NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767990385|ref|XP_011521575|]
View 

dipeptidase 2 isoform X10 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
1-254 3.73e-115

Membrane dipeptidase (Peptidase family M19);


:

Pssm-ID: 395996  Cd Length: 317  Bit Score: 336.14  E-value: 3.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385    1 MCASYSE-LELVTSAKALNDTQ---KLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAEssakGVHSFYN 76
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWAD----GAYERKD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   77 NISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:pfam01244 153 RDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  157 SMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLIEELLSRGWS 236
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLTAELLRRGYS 299
                         250
                  ....*....|....*...
gi 767990385  237 EEELQGVLRGNLLRVFRQ 254
Cdd:pfam01244 300 EADIEKILGGNWLRVLRE 317
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
1-254 3.73e-115

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 336.14  E-value: 3.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385    1 MCASYSE-LELVTSAKALNDTQ---KLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAEssakGVHSFYN 76
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWAD----GAYERKD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   77 NISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:pfam01244 153 RDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  157 SMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLIEELLSRGWS 236
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLTAELLRRGYS 299
                         250
                  ....*....|....*...
gi 767990385  237 EEELQGVLRGNLLRVFRQ 254
Cdd:pfam01244 300 EADIEKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
1-258 4.22e-99

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 295.51  E-value: 4.22e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   1 MCASYSE-LELVTSAK---ALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAeSSAKGVHSFYn 76
Cdd:COG2355   75 LVAASPDrLRLARTAAdleAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLA-DGATDPDTDG- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  77 nisGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:COG2355  153 ---GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINF 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385 157 SMGVI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGW 235
Cdd:COG2355  230 VPAFLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGE-------------GPEGLEDVSDLPNLTEALLKRGY 296
                        250       260
                 ....*....|....*....|...
gi 767990385 236 SEEELQGVLRGNLLRVFRQVEKV 258
Cdd:COG2355  297 SEEDIEKILGGNFLRVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
1-251 8.03e-92

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: 276.44  E-value: 8.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   1 MCASYSE-LELVTSA---KALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAESsaKGVHSFYn 76
Cdd:cd01301   74 LIAAYPRiFVLATSSadiRRALKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADG--CGEKRGG- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  77 nisGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:cd01301  151 ---GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNF 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385 157 SMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWS 236
Cdd:cd01301  228 YPAFLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGG-------------TPGGLEDVSDLPNLTAELLERGYS 294
                        250
                 ....*....|....*
gi 767990385 237 EEELQGVLRGNLLRV 251
Cdd:cd01301  295 EEEIEKIAGGNFLRV 309
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
1-254 3.73e-115

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 336.14  E-value: 3.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385    1 MCASYSE-LELVTSAKALNDTQ---KLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAEssakGVHSFYN 76
Cdd:pfam01244  77 LVRKNPEqLRLVRTADDIRRAKkegKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWAD----GAYERKD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   77 NISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:pfam01244 153 RDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  157 SMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLIEELLSRGWS 236
Cdd:pfam01244 233 YPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLTAELLRRGYS 299
                         250
                  ....*....|....*...
gi 767990385  237 EEELQGVLRGNLLRVFRQ 254
Cdd:pfam01244 300 EADIEKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
1-258 4.22e-99

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 295.51  E-value: 4.22e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   1 MCASYSE-LELVTSAK---ALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAeSSAKGVHSFYn 76
Cdd:COG2355   75 LVAASPDrLRLARTAAdleAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLA-DGATDPDTDG- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  77 nisGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:COG2355  153 ---GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINF 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385 157 SMGVI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGW 235
Cdd:COG2355  230 VPAFLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGE-------------GPEGLEDVSDLPNLTEALLKRGY 296
                        250       260
                 ....*....|....*....|...
gi 767990385 236 SEEELQGVLRGNLLRVFRQVEKV 258
Cdd:COG2355  297 SEEDIEKILGGNFLRVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
1-251 8.03e-92

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: 276.44  E-value: 8.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385   1 MCASYSE-LELVTSA---KALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAESsaKGVHSFYn 76
Cdd:cd01301   74 LIAAYPRiFVLATSSadiRRALKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADG--CGEKRGG- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385  77 nisGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSL 156
Cdd:cd01301  151 ---GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNF 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990385 157 SMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWS 236
Cdd:cd01301  228 YPAFLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGG-------------TPGGLEDVSDLPNLTAELLERGYS 294
                        250
                 ....*....|....*
gi 767990385 237 EEELQGVLRGNLLRV 251
Cdd:cd01301  295 EEEIEKIAGGNFLRV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH