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Conserved domains on  [gi|2212175853|ref|WP_242421563|]
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S9 family peptidase [Acidovorax sp. Root267]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 11445445)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
98-362 1.82e-12

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 66.58  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853  98 ADGKEVRasGLVSVPqkPAGAKSPVLSYQHGtiFRDSEAPSNNAVASEvsvvLASLGYIVLAPDYVGFGASKGTPHPYLL 177
Cdd:COG1506     5 ADGTTLP--GWLYLP--ADGKKYPVVVYVHG--GPGSRDDSFLPLAQA----LASRGYAVLAPDYRGYGESAGDWGGDEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 178 aapsaaatADFLTAARtWRGQANVADNGQLFLTGYSEGGYVTMAThralqAGGSPHLqqLRMVVAGAGPYNVQTTMDGLV 257
Cdd:COG1506    75 --------DDVLAAID-YLAARPYVDPDRIGIYGHSYGGYMALLA-----AARHPDR--FKAAVALAGVSDLRSYYGTTR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 258 DLVRQEQPVigalinpgflrhlgssvqrevrrlllraliPGDADVAYDTRfidyfladDVLALASasnvydwKPNVPVRL 337
Cdd:COG1506   139 EYTERLMGG------------------------------PWEDPEAYAAR--------SPLAYAD-------KLKTPLLL 173
                         250       260
                  ....*....|....*....|....*
gi 2212175853 338 YHGRDDRTVPYASSVSTVRAMRDRG 362
Cdd:COG1506   174 IHGEADDRVPPEQAERLYEALKKAG 198
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
98-362 1.82e-12

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 66.58  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853  98 ADGKEVRasGLVSVPqkPAGAKSPVLSYQHGtiFRDSEAPSNNAVASEvsvvLASLGYIVLAPDYVGFGASKGTPHPYLL 177
Cdd:COG1506     5 ADGTTLP--GWLYLP--ADGKKYPVVVYVHG--GPGSRDDSFLPLAQA----LASRGYAVLAPDYRGYGESAGDWGGDEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 178 aapsaaatADFLTAARtWRGQANVADNGQLFLTGYSEGGYVTMAThralqAGGSPHLqqLRMVVAGAGPYNVQTTMDGLV 257
Cdd:COG1506    75 --------DDVLAAID-YLAARPYVDPDRIGIYGHSYGGYMALLA-----AARHPDR--FKAAVALAGVSDLRSYYGTTR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 258 DLVRQEQPVigalinpgflrhlgssvqrevrrlllraliPGDADVAYDTRfidyfladDVLALASasnvydwKPNVPVRL 337
Cdd:COG1506   139 EYTERLMGG------------------------------PWEDPEAYAAR--------SPLAYAD-------KLKTPLLL 173
                         250       260
                  ....*....|....*....|....*
gi 2212175853 338 YHGRDDRTVPYASSVSTVRAMRDRG 362
Cdd:COG1506   174 IHGEADDRVPPEQAERLYEALKKAG 198
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
149-362 2.60e-07

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 51.08  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 149 VLASLGYIVLAPDYVGfGASKGTP-HPYLLAAPSAAATADFLTAARTWrGQANVADNGQLFLTGYSEGGYVTMAThrALQ 227
Cdd:pfam00326   9 LLADRGYVVAIANGRG-SGGYGEAfHDAGKGDLGQNEFDDFIAAAEYL-IEQGYTDPDRLAIWGGSYGGYLTGAA--LNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 228 AGgsphlQQLRMVVAGAGPYNVQTTMDglvdlvrqeqpvigalinpgflrhlgssvqrevrrlllralipgDADVAYDTR 307
Cdd:pfam00326  85 RP-----DLFKAAVAHVPVVDWLAYMS--------------------------------------------DTSLPFTER 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2212175853 308 FIDYFLADDVL----ALASASNVYDWKPNVPVRLYHGRDDRTVPYASSVSTVRAMRDRG 362
Cdd:pfam00326 116 YMEWGNPWDNEegydYLSPYSPADNVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKG 174
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
98-362 1.82e-12

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 66.58  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853  98 ADGKEVRasGLVSVPqkPAGAKSPVLSYQHGtiFRDSEAPSNNAVASEvsvvLASLGYIVLAPDYVGFGASKGTPHPYLL 177
Cdd:COG1506     5 ADGTTLP--GWLYLP--ADGKKYPVVVYVHG--GPGSRDDSFLPLAQA----LASRGYAVLAPDYRGYGESAGDWGGDEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 178 aapsaaatADFLTAARtWRGQANVADNGQLFLTGYSEGGYVTMAThralqAGGSPHLqqLRMVVAGAGPYNVQTTMDGLV 257
Cdd:COG1506    75 --------DDVLAAID-YLAARPYVDPDRIGIYGHSYGGYMALLA-----AARHPDR--FKAAVALAGVSDLRSYYGTTR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 258 DLVRQEQPVigalinpgflrhlgssvqrevrrlllraliPGDADVAYDTRfidyfladDVLALASasnvydwKPNVPVRL 337
Cdd:COG1506   139 EYTERLMGG------------------------------PWEDPEAYAAR--------SPLAYAD-------KLKTPLLL 173
                         250       260
                  ....*....|....*....|....*
gi 2212175853 338 YHGRDDRTVPYASSVSTVRAMRDRG 362
Cdd:COG1506   174 IHGEADDRVPPEQAERLYEALKKAG 198
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
149-362 2.60e-07

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 51.08  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 149 VLASLGYIVLAPDYVGfGASKGTP-HPYLLAAPSAAATADFLTAARTWrGQANVADNGQLFLTGYSEGGYVTMAThrALQ 227
Cdd:pfam00326   9 LLADRGYVVAIANGRG-SGGYGEAfHDAGKGDLGQNEFDDFIAAAEYL-IEQGYTDPDRLAIWGGSYGGYLTGAA--LNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 228 AGgsphlQQLRMVVAGAGPYNVQTTMDglvdlvrqeqpvigalinpgflrhlgssvqrevrrlllralipgDADVAYDTR 307
Cdd:pfam00326  85 RP-----DLFKAAVAHVPVVDWLAYMS--------------------------------------------DTSLPFTER 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2212175853 308 FIDYFLADDVL----ALASASNVYDWKPNVPVRLYHGRDDRTVPYASSVSTVRAMRDRG 362
Cdd:pfam00326 116 YMEWGNPWDNEegydYLSPYSPADNVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKG 174
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
82-351 3.90e-07

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 50.68  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853  82 PRYNVTSYRIEYLTADadgkEVRASGLVSVPqKPAGAKSPVLSYQHGtifrdseapsNNAVASEVSV---VLASLGYIVL 158
Cdd:COG1073     4 PSDKVNKEDVTFKSRD----GIKLAGDLYLP-AGASKKYPAVVVAHG----------NGGVKEQRALyaqRLAELGFNVL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 159 APDYVGFGASKGTPHPYLLaapsaAATADFLTAARTWRGQANVaDNGQLFLTGYSEGGyvtmAThrALQAGGSphLQQLR 238
Cdd:COG1073    69 AFDYRGYGESEGEPREEGS-----PERRDARAAVDYLRTLPGV-DPERIGLLGISLGG----GY--ALNAAAT--DPRVK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 239 MVVAgagpynvQTTMDGLVDLVRQEQPVIGALINPGFlrhlgssvqrevrrlllrALIPGDAdvaydtrfIDYFLADDVL 318
Cdd:COG1073   135 AVIL-------DSPFTSLEDLAAQRAKEARGAYLPGV------------------PYLPNVR--------LASLLNDEFD 181
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2212175853 319 ALASASNVydwkpNVPVRLYHGRDDRTVPYASS 351
Cdd:COG1073   182 PLAKIEKI-----SRPLLFIHGEKDEAVPFYMS 209
COG4099 COG4099
Predicted peptidase [General function prediction only];
310-363 1.28e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 43.03  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2212175853 310 DYFLAddVLALASASNVYDWKP--NVPVRLYHGRDDRTVPYASSVSTVRAMRDRGA 363
Cdd:COG4099   148 DLFAA--AVPICGGGDPANAANlkKVPVWIFHGAKDDVVPVEESRAMVEALKAAGA 201
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
150-230 4.44e-04

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 41.49  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 150 LASLGYIVLAPDYVGFGASKGTPH---PYLLAAPSAAATADFLTAARTWRGQANVaDNGQLFLTGYSEGGYVT--MATHR 224
Cdd:COG0412    52 LAAAGYVVLAPDLYGRGGPGDDPDearALMGALDPELLAADLRAALDWLKAQPEV-DAGRVGVVGFCFGGGLAllAAARG 130

                  ....*.
gi 2212175853 225 ALQAGG 230
Cdd:COG0412   131 PDLAAA 136
LIP pfam03583
Secretory lipase; These lipases are expressed and secreted during the infection cycle of these ...
154-366 4.61e-03

Secretory lipase; These lipases are expressed and secreted during the infection cycle of these pathogens. In particular, C. albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.


Pssm-ID: 367570  Cd Length: 286  Bit Score: 38.57  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 154 GYIVLAPDYVG----FGASKGTPHPYLlaapsaaataDFLTAARTWRGQANVADNGQLFLTGYSEGGYVTMAThRALQAG 229
Cdd:pfam03583  26 GYYVVVPDYEGpkstFTVGRQSGYAVL----------DSIRAALKSGDSTGINSDAKVGLWGYSGGSLASGWA-AELQPS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 230 GSPHLQqLRMVVAGAGPYNV--------QTTMDGLVDLVrqeqpvIGALIN--PGFLRHLGSSVQREVRRLLLR------ 293
Cdd:pfam03583  95 YAPELQ-LVGAALGGFAANLtataeavdGTVFAGLIALA------LNGLANeyPDFKSILYEETNDSGREALKKlsemcl 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 294 --ALI--PGDADVAYDTRFIDY---FLADDVLALASASNVYDWK--PNVPVRLYHGRDDRTVPYASSVSTVRAMRDRGAG 364
Cdd:pfam03583 168 adALIgyPGDSMFTGDNRVFESgwdILKDETISKTIEDNLLSKSavPQIPVFIYHGVIDEIIPIKDIKKLYQNWCDGGIS 247

                  ..
gi 2212175853 365 DL 366
Cdd:pfam03583 248 SL 249
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
150-262 4.79e-03

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 38.06  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212175853 150 LASLGYIVLAPDYVGFGASKGTPHpyllaapSAAATADFLTAARTWRGQANVADNGQLFLTGYSEGGYVTMathRALQAG 229
Cdd:COG2267    51 LAAAGYAVLAFDLRGHGRSDGPRG-------HVDSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAL---LYAARY 120
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2212175853 230 GSPhlqqLRMVVAGAGPYNVQTTMDGLVDLVRQ 262
Cdd:COG2267   121 PDR----VAGLVLLAPAYRADPLLGPSARWLRA 149
 
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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