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Conserved domains on  [gi|1052498132|gb|OCX54415|]
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lipase [Mucilaginibacter sp. PPCGB 2223]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

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
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 57-257 3.32e-103

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: 300.25  E-value: 3.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGWNKGRKEDQSGF-----SAFFKKGYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDH 131
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFmtntvKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 132 AAELNIDPNKIVIMGSSAGAHLALMGGLLANDHRFDTNC------PTNKIVKVAAIISQSGITDVWDWAH-GPHRTSKS- 203
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGNVgdytpeSSKESFKVNAVVDFYGPTDLLDMDScGTHNDAKSp 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1052498132 204 ATMWL-DKRADDQPFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKL 257
Cdd:pfam20434 161 ETLLLgAPPLENPDLAKSASPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
COG2945 super family cl43746
Alpha/beta superfamily hydrolase [General function prediction only];
233-295 1.89e-04

Alpha/beta superfamily hydrolase [General function prediction only];


The actual alignment was detected with superfamily member COG2945:

Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 41.69  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052498132 233 PTFVVHGDADPIVPYEqgvELYQKLQQMGVKSQFITVPGGGHgkFTNEKKTEIVTAYMAFLKD 295
Cdd:COG2945   144 PTLVIHGEQDEVVPPA---EVLDWARPLSPPLPVVVVPGADH--FFHGKLDELKELVARYLPR 201
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 57-257 3.32e-103

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: 300.25  E-value: 3.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGWNKGRKEDQSGF-----SAFFKKGYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDH 131
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFmtntvKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 132 AAELNIDPNKIVIMGSSAGAHLALMGGLLANDHRFDTNC------PTNKIVKVAAIISQSGITDVWDWAH-GPHRTSKS- 203
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGNVgdytpeSSKESFKVNAVVDFYGPTDLLDMDScGTHNDAKSp 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1052498132 204 ATMWL-DKRADDQPFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKL 257
Cdd:pfam20434 161 ETLLLgAPPLENPDLAKSASPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
57-296 1.05e-59

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 189.31  E-value: 1.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGWNKGRKEDQSGFSAFF--KKGYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDHAAE 134
Cdd:COG0657     1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLaaRAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 135 LNIDPNKIVIMGSSAGAHLALMGGLLANDHrfdtncptnKIVKVAAIISQSGITDVwdwahgphrtsksatmwldkradd 214
Cdd:COG0657    81 LGIDPDRIAVAGDSAGGHLAAALALRARDR---------GGPRPAAQVLIYPVLDL------------------------ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 215 qpfaqSVSPLTYVKKDSPPTFVVHGDADPIVpyEQGVELYQKLQQMGVKSQFITVPGGGHG---KFTNEKKTEIVTAYMA 291
Cdd:COG0657   128 -----TASPLRADLAGLPPTLIVTGEADPLV--DESEALAAALRAAGVPVELHVYPGGGHGfglLAGLPEARAALAEIAA 200


                  ....*
gi 1052498132 292 FLKDL 296
Cdd:COG0657   201 FLRRA 205
PRK10162 PRK10162
acetyl esterase;
75-275 1.79e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 60.50  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  75 IHGGGWNKGRKEDQSGFSAFFKK--GYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDHAAELNIDPNKIVIMGSSAGAH 152
Cdd:PRK10162   87 LHGGGFILGNLDTHDRIMRLLASysGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAM 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 153 LALMGGLLANDHRFDtncpTNKIVKVAAIISQSGITD---------VWDwahGPHRTSKSA--TMWLDKRAD-DQPFAQS 220
Cdd:PRK10162  167 LALASALWLRDKQID----CGKVAGVLLWYGLYGLRDsvsrrllggVWD---GLTQQDLQMyeEAYLSNDADrESPYYCL 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052498132 221 V-SPLTyvkKDSPPTFVVHGDADPIVpyEQGVELYQKLQQMGVKSQFITVPGGGHG 275
Cdd:PRK10162  240 FnNDLT---RDVPPCFIAGAEFDPLL--DDSRLLYQTLAAHQQPCEFKLYPGTLHA 290
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 59-151 1.38e-04

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 43.09  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  59 LYL------PSKDKGLSPIVINIHGGGWNKGrkedqSGfSAFFKKGYA-------VANVEYRL-----VQT----APAPA 116
Cdd:cd00312    79 LYLnvytpkNTKPGNSLPVMVWIHGGGFMFG-----SG-SLYPGDGLAregdnviVVSINYRLgvlgfLSTgdieLPGNY 152

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1052498132 117 AVQDIRCALIYIIDHAAELNIDPNKIVIMGSSAGA 151
Cdd:cd00312   153 GLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGG 187
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
233-295 1.89e-04

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 41.69  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052498132 233 PTFVVHGDADPIVPYEqgvELYQKLQQMGVKSQFITVPGGGHgkFTNEKKTEIVTAYMAFLKD 295
Cdd:COG2945   144 PTLVIHGEQDEVVPPA---EVLDWARPLSPPLPVVVVPGADH--FFHGKLDELKELVARYLPR 201
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
 57-245 3.62e-03

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: 37.85  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGwnkgrkedQSGFSAFFKKGYAVANVEYRLVQTAP-APAAVQDIRC------------ 123
Cdd:TIGR01840   1 MYVYVPAGLTGPRALVLALHGCG--------QTASAYVIDWGWKAAADRYGFVLVAPeQTSYNSSNNCwdwffthhrarg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 124 -----ALIYIIDH-AAELNIDPNKIVIMGSSAGAHLALMGGLLANDHrfdtncptnkivkVAAIISQSGitdvwdwahGP 197
Cdd:TIGR01840  73 tgeveSLHQLIDAvKANYSIDPNRVYVTGLSAGGGMTAVLGCTYPDV-------------FAGGASNAG---------LP 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052498132 198 HRTSKSATMWLDKRADDQPFAQ---SVSPLTYVKKDSPPTF-VVHGDADPIV 245
Cdd:TIGR01840 131 YGEASSSISATPQMCTAATAASvcrLVRGMQSEYNGPTPIMsVVHGDADYTV 182
 
Name Accession Description Interval E-value
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 57-257 3.32e-103

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: 300.25  E-value: 3.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGWNKGRKEDQSGF-----SAFFKKGYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDH 131
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFmtntvKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 132 AAELNIDPNKIVIMGSSAGAHLALMGGLLANDHRFDTNC------PTNKIVKVAAIISQSGITDVWDWAH-GPHRTSKS- 203
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGNVgdytpeSSKESFKVNAVVDFYGPTDLLDMDScGTHNDAKSp 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1052498132 204 ATMWL-DKRADDQPFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKL 257
Cdd:pfam20434 161 ETLLLgAPPLENPDLAKSASPITYVDKNDPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
57-296 1.05e-59

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 189.31  E-value: 1.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGWNKGRKEDQSGFSAFF--KKGYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDHAAE 134
Cdd:COG0657     1 MDVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLaaRAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 135 LNIDPNKIVIMGSSAGAHLALMGGLLANDHrfdtncptnKIVKVAAIISQSGITDVwdwahgphrtsksatmwldkradd 214
Cdd:COG0657    81 LGIDPDRIAVAGDSAGGHLAAALALRARDR---------GGPRPAAQVLIYPVLDL------------------------ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 215 qpfaqSVSPLTYVKKDSPPTFVVHGDADPIVpyEQGVELYQKLQQMGVKSQFITVPGGGHG---KFTNEKKTEIVTAYMA 291
Cdd:COG0657   128 -----TASPLRADLAGLPPTLIVTGEADPLV--DESEALAAALRAAGVPVELHVYPGGGHGfglLAGLPEARAALAEIAA 200


                  ....*
gi 1052498132 292 FLKDL 296
Cdd:COG0657   201 FLRRA 205
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
49-294 2.22e-38

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 135.14  E-value: 2.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  49 KVNGWdgrmdLYLPSKDKGLsPIVINIHGGGWNKgRKEDQSGFSAFFKKGYAVANVEYRLV---QTAPAPAAVQDIRCAL 125
Cdd:COG1506     9 TLPGW-----LYLPADGKKY-PVVVYVHGGPGSR-DDSFLPLAQALASRGYAVLAPDYRGYgesAGDWGGDEVDDVLAAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 126 IYIIDHAaelNIDPNKIVIMGSSAGAHLALMggLLANDHRFdtncptnkivkVAAIISQSGITDVWDWAHGphrTSKSAT 205
Cdd:COG1506    82 DYLAARP---YVDPDRIGIYGHSYGGYMALL--AAARHPDR-----------FKAAVALAGVSDLRSYYGT---TREYTE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 206 MWLDKRADDQPFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPGGGHGkFTNEKKTEI 285
Cdd:COG1506   143 RLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHG-FSGAGAPDY 221


                  ....*....
gi 1052498132 286 VTAYMAFLK 294
Cdd:COG1506   222 LERILDFLD 230
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 72-275 2.58e-26

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: 102.67  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  72 VINIHGGGWNKGrkedqSGFS--AFFKK-----GYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDHAAELNIDPNKIVI 144
Cdd:pfam07859   1 LVYFHGGGFVLG-----SADThdRLCRRlaaeaGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 145 MGSSAGAHLALMGGLLANDHrfdtncptnKIVKVAAII---------SQSGITDVWDWAHGPHRTSKS----ATMWLDKR 211
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDE---------GLPKPAGQVliypgtdlrTESPSYLAREFADGPLLTRAAmdwfWRLYLPGA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052498132 212 ADDQPFAqsvSPL-TYVKKDSPPTFVVHGDADPIVPyeQGVELYQKLQQMGVKSQFITVPGGGHG 275
Cdd:pfam07859 147 DRDDPLA---SPLfASDLSGLPPALVVVAEFDPLRD--EGEAYAERLRAAGVPVELIEYPGMPHG 206
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 44-295 5.00e-26

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 103.07  E-value: 5.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  44 DVVYSKVNGWDGRMDLYLPSKDKGLSPIVINIHGGGWNKgrkEDQSGFSAFF-KKGYAVANVEYR--------LVQTAPA 114
Cdd:COG1073    12 DVTFKSRDGIKLAGDLYLPAGASKKYPAVVVAHGNGGVK---EQRALYAQRLaELGFNVLAFDYRgygesegePREEGSP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 115 paAVQDIRCAliyiIDHAAEL-NIDPNKIVIMGSSAGAHLALMggLLANDHRfdtncptnkivkVAAIISQSGITDVWDW 193
Cdd:COG1073    89 --ERRDARAA----VDYLRTLpGVDPERIGLLGISLGGGYALN--AAATDPR------------VKAVILDSPFTSLEDL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 194 AHgpHRTSKSATM------WLDKRADDQPFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQQmgvKSQFI 267
Cdd:COG1073   149 AA--QRAKEARGAylpgvpYLPNVRLASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAE---PKELL 223

                         250       260
                  ....*....|....*....|....*...
gi 1052498132 268 TVPGGGHGKFTNEKKTEIVTAYMAFLKD 295
Cdd:COG1073   224 IVPGAGHVDLYDRPEEEYFDKLAEFFKK 251
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
129-275 2.86e-20

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 86.90  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 129 IDHAAELN-IDPNKIVIMGSSAGAHLALMgglLANDH--RFdtncptnkivkvAAIISQSGITDVwdwahgphRTSKSAT 205
Cdd:pfam00326  52 AEYLIEQGyTDPDRLAIWGGSYGGYLTGA---ALNQRpdLF------------KAAVAHVPVVDW--------LAYMSDT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 206 -MWLDKRADDQPFAQS-------VSPLTYV--KKDSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPGGGHG 275
Cdd:pfam00326 109 sLPFTERYMEWGNPWDneegydyLSPYSPAdnVKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGHG 188
COG4099 COG4099
Predicted peptidase [General function prediction only];
59-275 2.45e-12

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 65.37  E-value: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  59 LYLP-SKDKGLS-PIVINIHGGGW---------NKG-----RKEDQSGFSAFfkkgyaVANVEYRLVQTAPAPAAVQDIR 122
Cdd:COG4099    37 LYLPkGYDPGKKyPLVLFLHGAGErgtdnekqlTHGapkfiNPENQAKFPAI------VLAPQCPEDDYWSDTKALDAVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 123 CALIYIIdhaAELNIDPNKIVIMGSSAGAHLAL-MggLLANDHRFdtncptnkivkvAAIISQSGITDVWDWAhgphrts 201
Cdd:COG4099   111 ALLDDLI---AEYRIDPDRIYLTGLSMGGYGTWdL--AARYPDLF------------AAAVPICGGGDPANAA------- 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052498132 202 ksatmwldkraddqpfaqsvsPLTYVkkdspPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPGGGHG 275
Cdd:COG4099   167 ---------------------NLKKV-----PVWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHN 214
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
44-280 2.52e-12

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 64.99  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  44 DVVYSKVNGWDGRMDLYLPSKDKGLsPIVINIHGGGwnkGRKEDQSGFSAFF-KKGYAVANVEY--------------RL 108
Cdd:COG0412     5 TVTIPTPDGVTLPGYLARPAGGGPR-PGVVVLHEIF---GLNPHIRDVARRLaAAGYVVLAPDLygrggpgddpdearAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 109 VQTAPAPAAVQDIRCALiyiiDHAAEL-NIDPNKIVIMGSSAGAHLALMggLLANDHRfdtncptnkivkVAAIISQSGi 187
Cdd:COG0412    81 MGALDPELLAADLRAAL----DWLKAQpEVDAGRVGVVGFCFGGGLALL--AAARGPD------------LAAAVSFYG- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 188 tdvwdwahgphrtsksaTMWLDKRADDqpfaqsvspltyVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFI 267
Cdd:COG0412   142 -----------------GLPADDLLDL------------AARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELH 192

                         250
                  ....*....|...
gi 1052498132 268 TVPGGGHGkFTNE 280
Cdd:COG0412   193 VYPGAGHG-FTNP 204
PRK10162 PRK10162
acetyl esterase;
75-275 1.79e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 60.50  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  75 IHGGGWNKGRKEDQSGFSAFFKK--GYAVANVEYRLVQTAPAPAAVQDIRCALIYIIDHAAELNIDPNKIVIMGSSAGAH 152
Cdd:PRK10162   87 LHGGGFILGNLDTHDRIMRLLASysGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAM 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 153 LALMGGLLANDHRFDtncpTNKIVKVAAIISQSGITD---------VWDwahGPHRTSKSA--TMWLDKRAD-DQPFAQS 220
Cdd:PRK10162  167 LALASALWLRDKQID----CGKVAGVLLWYGLYGLRDsvsrrllggVWD---GLTQQDLQMyeEAYLSNDADrESPYYCL 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052498132 221 V-SPLTyvkKDSPPTFVVHGDADPIVpyEQGVELYQKLQQMGVKSQFITVPGGGHG 275
Cdd:PRK10162  240 FnNDLT---RDVPPCFIAGAEFDPLL--DDSRLLYQTLAAHQQPCEFKLYPGTLHA 290
YpfH COG0400
Predicted esterase [General function prediction only];
124-275 2.87e-10

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 58.77  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 124 ALIYIIDHA-AELNIDPNKIVIMGSSAGAHLALmGGLLANDHRFDtncptnkivKVAAIisqsgitdvwdwahgphrtsk 202
Cdd:COG0400    72 ALAAFIDELeARYGIDPERIVLAGFSQGAAMAL-SLALRRPELLA---------GVVAL--------------------- 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052498132 203 SATMWLDKRADDQPFAQSvspltyvkkdSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPgGGHG 275
Cdd:COG0400   121 SGYLPGEEALPAPEAALA----------GTPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYP-GGHE 182
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 50-275 5.11e-10

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 59.25  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  50 VNGWDGRMDLYLPS---KDKGLsPIVINIHGGGWNKGRKEDQSGFSAFF-KKGYAVA-------------NVEYRLVQTA 112
Cdd:COG3509    32 VGGGTRTYRLYVPAgydGGAPL-PLVVALHGCGGSAADFAAGTGLNALAdREGFIVVypegtgrapgrcwNWFDGRDQRR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 113 PA--PAAVQDIrcaliyiIDH-AAELNIDPNKIVIMGSSAGAHLALmggLLANDH--RFdtncptnkivkvAAIisqsgi 187
Cdd:COG3509   111 GRddVAFIAAL-------VDDlAARYGIDPKRVYVTGLSAGGAMAY---RLACEYpdVF------------AAV------ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 188 tdvwdwahGPHrtskSATMWLDKRADDQPFAQSVspltyvkkdspPTFVVHGDADPIVPYEQGVELyqkLQQM------- 260
Cdd:COG3509   163 --------APV----AGLPYGAASDAACAPGRPV-----------PVLVIHGTADPTVPYAGAEET---LAQWaalngca 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1052498132 261 ------------------------GVKSQFITVPGGGHG 275
Cdd:COG3509   217 atptrtevtdgggytrtrysdcagGAEVELYTVEGGGHA 255
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
58-282 7.18e-10

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 58.97  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  58 DLYLPSKDKGLS------PIVINIHGGGwnkGRKEDQSGFSAFF-KKGYAVANVEY---RLVQTAPAPAAVQDIRCA--- 124
Cdd:COG4188    45 DVWYPATAPADApaggpfPLVVLSHGLG---GSREGYAYLAEHLaSHGYVVAAPDHpgsNAADLSAALDGLADALDPeel 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 125 ------LIYIIDHAAELN---------IDPNKIVIMGSSAGAH--LALMGGLLaNDHRFDTNCPTNKIVKVAAIisqsgi 187
Cdd:COG4188   122 werpldLSFVLDQLLALNksdpplagrLDLDRIGVIGHSLGGYtaLALAGARL-DFAALRQYCGKNPDLQCRAL------ 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 188 tdvwdwahGPHRTSKSATmwlDKR-----ADDQPFAQSVSPLTYvKKDSPPTFVVHGDADPIVPYEQGVE-LYQKLQqmG 261
Cdd:COG4188   195 --------DLPRLAYDLR---DPRikavvALAPGGSGLFGEEGL-AAITIPVLLVAGSADDVTPAPDEQIrPFDLLP--G 260

                         250       260
                  ....*....|....*....|.
gi 1052498132 262 VKSQFITVPGGGHGKFTNEKK 282
Cdd:COG4188   261 ADKYLLTLEGATHFSFLDPCT 281
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
70-295 7.78e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 57.70  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  70 PIVInIHGGGWNKGRkedqsgFS----AFFKKGYAVANVEYR--------LVQTAPAPAAVQDIRCAliyiIDHAAELNI 137
Cdd:COG2267    30 TVVL-VHGLGEHSGR------YAelaeALAAAGYAVLAFDLRghgrsdgpRGHVDSFDDYVDDLRAA----LDALRARPG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 138 DPnkIVIMGSSAGAHLALmggLLANDHRfdtncptnkiVKVAAIISQSGitdvwDWAHGPHRTSkSATMWLDKRADDQPF 217
Cdd:COG2267    99 LP--VVLLGHSMGGLIAL---LYAARYP----------DRVAGLVLLAP-----AYRADPLLGP-SARWLRALRLAEALA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052498132 218 AQSVspltyvkkdspPTFVVHGDADPIVPYEQGVELYQKLQQmgvKSQFITVPGGGHGkFTNEKKTEIVTAYM-AFLKD 295
Cdd:COG2267   158 RIDV-----------PVLVLHGGADRVVPPEAARRLAARLSP---DVELVLLPGARHE-LLNEPAREEVLAAIlAWLER 221
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 70-296 5.23e-09

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: 55.39  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  70 PIVInIHGGGwnkGRKEDQSGFSAFFKKGYAVANVEYR---LVQTAPAPAAVQDIRCALIYIIDHaaeLNIDPnkIVIMG 146
Cdd:COG0596    25 PVVL-LHGLP---GSSYEWRPLIPALAAGYRVIAPDLRghgRSDKPAGGYTLDDLADDLAALLDA---LGLER--VVLVG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 147 SSAGAHLALmggLLANDHrfdtncPTnkivKVAAIISQSGITD-VWDWAHGPHRTSKSATMWLDKRADDQPFAQsvsplt 225
Cdd:COG0596    96 HSMGGMVAL---ELAARH------PE----RVAGLVLVDEVLAaLAEPLRRPGLAPEALAALLRALARTDLRER------ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052498132 226 yVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQQmgvkSQFITVPGGGHGkFTNEKKTEIVTAYMAFLKDL 296
Cdd:COG0596   157 -LARITVPTLVIWGEKDPIVPPALARRLAELLPN----AELVVLPGAGHF-PPLEQPEAFAAALRDFLARL 221
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
140-296 1.88e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 51.10  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 140 NKIVIMGSSAGAHLALmggLLANDHRfdtncptnkivKVAAIISQSGITDVWDWAHGPHRTSKSATMWLDKRADD----- 214
Cdd:COG1647    84 DKVIVIGLSMGGLLAL---LLAARYP-----------DVAGLVLLSPALKIDDPSAPLLPLLKYLARSLRGIGSDiedpe 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 215 -QPFAQSVSPL----------TYVKKDSP----PTFVVHGDADPIVPYEQGVELYQKLQqmGVKSQFITVPGGGHGkFTN 279
Cdd:COG1647   150 vAEYAYDRTPLralaelqrliREVRRDLPkitaPTLIIQSRKDEVVPPESARYIYERLG--SPDKELVWLEDSGHV-ITL 226

                         170
                  ....*....|....*...
gi 1052498132 280 EKKTEIVTAYM-AFLKDL 296
Cdd:COG1647   227 DKDREEVAEEIlDFLERL 244
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 71-274 6.47e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 49.01  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  71 IVInIHGGGwnkgrkEDQSGFSAFFKKGYAVANVEYRLV-QTAPAPAAVQDIRCaliyIIDHAAELnIDPNKIVIMGSSA 149
Cdd:pfam12697   1 VVL-VHGAG------LSAAPLAALLAAGVAVLAPDLPGHgSSSPPPLDLADLAD----LAALLDEL-GAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 150 GAHLALMGGLLANDHRFDTNCPTNKIVKVAAIISQ------SGITDVWDWAHGP----HRTSKSATMWLDKRADDQPFAQ 219
Cdd:pfam12697  69 GGAVALAAAAAALVVGVLVAPLAAPPGLLAALLALlarlgaALAAPAWLAAESLargfLDDLPADAEWAAALARLAALLA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052498132 220 SVSPLTYVK-KDSPPTFVVHGDADPIVPyeqgvELYQKLQQMGVKSQFITVPGGGH 274
Cdd:pfam12697 149 ALALLPLAAwRDLPVPVLVLAEEDRLVP-----ELAQRLLAALAGARLVVLPGAGH 199
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 125-274 1.89e-06

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 47.76  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 125 LIYIIDHAAELNIDPNKIVIMGSSAGAHLALMGGLlandhrfdtNCPTnkivKVAAIISQSGitdvwdwahgphrtsksa 204
Cdd:pfam02230  90 IEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSAL---------TLPL----PLGGIVAFSG------------------ 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 205 tmWLDKRaddQPFAQSVSPLTyvkkDSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPGGGH 274
Cdd:pfam02230 139 --FLPLP---TKFPSHPNLVT----KKTPIFLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAH 199
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
58-275 2.51e-06

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 47.72  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  58 DLYLPSKDKGLSPIVINI---HGGGWNKGRKEDQSGFSAFFKKGYAVANVEYR------------LVQTAPAPAAVqdir 122
Cdd:pfam02129   8 DIYRPTKTGGPVPALLTRspyGARRDGASDLALAHPEWEFAARGYAVVYQDVRgtggsegvftvgGPQEAADGKDV---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 123 caliyiIDHAAELNIDPNKIVIMGSSAGAHLALMggLLANDHRfdtncptnkivKVAAIISQSGITDVWDWA--HGPHRt 200
Cdd:pfam02129  84 ------IDWLAGQPWCNGKVGMTGISYLGTTQLA--AAATGPP-----------GLKAIAPESGISDLYDYYreGGAVR- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 201 SKSATMWLD---------------------------------KRADDQ--------------PFAQSVSPLTYVKKDSPP 233
Cdd:pfam02129 144 APGGLGWEDldllaealtsrraddgdayraaaryeaagdellAELDRQlfllewllqtgdydAFWQDRNYLEDADKVKAP 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1052498132 234 TFVVHGDADPIVPyEQGVELYQKLQQMGVKSQFITVPgGGHG 275
Cdd:pfam02129 224 VLLVGGWQDWNVK-NGAIKLYEALRAPGVKKKLILGP-WTHV 263
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
 216-275 3.86e-06

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 44.64  E-value: 3.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 216 PFAQSVSPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQqmgvKSQFITVPGGGHG 275
Cdd:pfam08386  18 PVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALG----GAVLVTVQGAGHG 73
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
46-272 2.11e-05

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 45.23  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  46 VYSKVNGWDGRMDLYLP---SKDKGLSPIVINIHGGGwnkgrkEDQSGFSAFFKKGYAVAN------------------- 103
Cdd:COG2382    86 YPSKALGRTRRVWVYLPpgyDNPGKKYPVLYLLDGGG------GDEQDWFDQGRLPTILDNliaagkippmivvmpdggd 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 104 VEYRLVQTAPAPAAVQDIRCALI-YIidhAAELNI--DPNKIVIMGSSAGAHLALMGGLlandHRFDTncptnkivkVAA 180
Cdd:COG2382   160 GGDRGTEGPGNDAFERFLAEELIpFV---EKNYRVsaDPEHRAIAGLSMGGLAALYAAL----RHPDL---------FGY 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 181 IISQSGitdvwdwahgphrtsksATMWLDKRADDqpfaqsVSPLTYVKKDSPPT----FVVHGDADPIvpYEQGVELYQK 256
Cdd:COG2382   224 VGSFSG-----------------SFWWPPGDADR------GGWAELLAAGAPKKplrfYLDVGTEDDL--LEANRALAAA 278

                         250
                  ....*....|....*.
gi 1052498132 257 LQQMGVKSQFITVPGG 272
Cdd:COG2382   279 LKAKGYDVEYREFPGG 294
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 59-151 1.38e-04

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 43.09  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  59 LYL------PSKDKGLSPIVINIHGGGWNKGrkedqSGfSAFFKKGYA-------VANVEYRL-----VQT----APAPA 116
Cdd:cd00312    79 LYLnvytpkNTKPGNSLPVMVWIHGGGFMFG-----SG-SLYPGDGLAregdnviVVSINYRLgvlgfLSTgdieLPGNY 152

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1052498132 117 AVQDIRCALIYIIDHAAELNIDPNKIVIMGSSAGA 151
Cdd:cd00312   153 GLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGG 187
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
233-295 1.89e-04

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 41.69  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052498132 233 PTFVVHGDADPIVPYEqgvELYQKLQQMGVKSQFITVPGGGHgkFTNEKKTEIVTAYMAFLKD 295
Cdd:COG2945   144 PTLVIHGEQDEVVPPA---EVLDWARPLSPPLPVVVVPGADH--FFHGKLDELKELVARYLPR 201
COesterase pfam00135
Carboxylesterase family;
59-151 6.39e-04

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 41.14  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  59 LYL-------PSKDKGLSPIVINIHGGG--WNKGRKEDQSGFSAffKKGYAVANVEYRL-----VQT----APAPAAVQD 120
Cdd:pfam00135  86 LYLnvytpkeLKENKNKLPVMVWIHGGGfmFGSGSLYDGSYLAA--EGDVIVVTINYRLgplgfLSTgddeAPGNYGLLD 163

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1052498132 121 IRCALIYIIDHAAELNIDPNKIVIMGSSAGA 151
Cdd:pfam00135 164 QVLALRWVQENIASFGGDPNRVTLFGESAGA 194
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 71-156 1.72e-03

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


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 39.40  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  71 IVINIHGGGWNKGRKEDQSGFSAFFKKGYAVANVE------YRLVqtapapaaVQDIRCAliyiIDHAAEL-NIDPNKIV 143
Cdd:COG3458   112 LVMDTRGQGSSWGDTPDPGGYSGGALPGYMTRGIDdpdtyyYRRV--------YLDAVRA----VDALRSLpEVDGKRIG 179

                          90
                  ....*....|...
gi 1052498132 144 IMGSSAGAHLALM 156
Cdd:COG3458   180 VTGGSQGGGLALA 192
DLH pfam01738
Dienelactone hydrolase family;
222-281 2.95e-03

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 38.10  E-value: 2.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 222 SPLTYVKKDSPPTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQFITVPGGGHGkFTNEK 281
Cdd:pfam01738 133 PPLIEAPDIKAPILFHFGEEDHFVPADSRELIEEALKAANVDHQIHSYPGAGHA-FANDS 191
esterase_phb TIGR01840
esterase, PHB depolymerase family; This model describes a subfamily among lipases of the ...
 57-245 3.62e-03

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: 37.85  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132  57 MDLYLPSKDKGLSPIVINIHGGGwnkgrkedQSGFSAFFKKGYAVANVEYRLVQTAP-APAAVQDIRC------------ 123
Cdd:TIGR01840   1 MYVYVPAGLTGPRALVLALHGCG--------QTASAYVIDWGWKAAADRYGFVLVAPeQTSYNSSNNCwdwffthhrarg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052498132 124 -----ALIYIIDH-AAELNIDPNKIVIMGSSAGAHLALMGGLLANDHrfdtncptnkivkVAAIISQSGitdvwdwahGP 197
Cdd:TIGR01840  73 tgeveSLHQLIDAvKANYSIDPNRVYVTGLSAGGGMTAVLGCTYPDV-------------FAGGASNAG---------LP 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052498132 198 HRTSKSATMWLDKRADDQPFAQ---SVSPLTYVKKDSPPTF-VVHGDADPIV 245
Cdd:TIGR01840 131 YGEASSSISATPQMCTAATAASvcrLVRGMQSEYNGPTPIMsVVHGDADYTV 182
PRK10566 PRK10566
esterase; Provisional
 233-274 7.10e-03

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 37.28  E-value: 7.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1052498132 233 PTFVVHGDADPIVPYEQGVELYQKLQQMGVKSQ--FITVPGGGH 274
Cdd:PRK10566  188 PLLLWHGLADDVVPAAESLRLQQALRERGLDKNltCLWEPGVRH 231
 
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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