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Conserved domains on  [gi|767990388|ref|XP_011521576|]
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dipeptidase 2 isoform X12 [Homo sapiens]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
18-204 7.61e-85

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member pfam01244:

Pssm-ID: 469705  Cd Length: 317  Bit Score: 257.17  E-value: 7.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLI 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLT 290
                         170       180
                  ....*....|....*....|....*..
gi 767990388  178 EELLSRGWSEEELQGVLRGNLLRVFRQ 204
Cdd:pfam01244 291 AELLRRGYSEADIEKILGGNWLRVLRE 317
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
18-204 7.61e-85

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 257.17  E-value: 7.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLI 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLT 290
                         170       180
                  ....*....|....*....|....*..
gi 767990388  178 EELLSRGWSEEELQGVLRGNLLRVFRQ 204
Cdd:pfam01244 291 AELLRRGYSEADIEKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
30-208 2.10e-75

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 233.11  E-value: 2.10e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:COG2355  153 GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFVPA 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388 110 VI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWSEE 188
Cdd:COG2355  233 FLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGE-------------GPEGLEDVSDLPNLTEALLKRGYSEE 299
                        170       180
                 ....*....|....*....|
gi 767990388 189 ELQGVLRGNLLRVFRQVEKV 208
Cdd:COG2355  300 DIEKILGGNFLRVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
30-201 1.98e-68

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: 214.81  E-value: 1.98e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:cd01301  151 GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPA 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388 110 VIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWSEEE 189
Cdd:cd01301  231 FLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGG-------------TPGGLEDVSDLPNLTAELLERGYSEEE 297
                        170
                 ....*....|..
gi 767990388 190 LQGVLRGNLLRV 201
Cdd:cd01301  298 IEKIAGGNFLRV 309
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
18-204 7.61e-85

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 257.17  E-value: 7.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388   98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGkesglkptswwphRFPQGLEDVSTYPVLI 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIG-------------ETPEGLEDVSKYPNLT 290
                         170       180
                  ....*....|....*....|....*..
gi 767990388  178 EELLSRGWSEEELQGVLRGNLLRVFRQ 204
Cdd:pfam01244 291 AELLRRGYSEADIEKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
30-208 2.10e-75

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 233.11  E-value: 2.10e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:COG2355  153 GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFVPA 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388 110 VI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWSEE 188
Cdd:COG2355  233 FLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGE-------------GPEGLEDVSDLPNLTEALLKRGYSEE 299
                        170       180
                 ....*....|....*....|
gi 767990388 189 ELQGVLRGNLLRVFRQVEKV 208
Cdd:COG2355  300 DIEKILGGNFLRVLREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
30-201 1.98e-68

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: 214.81  E-value: 1.98e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:cd01301  151 GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPA 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990388 110 VIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKesglkptswwphrFPQGLEDVSTYPVLIEELLSRGWSEEE 189
Cdd:cd01301  231 FLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGG-------------TPGGLEDVSDLPNLTAELLERGYSEEE 297
                        170
                 ....*....|..
gi 767990388 190 LQGVLRGNLLRV 201
Cdd:cd01301  298 IEKIAGGNFLRV 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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