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Conserved domains on  [gi|1430391654|gb|AXE19580|]
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membrane dipeptidase [Runella rosea]

Protein Classification

dipeptidase( domain architecture ID 10006403)

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

CATH:  3.20.20.140
EC:  3.4.13.-
Gene Ontology:  GO:0006508|GO:0070573|GO:0046872
MEROPS:  M19
PubMed:  9949873
SCOP:  4002206

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
36-411 9.88e-146

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


:

Pssm-ID: 441922  Cd Length: 319  Bit Score: 416.85  E-value: 9.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  36 HEKAFTVDTHADTPMLLSRGGFDITKDNDARTsnskVDYPRMKRGGLDAIFFAVYLGQGPRTseahEAAKKRALGIFDAV 115
Cdd:COG2355     1 HERMPVIDGHCDLLLRLLEPGRDLTERSPDGH----VDLPRLREGGVGAQFFAVFVPPEYRP----ASALARALEQIDAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 116 NTTLKQTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKgaE 195
Cdd:COG2355    73 HRLVAASPDRLRLARTAADLEAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLADGATDPD--T 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 196 YQGLSPLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNLL 275
Cdd:COG2355   151 DGGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 276 SDYIKTIPPSperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkypiqlATVKDAIDHIDHIVKVIGIDHV 355
Cdd:COG2355   231 PAFLSPDGPD------------------------------------------------ATLDDVVDHIDHIVELVGIDHV 262
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1430391654 356 GMGADFDGGGAL-ADCFDVSQYENMTIELVRRGYSKKDIEKIWSGNFFRVMKAVEKG 411
Cdd:COG2355   263 GLGSDFDGIGEGpEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFLRVLREVLAA 319
 
Name Accession Description Interval E-value
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
36-411 9.88e-146

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 416.85  E-value: 9.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  36 HEKAFTVDTHADTPMLLSRGGFDITKDNDARTsnskVDYPRMKRGGLDAIFFAVYLGQGPRTseahEAAKKRALGIFDAV 115
Cdd:COG2355     1 HERMPVIDGHCDLLLRLLEPGRDLTERSPDGH----VDLPRLREGGVGAQFFAVFVPPEYRP----ASALARALEQIDAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 116 NTTLKQTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKgaE 195
Cdd:COG2355    73 HRLVAASPDRLRLARTAADLEAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLADGATDPD--T 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 196 YQGLSPLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNLL 275
Cdd:COG2355   151 DGGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 276 SDYIKTIPPSperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkypiqlATVKDAIDHIDHIVKVIGIDHV 355
Cdd:COG2355   231 PAFLSPDGPD------------------------------------------------ATLDDVVDHIDHIVELVGIDHV 262
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1430391654 356 GMGADFDGGGAL-ADCFDVSQYENMTIELVRRGYSKKDIEKIWSGNFFRVMKAVEKG 411
Cdd:COG2355   263 GLGSDFDGIGEGpEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFLRVLREVLAA 319
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
35-407 5.86e-124

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 361.56  E-value: 5.86e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  35 IHEKAFTVDTHADTPMLLSRGGFDITKDNDartSNSKVDYPRMKRGGLDAIFFAVYLGQGPRTSEAHEAAKKRalgiFDA 114
Cdd:pfam01244   1 LHRDSPVIDGHNDLPLRLRQEGDNILFDGD---SGLQTDLPRLREGGVGAQFWAIFVPCDAQYDDAVQATLEQ----IDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 115 VNTTLKQTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKGA 194
Cdd:pfam01244  74 FYRLVRKNPEQLRLVRTADDIRRAKKEGKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWADGAYERKDR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 195 EYqGLSPLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNL 274
Cdd:pfam01244 154 DG-GLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 275 LSDYIKTIPPsperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkypiqlATVKDAIDHIDHIVKVIGIDH 354
Cdd:pfam01244 233 YPAFLSPDPE-------------------------------------------------ATIEDVVDHIDYIVELAGIDH 263
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1430391654 355 VGMGADFDGGGALADCF-DVSQYENMTIELVRRGYSKKDIEKIWSGNFFRVMKA 407
Cdd:pfam01244 264 VGLGSDFDGIGETPEGLeDVSKYPNLTAELLRRGYSEADIEKILGGNWLRVLRE 317
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
41-404 3.00e-119

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: 349.24  E-value: 3.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  41 TVDTHADTPMLLSRGGFDItkdnDARTSNSKVDYPRMKRGGLDAIFFAVYLGQGPRTsEAHEAAKKRALGIFDAVNTTLK 120
Cdd:cd01301     2 VVDGHNDLLYRLRREGKDF----FTKDAGGHVDLPRLREGGVGGQVFAIFVPPGELQ-PTWLDALERALEQIDRVRRLIA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 121 QTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKGAeyqGLS 200
Cdd:cd01301    77 AYPRIFVLATSSADIRRALKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADGCGEKRGG---GLT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 201 PLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNLLSDYIK 280
Cdd:cd01301   154 PFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPAFLS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 281 tippsperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkyPIQLATVKDAIDHIDHIVKVIGIDHVGMGAD 360
Cdd:cd01301   234 -------------------------------------------------PGADATLDDVVRHIDYIVDLIGIDHVGLGSD 264
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1430391654 361 FDGGGALAD-CFDVSQYENMTIELVRRGYSKKDIEKIWSGNFFRV 404
Cdd:cd01301   265 FDGIGGTPGgLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 309
 
Name Accession Description Interval E-value
COG2355 COG2355
Zn-dependent dipeptidase, microsomal dipeptidase homolog [Posttranslational modification, ...
36-411 9.88e-146

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


Pssm-ID: 441922  Cd Length: 319  Bit Score: 416.85  E-value: 9.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  36 HEKAFTVDTHADTPMLLSRGGFDITKDNDARTsnskVDYPRMKRGGLDAIFFAVYLGQGPRTseahEAAKKRALGIFDAV 115
Cdd:COG2355     1 HERMPVIDGHCDLLLRLLEPGRDLTERSPDGH----VDLPRLREGGVGAQFFAVFVPPEYRP----ASALARALEQIDAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 116 NTTLKQTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKgaE 195
Cdd:COG2355    73 HRLVAASPDRLRLARTAADLEAALAEGKIAALLGIEGAEALGGDLDNLDVLYRLGVRYIGLTWNGDNRLADGATDPD--T 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 196 YQGLSPLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNLL 275
Cdd:COG2355   151 DGGLTDFGREVVREMNRLGMIVDVSHLSDKTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAERGGVIGINFV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 276 SDYIKTIPPSperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkypiqlATVKDAIDHIDHIVKVIGIDHV 355
Cdd:COG2355   231 PAFLSPDGPD------------------------------------------------ATLDDVVDHIDHIVELVGIDHV 262
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1430391654 356 GMGADFDGGGAL-ADCFDVSQYENMTIELVRRGYSKKDIEKIWSGNFFRVMKAVEKG 411
Cdd:COG2355   263 GLGSDFDGIGEGpEGLEDVSDLPNLTEALLKRGYSEEDIEKILGGNFLRVLREVLAA 319
Peptidase_M19 pfam01244
Membrane dipeptidase (Peptidase family M19);
35-407 5.86e-124

Membrane dipeptidase (Peptidase family M19);


Pssm-ID: 395996  Cd Length: 317  Bit Score: 361.56  E-value: 5.86e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  35 IHEKAFTVDTHADTPMLLSRGGFDITKDNDartSNSKVDYPRMKRGGLDAIFFAVYLGQGPRTSEAHEAAKKRalgiFDA 114
Cdd:pfam01244   1 LHRDSPVIDGHNDLPLRLRQEGDNILFDGD---SGLQTDLPRLREGGVGAQFWAIFVPCDAQYDDAVQATLEQ----IDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 115 VNTTLKQTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKGA 194
Cdd:pfam01244  74 FYRLVRKNPEQLRLVRTADDIRRAKKEGKIAILLGLEGAHALGDDLALLRTFYALGVRYLGLTWNCNNLWADGAYERKDR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 195 EYqGLSPLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNL 274
Cdd:pfam01244 154 DG-GLTPFGKEVVREMNRLGMLIDLSHLSERTFWDVLELSKAPVIASHSNARALCDHPRNLTDEQLKAIAETGGVIGVNF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 275 LSDYIKTIPPsperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkypiqlATVKDAIDHIDHIVKVIGIDH 354
Cdd:pfam01244 233 YPAFLSPDPE-------------------------------------------------ATIEDVVDHIDYIVELAGIDH 263
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1430391654 355 VGMGADFDGGGALADCF-DVSQYENMTIELVRRGYSKKDIEKIWSGNFFRVMKA 407
Cdd:pfam01244 264 VGLGSDFDGIGETPEGLeDVSKYPNLTAELLRRGYSEADIEKILGGNWLRVLRE 317
rDP_like cd01301
renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal ...
41-404 3.00e-119

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: 349.24  E-value: 3.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654  41 TVDTHADTPMLLSRGGFDItkdnDARTSNSKVDYPRMKRGGLDAIFFAVYLGQGPRTsEAHEAAKKRALGIFDAVNTTLK 120
Cdd:cd01301     2 VVDGHNDLLYRLRREGKDF----FTKDAGGHVDLPRLREGGVGGQVFAIFVPPGELQ-PTWLDALERALEQIDRVRRLIA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 121 QTSELAELATTPEDAYRIGKTGKRVIFIGVENGYAMGHDLPMLQKFYDLGARYMTLCHSSNNDICDSSTDPKGAeyqGLS 200
Cdd:cd01301    77 AYPRIFVLATSSADIRRALKEGKLAAIISIEGAHALGGDLALLRLLYRLGVRYLGLTWNGDNKFADGCGEKRGG---GLT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 201 PLGEQVVKEMNRLGMIIDVSHVSDSTFYDVIRQSKVPVVATHSGAKAICNHPRNLTDDMLKALAKNGGVIQLNLLSDYIK 280
Cdd:cd01301   154 PFGKELVREMNRLGIIIDLSHLSERTFWDVLDISNAPVIASHSNARALCDHPRNLTDAQLKAIAETGGVIGVNFYPAFLS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430391654 281 tippsperegalkelyakysikdrrgmmtlpeaeqqkaradfmelnkkyPIQLATVKDAIDHIDHIVKVIGIDHVGMGAD 360
Cdd:cd01301   234 -------------------------------------------------PGADATLDDVVRHIDYIVDLIGIDHVGLGSD 264
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1430391654 361 FDGGGALAD-CFDVSQYENMTIELVRRGYSKKDIEKIWSGNFFRV 404
Cdd:cd01301   265 FDGIGGTPGgLEDVSDLPNLTAELLERGYSEEEIEKIAGGNFLRV 309
RRM2_SXL cd12651
RNA recognition motif 2 (RRM2) found in Drosophila sex-lethal (SXL) and similar proteins; This ...
248-283 4.99e-03

RNA recognition motif 2 (RRM2) found in Drosophila sex-lethal (SXL) and similar proteins; This subfamily corresponds to the RRM2 of the sex-lethal protein (SXL) which governs sexual differentiation and X chromosome dosage compensation in Drosophila melanogaster. It induces female-specific alternative splicing of the transformer (tra) pre-mRNA by binding to the tra uridine-rich polypyrimidine tract at the non-sex-specific 3' splice site during the sex-determination process. SXL binds also to its own pre-mRNA and promotes female-specific alternative splicing. SXL contains an N-terminal Gly/Asn-rich domain that may be responsible for the protein-protein interaction, and tandem RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), that show high preference to bind single-stranded, uridine-rich target RNA transcripts.


Pssm-ID: 410054 [Multi-domain]  Cd Length: 81  Bit Score: 36.02  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1430391654 248 ICNHPRNLTDDML-KALAKNGGVIQLNLLSDYIKTIP 283
Cdd:cd12651     7 VTNLPRTITEDELdTIFGAYGNIVQKNLLRDKLTGRP 43
 
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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