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Conserved domains on  [gi|881010789|ref|WP_048731546|]
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MULTISPECIES: S9 family peptidase [Corynebacterium]

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];
381-635 2.63e-55

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


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 188.30  E-value: 2.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 381 FVSRDGLELSGWLYLPEsvrnssndvsGNALPPAFIHIHGGPELQAKPIHHDVLAsIVEAGFVVFTPNVRGSSGSGRSFE 460
Cdd:COG1506    2 FKSADGTTLPGWLYLPA----------DGKKYPVVVYVHGGPGSRDDSFLPLAQA-LASRGYAVLAPDYRGYGESAGDWG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 461 H-------AGDRYgrfaaiadiaaarafLVDAGLADPERIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMTSFETYYQ 533
Cdd:COG1506   71 GdevddvlAAIDY---------------LAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 534 STEPWLAQaafpRYGYPYQDAELLRDISPLHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTDFLVVEGEGH 613
Cdd:COG1506  136 TTREYTER----LMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGH 211
                        250       260
                 ....*....|....*....|..
gi 881010789 614 KFSKPRSRALIgETIIAFFTEH 635
Cdd:COG1506  212 GFSGAGAPDYL-ERILDFLDRH 232
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
381-635 2.63e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 188.30  E-value: 2.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 381 FVSRDGLELSGWLYLPEsvrnssndvsGNALPPAFIHIHGGPELQAKPIHHDVLAsIVEAGFVVFTPNVRGSSGSGRSFE 460
Cdd:COG1506    2 FKSADGTTLPGWLYLPA----------DGKKYPVVVYVHGGPGSRDDSFLPLAQA-LASRGYAVLAPDYRGYGESAGDWG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 461 H-------AGDRYgrfaaiadiaaarafLVDAGLADPERIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMTSFETYYQ 533
Cdd:COG1506   71 GdevddvlAAIDY---------------LAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 534 STEPWLAQaafpRYGYPYQDAELLRDISPLHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTDFLVVEGEGH 613
Cdd:COG1506  136 TTREYTER----LMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGH 211
                        250       260
                 ....*....|....*....|..
gi 881010789 614 KFSKPRSRALIgETIIAFFTEH 635
Cdd:COG1506  212 GFSGAGAPDYL-ERILDFLDRH 232
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
433-635 6.60e-40

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 145.45  E-value: 6.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  433 VLASIVEAGFVVFTPNVRGSSGSGRSFEHAGDR-YGRFAAIADIAAARAfLVDAGLADPERIALGGRSYGGFMSLLASAW 511
Cdd:pfam00326   6 NAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGdLGQNEFDDFIAAAEY-LIEQGYTDPDRLAIWGGSYGGYLTGAALNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  512 YPDQFAAIVDACGMTSFETYYQSTEPWLAqAAFPRYGYPYQDAELLRDISPLHRAEEMKV--PTLFIHGEWDTNVPPRES 589
Cdd:pfam00326  85 RPDLFKAAVAHVPVVDWLAYMSDTSLPFT-ERYMEWGNPWDNEEGYDYLSPYSPADNVKVypPLLLIHGLLDDRVPPWQS 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 881010789  590 GQMRNAMDAYGVPTDFLVVEGEGHKFSKPRSRALIGETIIAFFTEH 635
Cdd:pfam00326 164 LKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEY 209
PRK10566 PRK10566
esterase; Provisional
485-635 3.58e-09

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 57.69  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 485 AGLADPERIALGGRSYGGFMSLLASAWYPDQFAAivdACGMTSfeTYYQStepwLAQAAFPRY--GYPYQDAELLRDISP 562
Cdd:PRK10566 101 EGWLLDDRLAVGGASMGGMTALGIMARHPWVKCV---ASLMGS--GYFTS----LARTLFPPLipETAAQQAEFNNIVAP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 563 L------HRAEEM-KVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTD--FLVVEGEGHKFSKPrsrALigETIIAFFT 633
Cdd:PRK10566 172 LaewevtHQLEQLaDRPLLLWHGLADDVVPAAESLRLQQALRERGLDKNltCLWEPGVRHRITPE---AL--DAGVAFFR 246

                 ..
gi 881010789 634 EH 635
Cdd:PRK10566 247 QH 248
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
441-602 1.21e-04

esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 273828 [Multi-domain]  Cd Length: 212  Bit Score: 43.63  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  441 GFVVFTPNVRGSSGSGRSFEHAGDryGRFAAIADIAAARAFLVDAGLA----DPERIALGGRSYGGFMSLLASAWYPDQF 516
Cdd:TIGR01840  43 GFVLVAPEQTSYNSSNNCWDWFFT--HHRARGTGEVESLHQLIDAVKAnysiDPNRVYVTGLSAGGGMTAVLGCTYPDVF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  517 AAIVDACGMTsfetyYQSTEpwLAQAAFPRYGYPYQDAELLRDISPLHRAEEMKVPTLFI-HGEWDTNVPPRESGQMRNA 595
Cdd:TIGR01840 121 AGGASNAGLP-----YGEAS--SSISATPQMCTAATAASVCRLVRGMQSEYNGPTPIMSVvHGDADYTVLPGNADEIRDA 193

                  ....*...
gi 881010789  596 M-DAYGVP 602
Cdd:TIGR01840 194 MlKVYGET 201
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
381-635 2.63e-55

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 188.30  E-value: 2.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 381 FVSRDGLELSGWLYLPEsvrnssndvsGNALPPAFIHIHGGPELQAKPIHHDVLAsIVEAGFVVFTPNVRGSSGSGRSFE 460
Cdd:COG1506    2 FKSADGTTLPGWLYLPA----------DGKKYPVVVYVHGGPGSRDDSFLPLAQA-LASRGYAVLAPDYRGYGESAGDWG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 461 H-------AGDRYgrfaaiadiaaarafLVDAGLADPERIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMTSFETYYQ 533
Cdd:COG1506   71 GdevddvlAAIDY---------------LAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 534 STEPWLAQaafpRYGYPYQDAELLRDISPLHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTDFLVVEGEGH 613
Cdd:COG1506  136 TTREYTER----LMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGH 211
                        250       260
                 ....*....|....*....|..
gi 881010789 614 KFSKPRSRALIgETIIAFFTEH 635
Cdd:COG1506  212 GFSGAGAPDYL-ERILDFLDRH 232
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
433-635 6.60e-40

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 145.45  E-value: 6.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  433 VLASIVEAGFVVFTPNVRGSSGSGRSFEHAGDR-YGRFAAIADIAAARAfLVDAGLADPERIALGGRSYGGFMSLLASAW 511
Cdd:pfam00326   6 NAQLLADRGYVVAIANGRGSGGYGEAFHDAGKGdLGQNEFDDFIAAAEY-LIEQGYTDPDRLAIWGGSYGGYLTGAALNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  512 YPDQFAAIVDACGMTSFETYYQSTEPWLAqAAFPRYGYPYQDAELLRDISPLHRAEEMKV--PTLFIHGEWDTNVPPRES 589
Cdd:pfam00326  85 RPDLFKAAVAHVPVVDWLAYMSDTSLPFT-ERYMEWGNPWDNEEGYDYLSPYSPADNVKVypPLLLIHGLLDDRVPPWQS 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 881010789  590 GQMRNAMDAYGVPTDFLVVEGEGHKFSKPRSRALIGETIIAFFTEH 635
Cdd:pfam00326 164 LKLVAALQRKGVPFLLLIFPDEGHGIGKPRNKVEEYARELAFLLEY 209
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
377-635 1.40e-23

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 100.37  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 377 ELVYFVSRDGLELSGWLYLPESVRNSsndvsgnalPPAFIHIHGGPELqakPIHHDVLASI-VEAGFVVFTPNVRG---S 452
Cdd:COG1073   11 EDVTFKSRDGIKLAGDLYLPAGASKK---------YPAVVVAHGNGGV---KEQRALYAQRlAELGFNVLAFDYRGygeS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 453 SGSGRSFE-------HAGDRYgrfaaiadiaaarafLVDAGLADPERIALGGRSYGGFMSLLASAWYPdQFAAIVDACGM 525
Cdd:COG1073   79 EGEPREEGsperrdaRAAVDY---------------LRTLPGVDPERIGLLGISLGGGYALNAAATDP-RVKAVILDSPF 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 526 TSFE--TYYQSTEPWLAQAAFPRYGYPYQDAELLRD-ISPLHRAEEMKVPTLFIHGEWDTNVPPRESgqmRNAMDAYGVP 602
Cdd:COG1073  143 TSLEdlAAQRAKEARGAYLPGVPYLPNVRLASLLNDeFDPLAKIEKISRPLLFIHGEKDEAVPFYMS---EDLYEAAAEP 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 881010789 603 TDFLVVEGEGHK--FSKPRSRALigETIIAFFTEH 635
Cdd:COG1073  220 KELLIVPGAGHVdlYDRPEEEYF--DKLAEFFKKN 252
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
377-632 9.04e-18

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 82.71  E-value: 9.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 377 ELVYFVSRDGLELSGWLYLPESvrnssndvSGNAlpPA--FIHIHGGPELQAKpihhDVLASIVEAGFVVFTPNVRGSSG 454
Cdd:COG0412    4 ETVTIPTPDGVTLPGYLARPAG--------GGPR--PGvvVLHEIFGLNPHIR----DVARRLAAAGYVVLAPDLYGRGG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 455 SGRSFEHAGDRYGRFAAIADIAAaraflVDAGLA--------DPERIALGGRSYGGFMSLLASAWYPDqfaaivdacgmt 526
Cdd:COG0412   70 PGDDPDEARALMGALDPELLAAD-----LRAALDwlkaqpevDAGRVGVVGFCFGGGLALLAAARGPD------------ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 527 sfetyyqstepwlAQAAFPRYGYPYQDAellrdisPLHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTDFL 606
Cdd:COG0412  133 -------------LAAAVSFYGGLPADD-------LLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELH 192
                        250       260       270
                 ....*....|....*....|....*....|...
gi 881010789 607 VVEGEGHKFSKP-------RSRALIGETIIAFF 632
Cdd:COG0412  193 VYPGAGHGFTNPgrprydpAAAEDAWQRTLAFL 225
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
376-634 2.34e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.73  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 376 PELVYFVSRDGLELSGWLYLPESVRnssndvsgnalPPAFIHIHGGPElqakpiHHDVLASIVE----AGFVVFTPNVRG 451
Cdd:COG2267    3 RRLVTLPTRDGLRLRGRRWRPAGSP-----------RGTVVLVHGLGE------HSGRYAELAEalaaAGYAVLAFDLRG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 452 SsgsGRSfehaGDRYGRFAAIADIAAARAFLVDAGLADP-ERIALGGRSYGGFMSLLASAWYPDQFAAIVdACGmtsfet 530
Cdd:COG2267   66 H---GRS----DGPRGHVDSFDDYVDDLRAALDALRARPgLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLA------ 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 531 yyqstePWLAqaAFPRYGYPYQdaeLLRDISPLHRAEEMKVPTLFIHGEWDTNVPPRESgqmRNAMDAYGVPTDFLVVEG 610
Cdd:COG2267  132 ------PAYR--ADPLLGPSAR---WLRALRLAEALARIDVPVLVLHGGADRVVPPEAA---RRLAARLSPDVELVLLPG 197
                        250       260
                 ....*....|....*....|....*.
gi 881010789 611 EGH--KFSKPRSRALigETIIAFFTE 634
Cdd:COG2267  198 ARHelLNEPAREEVL--AAILAWLER 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
379-613 1.45e-11

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 64.60  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 379 VYFVSRDGLELSGWLYLPEsvrnssnDVSGNALPPAFIHIHG----GPELQaKPIHH--DVLASIVEA---GFVVFTPNV 449
Cdd:COG4099   23 TFTDPSDGDTLPYRLYLPK-------GYDPGKKYPLVLFLHGagerGTDNE-KQLTHgaPKFINPENQakfPAIVLAPQC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 450 RGSSGSGRSFEHAgdrygrfaaiadiaaARAFLVDAGLA----DPERIALGGRSYGGFMSL-LASAwYPDQFAAIVDACG 524
Cdd:COG4099   95 PEDDYWSDTKALD---------------AVLALLDDLIAeyriDPDRIYLTGLSMGGYGTWdLAAR-YPDLFAAAVPICG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 525 MTSFETYyqstePWLAqaafprygypyqdaellrdisplhraeemKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTD 604
Cdd:COG4099  159 GGDPANA-----ANLK-----------------------------KVPVWIFHGAKDDVVPVEESRAMVEALKAAGADVK 204

                 ....*....
gi 881010789 605 FLVVEGEGH 613
Cdd:COG4099  205 YTEYPGVGH 213
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
393-635 1.74e-11

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 63.74  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 393 LYLPESvrnssndvsGNALPPAFIHIHGG-PELQAKPIHHDVLASIVE-AGFVVFTPNVRgssgsgRSFEHA-------- 462
Cdd:COG0657    3 VYRPAG---------AKGPLPVVVYFHGGgWVSGSKDTHDPLARRLAArAGAAVVSVDYR------LAPEHPfpaaleda 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 463 ----------GDRYGrfaaiadiaaaraflvdaglADPERIALGGRSYGGFMSLLASAWYPD----QFAAIVDACGMTSF 528
Cdd:COG0657   68 yaalrwlranAAELG--------------------IDPDRIAVAGDSAGGHLAAALALRARDrggpRPAAQVLIYPVLDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 529 etyyqstepwlaqaafprygypyqdaellrDISPLHRAEEMKVPTLFIHGEWDTNVppRESGQMRNAMDAYGVPTDFLVV 608
Cdd:COG0657  128 ------------------------------TASPLRADLAGLPPTLIVTGEADPLV--DESEALAAALRAAGVPVELHVY 175
                        250       260       270
                 ....*....|....*....|....*....|.
gi 881010789 609 EGEGHKF----SKPRSRALIgETIIAFFTEH 635
Cdd:COG0657  176 PGGGHGFgllaGLPEARAAL-AEIAAFLRRA 205
DLH pfam01738
Dienelactone hydrolase family;
430-621 1.49e-09

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 58.52  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  430 HHDVLASIVEAGFVVFTPNV---RGSSGSGRSFEHAGDRYGRFAAIADIAAARAFLVDAGLADPE----RIALGGRSYGG 502
Cdd:pfam01738  28 IREIADRLADEGYVALAPDLyfrQGDPNDEADAARAMFELVSKRVMEKVLDDLEAAVNYLKSQPEvspkKVGVVGYCMGG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  503 FMSLLASAwypdqfaaivdacgmtsfetyyqstEPWLAQAAFPRYGypyqdaelLRDISPLHRAEEMKVPTLFIHGEWDT 582
Cdd:pfam01738 108 ALAVLLAA-------------------------KGPLVDAAVGFYG--------VGPEPPLIEAPDIKAPILFHFGEEDH 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 881010789  583 NVPPRESGQMRNAMDAYGVPTDFLVVEGEGHKFSKPRSR 621
Cdd:pfam01738 155 FVPADSRELIEEALKAANVDHQIHSYPGAGHAFANDSRP 193
PRK10566 PRK10566
esterase; Provisional
485-635 3.58e-09

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 57.69  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 485 AGLADPERIALGGRSYGGFMSLLASAWYPDQFAAivdACGMTSfeTYYQStepwLAQAAFPRY--GYPYQDAELLRDISP 562
Cdd:PRK10566 101 EGWLLDDRLAVGGASMGGMTALGIMARHPWVKCV---ASLMGS--GYFTS----LARTLFPPLipETAAQQAEFNNIVAP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 563 L------HRAEEM-KVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTD--FLVVEGEGHKFSKPrsrALigETIIAFFT 633
Cdd:PRK10566 172 LaewevtHQLEQLaDRPLLLWHGLADDVVPAAESLRLQQALRERGLDKNltCLWEPGVRHRITPE---AL--DAGVAFFR 246

                 ..
gi 881010789 634 EH 635
Cdd:PRK10566 247 QH 248
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
487-613 7.18e-09

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 57.56  E-value: 7.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 487 LADPERIALGGRSYGGFMSLLASAWYPDQFAAIVDacgmtsfetyyQSTEPWLAQAAFPRYGYPyqdaELLRDISPLHRa 566
Cdd:COG2382  192 SADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGS-----------FSGSFWWPPGDADRGGWA----ELLAAGAPKKP- 255
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 881010789 567 eemkvPTLFIH-GEWDTNVPPreSGQMRNAMDAYGVPTDFLVVEGeGH 613
Cdd:COG2382  256 -----LRFYLDvGTEDDLLEA--NRALAAALKAKGYDVEYREFPG-GH 295
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
482-613 9.19e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 53.08  E-value: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 482 LVDAglADPERIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMtsFETYYQS-TEPWLAQAAFPRygypyqDAELLRDI 560
Cdd:COG0596   82 LLDA--LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV--LAALAEPlRRPGLAPEALAA------LLRALART 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 881010789 561 SPLHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYgvptDFLVVEGEGH 613
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNA----ELVVLPGAGH 200
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
492-599 4.66e-07

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 51.57  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  492 RIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMTSFETYY--------QSTEPWLAQA------------------AFP 545
Cdd:pfam02129  96 KVGMTGISYLGTTQLAAAATGPPGLKAIAPESGISDLYDYYreggavraPGGLGWEDLDllaealtsrraddgdayrAAA 175
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881010789  546 RYGY------PYQDAELL---------------RDISPLHRAEEMKVPTLFIHGEWDTNVppresgqMRNAMDAY 599
Cdd:pfam02129 176 RYEAagdellAELDRQLFllewllqtgdydafwQDRNYLEDADKVKAPVLLVGGWQDWNV-------KNGAIKLY 243
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
393-589 3.95e-06

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 48.33  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  393 LYLPESVRNSSndvsgnalpPAFIHIHGG------PELQAKPIHhDVLASIVEAGFVVFTPNVRgSSGSGR--------- 457
Cdd:pfam20434   3 IYLPKNAKGPY---------PVVIWIHGGgwnsgdKEADMGFMT-NTVKALLKAGYAVASINYR-LSTDAKfpaqiqdvk 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  458 ---SF--EHAgDRYGRfaaiadiaaaraflvdaglaDPERIALGGRSYGGFMSLLA-------------------SAWYP 513
Cdd:pfam20434  72 aaiRFlrANA-AKYGI--------------------DTNKIALMGFSAGGHLALLAglsnnnkefegnvgdytpeSSKES 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881010789  514 DQFAAIVDACG---MTSFETYYQSTEPWLAQAAFPRyGYPYQDAELLRDISPLHRAEEMKVPTLFIHGEWDTNVPPRES 589
Cdd:pfam20434 131 FKVNAVVDFYGptdLLDMDSCGTHNDAKSPETLLLG-APPLENPDLAKSASPITYVDKNDPPFLIIHGDKDPLVPYCQS 208
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
385-585 5.88e-06

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 48.46  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 385 DGLELSGWLYLPESVRNSSNdvsgnalPPAFIHIHGG---PELQAKPIHHDVLASivEAGFVVFTPNVRGSSGSG--RSF 459
Cdd:COG3509   33 GGGTRTYRLYVPAGYDGGAP-------LPLVVALHGCggsAADFAAGTGLNALAD--REGFIVVYPEGTGRAPGRcwNWF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 460 EHAGDRYGRFaaiadiaaaraflvDAGL-------------ADPERIALGGRSYGGFMSLLASAWYPDQFAAIvdacGMT 526
Cdd:COG3509  104 DGRDQRRGRD--------------DVAFiaalvddlaarygIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAV----APV 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 881010789 527 SfetyyqstepwlaqaafpryGYPYQDAellrdiSPLHRAEEMKVPTLFIHGEWDTNVP 585
Cdd:COG3509  166 A--------------------GLPYGAA------SDAACAPGRPVPVLVIHGTADPTVP 198
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
491-635 1.17e-05

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 47.24  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 491 ERIALGGRSYGGFMSLLASAWYPDqFAAIVDACGMTSFETYYQSTEPWLAQAA--------------FPRYGYPYQDAEL 556
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYLArslrgigsdiedpeVAEYAYDRTPLRA 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 557 LRDISPL-----HRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVptDFLVVEGEGHKFSKPRSRALIGETIIAF 631
Cdd:COG1647  163 LAELQRLirevrRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDK--ELVWLEDSGHVITLDKDREEVAEEILDF 240

                 ....
gi 881010789 632 FTEH 635
Cdd:COG1647  241 LERL 244
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
434-613 2.74e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 46.64  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 434 LASiveAGFVVFTPNVRGSSGSGRSFEHAGDRYGRFAAIADI-------------AAARAFLVDAGLADPERIALGGRSY 500
Cdd:COG4188   85 LAS---HGYVVAAPDHPGSNAADLSAALDGLADALDPEELWErpldlsfvldqllALNKSDPPLAGRLDLDRIGVIGHSL 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 501 GGFMSLLASAWYPDqFAAIVDACGmtsfetyyQSTEPWLAQAAFPRYGYPYQDAELLR--DISPLHRA-------EEMKV 571
Cdd:COG4188  162 GGYTALALAGARLD-FAALRQYCG--------KNPDLQCRALDLPRLAYDLRDPRIKAvvALAPGGSGlfgeeglAAITI 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 881010789 572 PTLFIHGEWDTNVPPrESGQMRNAMDAYGVPTDFLVVEGEGH 613
Cdd:COG4188  233 PVLLVAGSADDVTPA-PDEQIRPFDLLPGADKYLLTLEGATH 273
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
441-602 1.21e-04

esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ab-hydrolase family. This subfamily includes bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases, feruloyl esterases, and others from fungi. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 273828 [Multi-domain]  Cd Length: 212  Bit Score: 43.63  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  441 GFVVFTPNVRGSSGSGRSFEHAGDryGRFAAIADIAAARAFLVDAGLA----DPERIALGGRSYGGFMSLLASAWYPDQF 516
Cdd:TIGR01840  43 GFVLVAPEQTSYNSSNNCWDWFFT--HHRARGTGEVESLHQLIDAVKAnysiDPNRVYVTGLSAGGGMTAVLGCTYPDVF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  517 AAIVDACGMTsfetyYQSTEpwLAQAAFPRYGYPYQDAELLRDISPLHRAEEMKVPTLFI-HGEWDTNVPPRESGQMRNA 595
Cdd:TIGR01840 121 AGGASNAGLP-----YGEAS--SSISATPQMCTAATAASVCRLVRGMQSEYNGPTPIMSVvHGDADYTVLPGNADEIRDA 193

                  ....*...
gi 881010789  596 M-DAYGVP 602
Cdd:TIGR01840 194 MlKVYGET 201
YpfH COG0400
Predicted esterase [General function prediction only];
489-613 1.89e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 489 DPERIALGGRSYGGFMSLLASAWYPDQFAAIVdacgmtsfetyyqstepwlaqaAFprYGYPYQDAELLRDISPLHRaee 568
Cdd:COG0400   87 DPERIVLAGFSQGAAMALSLALRRPELLAGVV----------------------AL--SGYLPGEEALPAPEAALAG--- 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 881010789 569 mkVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPTDFLVVEGeGH 613
Cdd:COG0400  140 --TPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYPG-GH 181
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
488-615 1.37e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 40.66  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  488 ADPERIALGGRSYGGFMSLLASAWYPD----QFAAIVDACGMT-------SFETYYQSTEPWLAQAAFPRYGYPYQDAEL 556
Cdd:pfam07859  68 ADPSRIAVAGDSAGGNLAAAVALRARDeglpKPAGQVLIYPGTdlrtespSYLAREFADGPLLTRAAMDWFWRLYLPGAD 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881010789  557 LRD--ISPLHRAEEMKV-PTLFIHGEWDtnvPPRESG-QMRNAMDAYGVPTDFLVVEGEGHKF 615
Cdd:pfam07859 148 RDDplASPLFASDLSGLpPALVVVAEFD---PLRDEGeAYAERLRAAGVPVELIEYPGMPHGF 207
PRK05371 PRK05371
x-prolyl-dipeptidyl aminopeptidase; Provisional
492-603 1.53e-03

x-prolyl-dipeptidyl aminopeptidase; Provisional


Pssm-ID: 235435 [Multi-domain]  Cd Length: 767  Bit Score: 41.91  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 492 RIALGGRSYGGFMSLLASAWYPDQFAAIVDACGMTSFETYYQS----TEP---------WLAQAAFPRYGYPYQD----- 553
Cdd:PRK05371 339 KVAMTGKSYLGTLPNAVATTGVEGLETIIPEAAISSWYDYYREnglvRAPggyqgedldVLAELTYSRNLLAGDYlrhne 418
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789 554 ------AELLRDISP--------------LHRAEEMKVPTLFIHGEWDTNVPPRESGQMRNAMDAYGVPT 603
Cdd:PRK05371 419 acekllAELTAAQDRktgdyndfwddrnyLKDADKIKASVLVVHGLNDWNVKPKQVYQWWDALPENGVPK 488
Esterase_PHB pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
489-596 2.26e-03

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 40.04  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  489 DPERIALGGRSYGGFMSLLASAWYPDQFAAIvdacGMTSFETYYQSTEPWLAQAAFpRYGyPYQDAELLRDISPLHRAEE 568
Cdd:pfam10503  98 DGARVYLAGLSAGAALAALLAHCYPDVFAAV----GLHSGLPFGCAADAASALDAM-RRG-PGPAPGALIDAASDVRSYP 171
                          90       100
                  ....*....|....*....|....*...
gi 881010789  569 mKVPTLFIHGEWDTNVPPRESGQMRNAM 596
Cdd:pfam10503 172 -ALPAIIFHGDADSTVASANADQLTAAF 198
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
413-520 6.40e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 38.64  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881010789  413 PAFIHIHGGPElqAKPIHHDVLASIVEAGFVVFTPNVRGSSGSgrSFEHAGDRYGRFAAIADIAAarafLVDAglADPER 492
Cdd:pfam00561   1 PPVLLLHGLPG--SSDLWRKLAPALARDGFRVIALDLRGFGKS--SRPKAQDDYRTDDLAEDLEY----ILEA--LGLEK 70
                          90       100
                  ....*....|....*....|....*...
gi 881010789  493 IALGGRSYGGFMSLLASAWYPDQFAAIV 520
Cdd:pfam00561  71 VNLVGHSMGGLIALAYAAKYPDRVKALV 98
 
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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