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Conserved domains on  [gi|489183427|ref|WP_003092865|]
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MULTISPECIES: alpha/beta hydrolase [Pseudomonas]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta hydrolase 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
6-295 1.87e-67

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 210.93  E-value: 1.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   6 VEFRSE-GVALRGWLYLPEARAE-RPAIVMTHGFSGVKEQYLDrYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEIDPvmQ 83
Cdd:COG1073   13 VTFKSRdGIKLAGDLYLPAGASKkYPAVVVAHGNGGVKEQRAL-YAQRLAELGFNVLAFDYRGYGESEGEPREEGSP--E 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  84 RRGYRDAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVAQVPTVSghasalrrtraeqlpalLASFDADR 163
Cdd:COG1073   90 RRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS-----------------LEDLAAQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 164 QRRFEGlppALLPAVAAGPdepcamagadahrfftdsaalapswcnRVTLRSAeLARENEPGIHIGRISpTPLLMIVADR 243
Cdd:COG1073  153 AKEARG---AYLPGVPYLP---------------------------NVRLASL-LNDEFDPLAKIEKIS-RPLLFIHGEK 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489183427 244 DLLTPTDLCLEAYQRALPPKRLLMLAG-GHFTPYIEHFDATSQAAADWFVRHL 295
Cdd:COG1073  201 DEAVPFYMSEDLYEAAAEPKELLIVPGaGHVDLYDRPEEEYFDKLAEFFKKNL 253
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
6-295 1.87e-67

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 210.93  E-value: 1.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   6 VEFRSE-GVALRGWLYLPEARAE-RPAIVMTHGFSGVKEQYLDrYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEIDPvmQ 83
Cdd:COG1073   13 VTFKSRdGIKLAGDLYLPAGASKkYPAVVVAHGNGGVKEQRAL-YAQRLAELGFNVLAFDYRGYGESEGEPREEGSP--E 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  84 RRGYRDAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVAQVPTVSghasalrrtraeqlpalLASFDADR 163
Cdd:COG1073   90 RRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS-----------------LEDLAAQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 164 QRRFEGlppALLPAVAAGPdepcamagadahrfftdsaalapswcnRVTLRSAeLARENEPGIHIGRISpTPLLMIVADR 243
Cdd:COG1073  153 AKEARG---AYLPGVPYLP---------------------------NVRLASL-LNDEFDPLAKIEKIS-RPLLFIHGEK 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489183427 244 DLLTPTDLCLEAYQRALPPKRLLMLAG-GHFTPYIEHFDATSQAAADWFVRHL 295
Cdd:COG1073  201 DEAVPFYMSEDLYEAAAEPKELLIVPGaGHVDLYDRPEEEYFDKLAEFFKKNL 253
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
29-280 8.54e-12

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: 64.06  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   29 PAIVMTHGFSGVKEQYlDRYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEidpVMQRRGYRDAITWLgaQARVDASRIGIW 108
Cdd:pfam00561   1 PPVLLLHGLPGSSDLW-RKLAPALARDGFRVIALDLRGFGKSSRPKAQD---DYRTDDLAEDLEYI--LEALGLEKVNLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  109 GTSYSGGHVLEVAAL-DRRVKCVVAQVPTVSGHA-SALRRTRAEQLPALLASFDADRQRRFEGLPPALLPAVAAGPDEPC 186
Cdd:pfam00561  75 GHSMGGLIALAYAAKyPDRVKALVLLGALDPPHElDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  187 AMAGADAHRFFTDSAALAPSWC-NRVTLRSAELARENEPGIHIGRIsptPLLMIVADRDLLTPTDLcLEAYQRALPPKRL 265
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVtGALLFIETWSTELRAKFLGRLDE---PTLIIWGDQDPLVPPQA-LEKLAQLFPNARL 230
                         250
                  ....*....|....*.
gi 489183427  266 LMLA-GGHFtPYIEHF 280
Cdd:pfam00561 231 VVIPdAGHF-AFLEGP 245
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
6-136 3.26e-05

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 45.18  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427    6 VEFRSeGVALRGWLYLPEARAERPAIVMTHGFSgvKEQYLDRYAEV-----FAAAGFVVLLYDHPNFGDSDGEpRQEIDP 80
Cdd:TIGR00976   1 VPMRD-GTRLAIDVYRPAGGGPVPVILSRTPYG--KDAGLRWGLDKtepawFVAQGYAVVIQDTRGRGASEGE-FDLLGS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489183427   81 VMQRRGYrDAITWLGAQARVDAsRIGIWGTSYSGGHVLEVAALDRR-VKCVVAQVPT 136
Cdd:TIGR00976  77 DEAADGY-DLVDWIAKQPWCDG-NVGMLGVSYLAVTQLLAAVLQPPaLRAIAPQEGV 131
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
7-72 8.79e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 40.51  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489183427   7 EFRSEGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRYAEVFAAAGFVVLLYDHPNFGDSDG 72
Cdd:PLN02385  66 EVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEG 131
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
6-295 1.87e-67

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 210.93  E-value: 1.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   6 VEFRSE-GVALRGWLYLPEARAE-RPAIVMTHGFSGVKEQYLDrYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEIDPvmQ 83
Cdd:COG1073   13 VTFKSRdGIKLAGDLYLPAGASKkYPAVVVAHGNGGVKEQRAL-YAQRLAELGFNVLAFDYRGYGESEGEPREEGSP--E 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  84 RRGYRDAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVAQVPTVSghasalrrtraeqlpalLASFDADR 163
Cdd:COG1073   90 RRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATDPRVKAVILDSPFTS-----------------LEDLAAQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 164 QRRFEGlppALLPAVAAGPdepcamagadahrfftdsaalapswcnRVTLRSAeLARENEPGIHIGRISpTPLLMIVADR 243
Cdd:COG1073  153 AKEARG---AYLPGVPYLP---------------------------NVRLASL-LNDEFDPLAKIEKIS-RPLLFIHGEK 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489183427 244 DLLTPTDLCLEAYQRALPPKRLLMLAG-GHFTPYIEHFDATSQAAADWFVRHL 295
Cdd:COG1073  201 DEAVPFYMSEDLYEAAAEPKELLIVPGaGHVDLYDRPEEEYFDKLAEFFKKNL 253
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
10-296 2.09e-31

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 117.04  E-value: 2.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  10 SEGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRYAEVFAAAGFVVLLYDHPNFGDSDGE-PRQEIDPVMqrrgyr 88
Cdd:COG1506    5 ADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDwGGDEVDDVL------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  89 DAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALD-RRVKCVVAQVPtVSGHASALRRTRaeqlpallasfdaDRQRRF 167
Cdd:COG1506   79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHpDRFKAAVALAG-VSDLRSYYGTTR-------------EYTERL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 168 EGLPPallpavaagpdepcamagadahrfftdsaalapswcnrvtlRSAELARENEPGIHIGRIsPTPLLMIVADRDLLT 247
Cdd:COG1506  145 MGGPW-----------------------------------------EDPEAYAARSPLAYADKL-KTPLLLIHGEADDRV 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489183427 248 PTDLCLEAYQRAL---PPKRLLMLAG-GHFTPYIEHFDATsQAAADWFVRHLG 296
Cdd:COG1506  183 PPEQAERLYEALKkagKPVELLVYPGeGHGFSGAGAPDYL-ERILDFLDRHLK 234
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
10-132 1.12e-20

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 88.48  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  10 SEGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRyAEVFAAAGFVVL---LYDHPNFGDSDGEPRQEIDPVMQRRG 86
Cdd:COG0412   11 PDGVTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDV-ARRLAAAGYVVLapdLYGRGGPGDDPDEARALMGALDPELL 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489183427  87 YRD---AITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVA 132
Cdd:COG0412   90 AADlraALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVS 138
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
6-165 3.65e-14

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 71.76  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   6 VEFRS-EGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRYAevFAAAGFVVLLYD---HPNFGDSDGEPRQEIDPV 81
Cdd:COG3458   59 VTFTGfGGARIYGWLLRPKGEGPLPAVVEFHGYGGGRGLPHEDLD--WAAAGYAVLVMDtrgQGSSWGDTPDPGGYSGGA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  82 ---MQRRG--------YRD-------AITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVAQVPTVSGHASA 143
Cdd:COG3458  137 lpgYMTRGiddpdtyyYRRvyldavrAVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAAADVPFLCDFRRA 216
                        170       180
                 ....*....|....*....|..
gi 489183427 144 LRRTRAEQLPALLASFDADRQR 165
Cdd:COG3458  217 LELGRAGPYPEIRRYLRRHRER 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-291 1.38e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.79  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   1 MQRLNVEFRS-EGVALRGWLYLPEARAeRPAIVMTHGFSGVKEQYlDRYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEID 79
Cdd:COG2267    1 MTRRLVTLPTrDGLRLRGRRWRPAGSP-RGTVVLVHGLGEHSGRY-AELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  80 PVMQRRGYRDAITWLGAQarvDASRIGIWGTSYSGGHVLEVAaldrrvkcvvaqvptvsghasalrrtraeqlpallasf 159
Cdd:COG2267   79 FDDYVDDLRAALDALRAR---PGLPVVLLGHSMGGLIALLYA-------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 160 dADRQRRFEGLppallpaVAAGPDEpcamagaDAHRFFTDSAALapswcnrvtLRSAELARenepgiHIGRISpTPLLMI 239
Cdd:COG2267  118 -ARYPDRVAGL-------VLLAPAY-------RADPLLGPSARW---------LRALRLAE------ALARID-VPVLVL 166
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489183427 240 VADRDLLTPTDLCLEAYQRALPPKRLLMLAGG-HFTPYIEHFDATSQAAADWF 291
Cdd:COG2267  167 HGGADRVVPPEAARRLAARLSPDVELVLLPGArHELLNEPAREEVLAAILAWL 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
29-280 8.54e-12

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: 64.06  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   29 PAIVMTHGFSGVKEQYlDRYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEidpVMQRRGYRDAITWLgaQARVDASRIGIW 108
Cdd:pfam00561   1 PPVLLLHGLPGSSDLW-RKLAPALARDGFRVIALDLRGFGKSSRPKAQD---DYRTDDLAEDLEYI--LEALGLEKVNLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  109 GTSYSGGHVLEVAAL-DRRVKCVVAQVPTVSGHA-SALRRTRAEQLPALLASFDADRQRRFEGLPPALLPAVAAGPDEPC 186
Cdd:pfam00561  75 GHSMGGLIALAYAAKyPDRVKALVLLGALDPPHElDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  187 AMAGADAHRFFTDSAALAPSWC-NRVTLRSAELARENEPGIHIGRIsptPLLMIVADRDLLTPTDLcLEAYQRALPPKRL 265
Cdd:pfam00561 155 KALPLLNKRFPSGDYALAKSLVtGALLFIETWSTELRAKFLGRLDE---PTLIIWGDQDPLVPPQA-LEKLAQLFPNARL 230
                         250
                  ....*....|....*.
gi 489183427  266 LMLA-GGHFtPYIEHF 280
Cdd:pfam00561 231 VVIPdAGHF-AFLEGP 245
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
12-162 1.37e-09

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 57.74  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   12 GVALRGWLYLPEARAER-PAIVM-------THGFSGVKEQYLDryaEVFAAAGFVVLLYDHPNFGDSDGEP----RQEID 79
Cdd:pfam02129   2 GVRLAADIYRPTKTGGPvPALLTrspygarRDGASDLALAHPE---WEFAARGYAVVYQDVRGTGGSEGVFtvggPQEAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   80 pvmqrrGYRDAITWLGAQarvDAS--RIGIWGTSYSGGHVLEVAAL-DRRVKCVVAQVPTVSGHASaLRRTRAEQLPALL 156
Cdd:pfam02129  79 ------DGKDVIDWLAGQ---PWCngKVGMTGISYLGTTQLAAAATgPPGLKAIAPESGISDLYDY-YREGGAVRAPGGL 148

                  ....*.
gi 489183427  157 ASFDAD 162
Cdd:pfam02129 149 GWEDLD 154
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
19-116 3.27e-08

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: 52.95  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   19 LYLPE-ARAERPAIVMTHG---FSGVKEQYLDRYAEV---FAAAGFVV------LLYDHPnFgdsdgePRQEIDpvmqrr 85
Cdd:pfam20434   3 IYLPKnAKGPYPVVIWIHGggwNSGDKEADMGFMTNTvkaLLKAGYAVasinyrLSTDAK-F------PAQIQD------ 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 489183427   86 gYRDAITWLGAQA---RVDASRIGIWGTSySGGH 116
Cdd:pfam20434  70 -VKAAIRFLRANAakyGIDTNKIALMGFS-AGGH 101
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
12-295 7.97e-08

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 53.39  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  12 GVALRGWLYLPEARAERPAIVMTH---GFSGVKEQYLDRYAEVFAAAGFVVLLYDHPNFGDSDGEP----RQEIDpvmqr 84
Cdd:COG2936   22 GVRLAADIYRPKDAEGPVPVILERtpyGKRDGTAGRDLGPHPYFAERGYAVVVQDVRGTGGSEGEFdpyrVDEQT----- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  85 rGYRDAITWLGAQARVDAsRIGIWGTSYSGGHVLEVAALD-RRVKCVVAQVPTVSGHASALRRTRAEQLPALL---ASFD 160
Cdd:COG2936   97 -DGYDTIDWLAKQPWSNG-KVGMIGISYGGFTQLAAAADRpPALKAIVPQAPTSDRYDDDHYHGGAFLLGFNLgwaATMG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 161 ADRQRRFEGLPPALLPAVAAGPDEPCAMAGADAHRFFTDSAALAPSWCNRVTlRSAELARENEPGiHIGRISPtPLLMIV 240
Cdd:COG2936  175 AYKERPPDPADARWRELLPDDYADRLEHLPLSDADALGEQLPFWEDWLAHPD-YDAFWQERSLLE-DLDRIKV-PVLAVG 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489183427 241 ADRDLLTPTDlcLEAYQ----RALPPKRLLMLAGGH----FTPYIEHFDATS----QAAADWFVRHL 295
Cdd:COG2936  252 GWYDVFLNGT--LRLYEalraPAGVPRKLVIGPWTHgpwaRGQLGPLFGATAidflQEALRWFDHWL 316
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
44-137 1.05e-06

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 48.38  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   44 YLDRYAEVFAAAGFVVLLydhPNFGDSDG---EPRQEIDPVMQRRGYRD---AITWLGAQARVDASRIGIWGTSYsGGHV 117
Cdd:pfam00326   2 SFSWNAQLLADRGYVVAI---ANGRGSGGygeAFHDAGKGDLGQNEFDDfiaAAEYLIEQGYTDPDRLAIWGGSY-GGYL 77
                          90       100
                  ....*....|....*....|..
gi 489183427  118 LEVAALDR--RVKCVVAQVPTV 137
Cdd:pfam00326  78 TGAALNQRpdLFKAAVAHVPVV 99
DLH pfam01738
Dienelactone hydrolase family;
16-132 1.41e-06

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 48.12  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   16 RGWLYLPeARAERPAIVMTHGFSGVKEQYLDrYAEVFAAAGFVVL---LYdhpnFGDSDGEPRQEIDPVMQR-------- 84
Cdd:pfam01738   1 DAYLATP-KNPPWPVVVVFQEIFGVNDNIRE-IADRLADEGYVALapdLY----FRQGDPNDEADAARAMFElvskrvme 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489183427   85 ---RGYRDAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVA 132
Cdd:pfam01738  75 kvlDDLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVG 125
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
2-274 4.15e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 47.41  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   2 QRLNVEFRSEGVALRGWLYLPE-------ARAERPAIVMTHGFSGVKEQYLDrYAEVFAAAGFVVLLYDHP--NFGDS-- 70
Cdd:COG4188   29 QTLTLRDPSRDRPLPVDVWYPAtapadapAGGPFPLVVLSHGLGGSREGYAY-LAEHLASHGYVVAAPDHPgsNAADLsa 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  71 --DGEPRQEIDPVMQRRgYRD---AITWLGA--------QARVDASRIGIWGTSYSGGHVLEVAAldrrvkcvvaqvptv 137
Cdd:COG4188  108 alDGLADALDPEELWER-PLDlsfVLDQLLAlnksdpplAGRLDLDRIGVIGHSLGGYTALALAG--------------- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 138 sghasalrrtraeqlpallASFDADRQRRFEGLPPALLPAVAAGPDEPcamagadahRFFTDS-----AALAPSwcNRVT 212
Cdd:COG4188  172 -------------------ARLDFAALRQYCGKNPDLQCRALDLPRLA---------YDLRDPrikavVALAPG--GSGL 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489183427 213 LRSAELArenepGIHIgrisptPLLMIVADRDLLTPTDLCLEAYQRALP--PKRLLMLAGG-HFT 274
Cdd:COG4188  222 FGEEGLA-----AITI------PVLLVAGSADDVTPAPDEQIRPFDLLPgaDKYLLTLEGAtHFS 275
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
17-138 1.55e-05

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 45.85  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427   17 GWLYLPEARAER-PAIVMTHGFSGVKEQYLDRYAevFAAAGFVVLLYD-HPNFGDSDGEPRQEIDP-------------- 80
Cdd:pfam05448  70 AWYVVPKESEEKhPAVVHFHGYNGRRGDWHDMLH--WAAHGYAVFVMDvRGQGGLSEDDPRGPKGNtykghitrglldre 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489183427   81 -VMQRRGYRDAITWLGAQA---RVDASRIGIWGTSYSGGHVLEVAALDRRVKCVVAQVPTVS 138
Cdd:pfam05448 148 tYYYRRVFLDAVRAVEIVMsfpEVDEERIVVTGGSQGGALALAAAALSPRIKAVVADYPFLS 209
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
6-136 3.26e-05

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 45.18  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427    6 VEFRSeGVALRGWLYLPEARAERPAIVMTHGFSgvKEQYLDRYAEV-----FAAAGFVVLLYDHPNFGDSDGEpRQEIDP 80
Cdd:TIGR00976   1 VPMRD-GTRLAIDVYRPAGGGPVPVILSRTPYG--KDAGLRWGLDKtepawFVAQGYAVVIQDTRGRGASEGE-FDLLGS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489183427   81 VMQRRGYrDAITWLGAQARVDAsRIGIWGTSYSGGHVLEVAALDRR-VKCVVAQVPT 136
Cdd:TIGR00976  77 DEAADGY-DLVDWIAKQPWCDG-NVGMLGVSYLAVTQLLAAVLQPPaLRAIAPQEGV 131
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
19-175 3.33e-05

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 44.09  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  19 LYLPEARAE-RPAIVMTHG---FSGVKEQYlDRYAEVFAA-AGFVVLL--------YDHPnfgdsdgEPRQEIdpvmqrr 85
Cdd:COG0657    3 VYRPAGAKGpLPVVVYFHGggwVSGSKDTH-DPLARRLAArAGAAVVSvdyrlapeHPFP-------AALEDA------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  86 gyRDAITWLGAQAR---VDASRIGIWGTSySGGH-VLEVAALDR-----RVKCVVAQVPTVSGHASALRrtraeqlpall 156
Cdd:COG0657   68 --YAALRWLRANAAelgIDPDRIAVAGDS-AGGHlAAALALRARdrggpRPAAQVLIYPVLDLTASPLR----------- 133
                        170
                 ....*....|....*....
gi 489183427 157 asfdadrqRRFEGLPPALL 175
Cdd:COG0657  134 --------ADLAGLPPTLI 144
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
23-294 5.99e-05

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: 43.45  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427  23 EARAERPAIVMTHGFSGVKEQYlDRYAEVFAAaGFVVLLYDHPNFGDSDGePRQEIDPVMQRRGYRDAITWLGAQarvda 102
Cdd:COG0596   18 EAGPDGPPVVLLHGLPGSSYEW-RPLIPALAA-GYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALGLE----- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 103 sRIGIWGTSYSGGHVLEVAALD-RRVKCVVAQvptvsghasalrrtrAEQLPALLASFDADRQRrfeglPPALLPAVAAG 181
Cdd:COG0596   90 -RVVLVGHSMGGMVALELAARHpERVAGLVLV---------------DEVLAALAEPLRRPGLA-----PEALAALLRAL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427 182 PDepcamagadahrffTDSAALAPSWcnrvtlrsaelarenepgihigrisPTPLLMIVADRDLLTPTDlCLEAYQRALP 261
Cdd:COG0596  149 AR--------------TDLRERLARI-------------------------TVPTLVIWGEKDPIVPPA-LARRLAELLP 188
                        250       260       270
                 ....*....|....*....|....*....|....
gi 489183427 262 PKRLLMLAG-GHFtPYIEHFDATSQAAADWFVRH 294
Cdd:COG0596  189 NAELVVLPGaGHF-PPLEQPEAFAAALRDFLARL 221
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
7-72 8.79e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 40.51  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489183427   7 EFRSEGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRYAEVFAAAGFVVLLYDHPNFGDSDG 72
Cdd:PLN02385  66 EVNSRGVEIFSKSWLPENSRPKAAVCFCHGYGDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEG 131
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
1-137 3.32e-03

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 38.70  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183427    1 MQRLNVEFrSEGVALRGWLYLPEARAERPAIVMTHGFSGVKEQYLDRYAEVFAAAGFVVLLYDHPNFGDSDGEPRQEIDP 80
Cdd:pfam06500 168 MKQLEFPY-QGGAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWKLTQDSS 246
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489183427   81 VMqrrgYRDAITWLGAQARVDASRIGIWGTSYSGGHVLEVAALD-RRVKCVVAQVPTV 137
Cdd:pfam06500 247 CL----HQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLEsPRVKAVACLGPPV 300
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
28-73 7.25e-03

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 37.19  E-value: 7.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489183427   28 RPAIVMTHGF---SGvkeqyldRYAEV---FAAAGFVVLLYDHPNFGDSDGE 73
Cdd:pfam12146   4 RAVVVLVHGLgehSG-------RYAHLadaLAAQGFAVYAYDHRGHGRSDGK 48
 
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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