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Conserved domains on  [gi|1370468961|ref|XP_024306144|]
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dipeptidase 2 isoform X13 [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 ...
18-191 3.35e-88

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: 265.26  E-value: 3.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEEL 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADI 303
                         170
                  ....*....|....
gi 1370468961 178 QGVLRGNLLRVFRQ 191
Cdd:pfam01244 304 EKILGGNWLRVLRE 317
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
18-191 3.35e-88

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 265.26  E-value: 3.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEEL 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADI 303
                         170
                  ....*....|....
gi 1370468961 178 QGVLRGNLLRVFRQ 191
Cdd:pfam01244 304 EKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
30-195 7.76e-79

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 241.20  E-value: 7.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:COG2355   153 GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFVPA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961 110 VI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRV 188
Cdd:COG2355   233 FLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGEGPEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFLRV 312

                  ....*..
gi 1370468961 189 FRQVEKV 195
Cdd:COG2355   313 LREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
30-188 6.01e-72

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: 223.28  E-value: 6.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:cd01301   151 GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPA 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468961 110 VIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRV 188
Cdd:cd01301   231 FLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGGTPGGLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 309
 
Name Accession Description Interval E-value
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
18-191 3.35e-88

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 265.26  E-value: 3.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  18 AKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKK 97
Cdd:pfam01244 144 ADGAYERKDRDGGLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  98 NGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEEL 177
Cdd:pfam01244 224 TGGVIGVNFYPAFLSPDPEATIEDVVDHIDYIVELAGIDHVGLGSDFDGIGETPEGLEDVSKYPNLTAELLRRGYSEADI 303
                         170
                  ....*....|....
gi 1370468961 178 QGVLRGNLLRVFRQ 191
Cdd:pfam01244 304 EKILGGNWLRVLRE 317
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
30-195 7.76e-79

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 241.20  E-value: 7.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:COG2355   153 GLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFVPA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961 110 VI-QCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRV 188
Cdd:COG2355   233 FLsPDGPDATLDDVVDHIDHIVELVGIDHVGLGSDFDGIGEGPEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFLRV 312

                  ....*..
gi 1370468961 189 FRQVEKV 195
Cdd:COG2355   313 LREVLAA 319
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
30-188 6.01e-72

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: 223.28  E-value: 6.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468961  30 GLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMG 109
Cdd:cd01301   151 GLTPFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPA 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370468961 110 VIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRV 188
Cdd:cd01301   231 FLSPGADATLDDVVRHIDYIVDLIGIDHVGLGSDFDGIGGTPGGLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 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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