-407 1.22e-138

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 401.62  E-value: 1.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  87 LMRSFPLVDGHNDLPQVLRQRYKNVLQDvnlrNFSHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHR 166
Cdd:pfam01244   1 LHRDSPVIDGHNDLPLRLRQEGDNILFD----GDSGLQTDLPRLREGGVGAQFWAIFVPCDAQYDDAVQATLEQIDLFYR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 167 MCASYSE-LELVTSAEGLNSSQ---KLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHmyt 242
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWADGAYERKDR--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 243 nVSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTL 322
Cdd:pfam01244 154 -DGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 323 SMGVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLL 402
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADIEKILGGNWL 312

                  ....*
gi 1631970745 403 RVFRQ 407
Cdd:pfam01244 313 RVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
88-411 9.30e-114

Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441922  Cd Length: 319  Bit Score: 338.27  E-value: 9.30e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  88 MRSFPLVDGHNDLPQVLRQRYKNVLQDVNlrnfsHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHRM 167
Cdd:COG2355     1 HERMPVIDGHCDLLLRLLEPGRDLTERSP-----DGHVDLPRLREGGVGAQFFAVFVPPEYRPASALARALEQIDALHRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 168 CASYSE-LELVTSAEGLN---SSQKLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHmytn 243
Cdd:COG2355    76 VAASPDrLRLARTAADLEaalAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLADGATDPDTD---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 244 vSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTLS 323
Cdd:COG2355   152 -GGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 324 MGVLQCNLL-ANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLL 402
Cdd:COG2355   231 PAFLSPDGPdATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGEGPEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFL 310

                  ....*....
gi 1631970745 403 RVFRQVEKV 411
Cdd:COG2355   311 RVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
92-404 1.12e-108

renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal dipeptidase, is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. Although the biological function of the enzyme is still unknown, it has been suggested to play a role in the renal glutathione metabolism.


Pssm-ID: 238626  Cd Length: 309  Bit Score: 324.97  E-value: 1.12e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  92 PLVDGHNDLPQVLRQRYKNVLQDVNlrnfsHGQTSLDRLRDGLVGAQFWSASVSCQSQDQT---AVRLALEQIDLIHRMC 168
Cdd:cd01301     1 PVVDGHNDLLYRLRREGKDFFTKDA-----GGHVDLPRLREGGVGGQVFAIFVPPGELQPTwldALERALEQIDRVRRLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 169 ASYSE-LELVTSAEGL---NSSQKLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHhmytnv 244
Cdd:cd01301    76 AAYPRiFVLATSSADIrraLKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADGCGEKRG------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 245 SGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTLSM 324
Cdd:cd01301   150 GGLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 325 GVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLLRV 404
Cdd:cd01301   230 AFLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGGTPGGLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 309
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
87-407 1.22e-138

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 401.62  E-value: 1.22e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  87 LMRSFPLVDGHNDLPQVLRQRYKNVLQDvnlrNFSHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHR 166
Cdd:pfam01244   1 LHRDSPVIDGHNDLPLRLRQEGDNILFD----GDSGLQTDLPRLREGGVGAQFWAIFVPCDAQYDDAVQATLEQIDLFYR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 167 MCASYSE-LELVTSAEGLNSSQ---KLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHmyt 242
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWADGAYERKDR--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 243 nVSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTL 322
Cdd:pfam01244 154 -DGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 323 SMGVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLL 402
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADIEKILGGNWL 312

                  ....*
gi 1631970745 403 RVFRQ 407
Cdd:pfam01244 313 RVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
88-411 9.30e-114

Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441922  Cd Length: 319  Bit Score: 338.27  E-value: 9.30e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  88 MRSFPLVDGHNDLPQVLRQRYKNVLQDVNlrnfsHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHRM 167
Cdd:COG2355     1 HERMPVIDGHCDLLLRLLEPGRDLTERSP-----DGHVDLPRLREGGVGAQFFAVFVPPEYRPASALARALEQIDALHRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 168 CASYSE-LELVTSAEGLN---SSQKLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHmytn 243
Cdd:COG2355    76 VAASPDrLRLARTAADLEaalAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLADGATDPDTD---- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 244 vSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTLS 323
Cdd:COG2355   152 -GGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 324 MGVLQCNLL-ANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLL 402
Cdd:COG2355   231 PAFLSPDGPdATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGEGPEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFL 310

                  ....*....
gi 1631970745 403 RVFRQVEKV 411
Cdd:COG2355   311 RVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
92-404 1.12e-108

renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal dipeptidase, is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. Although the biological function of the enzyme is still unknown, it has been suggested to play a role in the renal glutathione metabolism.


Pssm-ID: 238626  Cd Length: 309  Bit Score: 324.97  E-value: 1.12e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745  92 PLVDGHNDLPQVLRQRYKNVLQDVNlrnfsHGQTSLDRLRDGLVGAQFWSASVSCQSQDQT---AVRLALEQIDLIHRMC 168
Cdd:cd01301     1 PVVDGHNDLLYRLRREGKDFFTKDA-----GGHVDLPRLREGGVGGQVFAIFVPPGELQPTwldALERALEQIDRVRRLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 169 ASYSE-LELVTSAEGL---NSSQKLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHhmytnv 244
Cdd:cd01301    76 AAYPRiFVLATSSADIrraLKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADGCGEKRG------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 245 SGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTLSM 324
Cdd:cd01301   150 GGLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970745 325 GVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLLRV 404
Cdd:cd01301   230 AFLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGGTPGGLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 309
 
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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