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Conserved domains on  [gi|219983728|emb|CAX06853|]
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unnamed protein product [Arabidopsis thaliana]

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
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
144-394 6.23e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 131.15  E-value: 6.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 144 DLYLPSNNDGLKPVVVFVTGGAWIIGYKAWGSLLGMQLAE-RDIIVACLDYRNFPQGTISDMVTDASQGISFVCNNISAF 222
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 223 GGDPNRIYLMGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegee 302
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDRGG---------PRPAAQVLIYPVLDL------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 303 sfeKFSPE-VRLKDpvvgkaaslLPPIILFHGSSDysIPCDESKTFTDALQAVGAKAELVLYSGKTHTdlFLQDPLRGGK 381
Cdd:COG0657  128 ---TASPLrADLAG---------LPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHG--FGLLAGLPEA 191

                        250
                 ....*....|...
gi 219983728 382 DELFDDIVSVIHA 394
Cdd:COG0657  192 RAALAEIAAFLRR 204
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
144-394 6.23e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 131.15  E-value: 6.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 144 DLYLPSNNDGLKPVVVFVTGGAWIIGYKAWGSLLGMQLAE-RDIIVACLDYRNFPQGTISDMVTDASQGISFVCNNISAF 222
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 223 GGDPNRIYLMGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegee 302
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDRGG---------PRPAAQVLIYPVLDL------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 303 sfeKFSPE-VRLKDpvvgkaaslLPPIILFHGSSDysIPCDESKTFTDALQAVGAKAELVLYSGKTHTdlFLQDPLRGGK 381
Cdd:COG0657  128 ---TASPLrADLAG---------LPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHG--FGLLAGLPEA 191

                        250
                 ....*....|...
gi 219983728 382 DELFDDIVSVIHA 394
Cdd:COG0657  192 RAALAEIAAFLRR 204
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 143-351 2.34e-30

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: 116.51  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  143 LDLYLPSNNDGLKPVVVFVTGGAWIIGYKA----WGSLLGMQLAERDIIVACLDYRNFPQGTISDMVTDASQGISFVCNN 218
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEadmgFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  219 ISAFGGDPNRIYLMGQSAGAHIAACALLEQATKELKGEsiswtvsqIKAYFGLSGGYNL-YKLV-DHFhnrGLyrSIFLS 296
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGN--------VGDYTPESSKESFkVNAVvDFY---GP--TDLLD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219983728  297 IMEGEESFEKFSPEVRL------KDPVVGKAASLL-------PPIILFHGSSDYSIPCDESKTFTDAL 351
Cdd:pfam20434 148 MDSCGTHNDAKSPETLLlgapplENPDLAKSASPItyvdkndPPFLIIHGDKDPLVPYCQSVLLHEKL 215
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 143-253 9.10e-11

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: 63.51  E-value: 9.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 143 LDLYLP--SNNDGLKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYRNFPQGTISDMVTDAS-------Q 210
Cdd:cd00312   81 LNVYTPknTKPGNSLPVMVWIHGGGFMFGS---GSLYpgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPgnyglkdQ 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 219983728 211 --GISFVCNNISAFGGDPNRIYLMGQSAGAHIAACALLEQATKEL 253
Cdd:cd00312  158 rlALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGL 202
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
144-394 6.23e-36

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 131.15  E-value: 6.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 144 DLYLPSNNDGLKPVVVFVTGGAWIIGYKAWGSLLGMQLAE-RDIIVACLDYRNFPQGTISDMVTDASQGISFVCNNISAF 222
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 223 GGDPNRIYLMGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegee 302
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDRGG---------PRPAAQVLIYPVLDL------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 303 sfeKFSPE-VRLKDpvvgkaaslLPPIILFHGSSDysIPCDESKTFTDALQAVGAKAELVLYSGKTHTdlFLQDPLRGGK 381
Cdd:COG0657  128 ---TASPLrADLAG---------LPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHG--FGLLAGLPEA 191

                        250
                 ....*....|...
gi 219983728 382 DELFDDIVSVIHA 394
Cdd:COG0657  192 RAALAEIAAFLRR 204
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 143-351 2.34e-30

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: 116.51  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  143 LDLYLPSNNDGLKPVVVFVTGGAWIIGYKA----WGSLLGMQLAERDIIVACLDYRNFPQGTISDMVTDASQGISFVCNN 218
Cdd:pfam20434   1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEadmgFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  219 ISAFGGDPNRIYLMGQSAGAHIAACALLEQATKELKGEsiswtvsqIKAYFGLSGGYNL-YKLV-DHFhnrGLyrSIFLS 296
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGN--------VGDYTPESSKESFkVNAVvDFY---GP--TDLLD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219983728  297 IMEGEESFEKFSPEVRL------KDPVVGKAASLL-------PPIILFHGSSDYSIPCDESKTFTDAL 351
Cdd:pfam20434 148 MDSCGTHNDAKSPETLLlgapplENPDLAKSASPItyvdkndPPFLIIHGDKDPLVPYCQSVLLHEKL 215
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
145-376 2.83e-20

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 89.31  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 145 LYLPSNNdGLKPVVVFVTGGAWIIgYKAWgSLLGMQLAERDIIVACLDYRNFPQGT---ISDMVTDASQGISFVcnnISA 221
Cdd:COG1506   14 LYLPADG-KKYPVVVYVHGGPGSR-DDSF-LPLAQALASRGYAVLAPDYRGYGESAgdwGGDEVDDVLAAIDYL---AAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 222 FGGDPNRIYLMGQSAGAHIAACALLEQAtkelkgesiswtvSQIKAYFGLSGGYNLYKLVDHFhnRGLYRSIFLSIMEGE 301
Cdd:COG1506   88 PYVDPDRIGIYGHSYGGYMALLAAARHP-------------DRFKAAVALAGVSDLRSYYGTT--REYTERLMGGPWEDP 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219983728 302 ESFEKFSPevrlkdpvVGKAASLLPPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSGKTHTDLFLQDP 376
Cdd:COG1506  153 EAYAARSP--------LAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAP 219
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 144-394 1.05e-19

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 88.05  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 144 DLYLPSNNDGLKPVVVFVTGGAwiiGYKAWGSLLGMQLAERDIIVACLDYRNFPQ--GTISDMVT----DASQGISFVcn 217
Cdd:COG1073   26 DLYLPAGASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFDYRGYGEseGEPREEGSperrDARAAVDYL-- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 218 nISAFGGDPNRIYLMGQSAGAHIAACALLEQatkelkgesiswtvSQIKAYFGLSGGYNLYKLVDHF--HNRGLYRSIFl 295
Cdd:COG1073  101 -RTLPGVDPERIGLLGISLGGGYALNAAATD--------------PRVKAVILDSPFTSLEDLAAQRakEARGAYLPGV- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 296 simegeesfeKFSPEVRLKD------PVVGKAASLLPPIILFHGSSDYSIPCDESKtftDALQAVGAKAELVLYSGKTHT 369
Cdd:COG1073  165 ----------PYLPNVRLASllndefDPLAKIEKISRPLLFIHGEKDEAVPFYMSE---DLYEAAAEPKELLIVPGAGHV 231

                        250       260
                 ....*....|....*....|....*
gi 219983728 370 DLFLQDPlrggkDELFDDIVSVIHA 394
Cdd:COG1073  232 DLYDRPE-----EEYFDKLAEFFKK 251
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 158-368 9.17e-16

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: 75.71  E-value: 9.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  158 VVFVTGGAWIIGYKAWGSLLGMQLAER-DIIVACLDYR-----NFPQGtisdmVTDASQGISFVCNNISAFGGDPNRIYL 231
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEaGAVVVSVDYRlapehPFPAA-----YDDAYAALRWLAEQAAELGADPSRIAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  232 MGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLYKLVDHFHNRGLYRSIFLSIMEGEESFEKFSPEV 311
Cdd:pfam07859  76 AGDSAGGNLAAAVALRARDEGL---------PKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219983728  312 RLKDPVV--GKAASL--LPPIILFHGSSDYSIpcDESKTFTDALQAVGAKAELVLYSGKTH 368
Cdd:pfam07859 147 DRDDPLAspLFASDLsgLPPALVVVAEFDPLR--DEGEAYAERLRAAGVPVELIEYPGMPH 205
COesterase pfam00135
Carboxylesterase family;
142-246 1.14e-12

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 69.64  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  142 RLDLYLP---SNNDGLKPVVVFVTGGAWIIGYkawGSLL-GMQLAER-DIIVACLDYR----------------NFPqgt 200
Cdd:pfam00135  87 YLNVYTPkelKENKNKLPVMVWIHGGGFMFGS---GSLYdGSYLAAEgDVIVVTINYRlgplgflstgddeapgNYG--- 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 219983728  201 ISDMVtdasQGISFVCNNISAFGGDPNRIYLMGQSAGAhIAACALL 246
Cdd:pfam00135 161 LLDQV----LALRWVQENIASFGGDPNRVTLFGESAGA-ASVSLLL 201
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
145-246 1.93e-12

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 68.76  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 145 LYL----PSNNDG-LKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYR-------NFPQgtisdmVTDAS 209
Cdd:COG2272   90 LYLnvwtPALAAGaKLPVMVWIHGGGFVSGS---GSEPlydGAALARRGVVVVTINYRlgalgflALPA------LSGES 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 219983728 210 QGIS-------------FVCNNISAFGGDPNRIYLMGQSAGAhIAACALL 246
Cdd:COG2272  161 YGASgnyglldqiaalrWVRDNIAAFGGDPDNVTIFGESAGA-ASVAALL 209
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 143-253 9.10e-11

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: 63.51  E-value: 9.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 143 LDLYLP--SNNDGLKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYRNFPQGTISDMVTDAS-------Q 210
Cdd:cd00312   81 LNVYTPknTKPGNSLPVMVWIHGGGFMFGS---GSLYpgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPgnyglkdQ 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 219983728 211 --GISFVCNNISAFGGDPNRIYLMGQSAGAHIAACALLEQATKEL 253
Cdd:cd00312  158 rlALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGL 202
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
155-394 7.41e-10

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 58.86  E-value: 7.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 155 KPVVVFVTGGAWIIGYkaWGSLLGmQLAERDIIVACLDYRNF-----PQG---TISDMVTDASQGISFvcnnISAFGGDP 226
Cdd:COG2267   28 RGTVVLVHGLGEHSGR--YAELAE-ALAAAGYAVLAFDLRGHgrsdgPRGhvdSFDDYVDDLRAALDA----LRARPGLP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 227 nrIYLMGQSAGAHIAACALLEQATKelkgesiswtvsqIKAYFGLSGGYNLYKLVdhFHNRGLYRSIFLsimegeesfek 306
Cdd:COG2267  101 --VVLLGHSMGGLIALLYAARYPDR-------------VAGLVLLAPAYRADPLL--GPSARWLRALRL----------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 307 fspevrlkdpvVGKAASLLPPIILFHGSSDYSIPCDESKTFTDALqavGAKAELVLYSGKTHtdLFLQDPLRggkDELFD 386
Cdd:COG2267  153 -----------AEALARIDVPVLVLHGGADRVVPPEAARRLAARL---SPDVELVLLPGARH--ELLNEPAR---EEVLA 213


                 ....*...
gi 219983728 387 DIVSVIHA 394
Cdd:COG2267  214 AILAWLER 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
99-368 7.45e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 53.05  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  99 MTKLLALtcyaMLLMPGFLQVAYSY--FFSKQVRRSIVYGdqprnrldLYLPSNNDGLK--PVVVFVTGGAW----IIGY 170
Cdd:COG4099    1 MKKLLLL----LLLLGCAAQDGFEArtFTDPSDGDTLPYR--------LYLPKGYDPGKkyPLVLFLHGAGErgtdNEKQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 171 KAWGSLLGMQLAERD----IIVA--CLDYRNFPQGTISDMVTDAsqgISFVcnnISAFGGDPNRIYLMGQSAGAHIAACA 244
Cdd:COG4099   69 LTHGAPKFINPENQAkfpaIVLApqCPEDDYWSDTKALDAVLAL---LDDL---IAEYRIDPDRIYLTGLSMGGYGTWDL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 245 LLEQATKelkgesiswtvsqIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegeesfekfspevrlkdPVVGKAASL 324
Cdd:COG4099  143 AARYPDL-------------FAAAVPICGGGDP--------------------------------------ANAANLKKV 171

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 219983728 325 lpPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSGKTH 368
Cdd:COG4099  172 --PVWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGH 213
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 155-368 1.20e-04

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: 43.36  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  155 KPVVVFVTGGAWIIG-YkawgSLLGMQLAERDIIVACLDYRNF-----PQGTI---SDMVTDASQGISFVCNNisaFGGD 225
Cdd:pfam12146   4 RAVVVLVHGLGEHSGrY----AHLADALAAQGFAVYAYDHRGHgrsdgKRGHVpsfDDYVDDLDTFVDKIREE---HPGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  226 PnrIYLMGQSAGAHIAACALLEQATKeLKG-------------------ESISWTVSQIKAYFGLSGGYNLYKLVDHFHN 286
Cdd:pfam12146  77 P--LFLLGHSMGGLIAALYALRYPDK-VDGlilsapalkikpylappilKLLAKLLGKLFPRLRVPNNLLPDSLSRDPEV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  287 RGLYRS-----------IFLSIMEGEESFEKFSPEVRLkdpvvgkaasllpPIILFHGSSDYSIPCDESKTFTDALQAVG 355
Cdd:pfam12146 154 VAAYAAdplvhggisarTLYELLDAGERLLRRAAAITV-------------PLLLLHGGADRVVDPAGSREFYERAGSTD 220

                         250
                  ....*....|...
gi 219983728  356 akAELVLYSGKTH 368
Cdd:pfam12146 221 --KTLKLYPGLYH 231
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
181-368 6.83e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 40.68  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  181 LAERDIIVACLDYR---------------NFPQGTISDMVTdasqGISFVcnnISAFGGDPNRIYLMGQSAGAHIAACAL 245
Cdd:pfam00326  10 LADRGYVVAIANGRgsggygeafhdagkgDLGQNEFDDFIA----AAEYL---IEQGYTDPDRLAIWGGSYGGYLTGAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  246 lEQATKELKG-----------ESISWTVSQIKAYFGLSG-------GYNLYKLVDHFHNRGLYrsiflsimegeesfekf 307
Cdd:pfam00326  83 -NQRPDLFKAavahvpvvdwlAYMSDTSLPFTERYMEWGnpwdneeGYDYLSPYSPADNVKVY----------------- 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219983728  308 spevrlkdpvvgkaasllPPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSGKTH 368
Cdd:pfam00326 145 ------------------PPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLLIFPDEGH 187
DLH pfam01738
Dienelactone hydrolase family;
303-368 9.75e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 40.41  E-value: 9.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219983728  303 SFEKFSPEVRLKDPVVGKAasllpPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSGKTH 368
Cdd:pfam01738 125 GFYGVGPEPPLIEAPDIKA-----PILFHFGEEDHFVPADSRELIEEALKAANVDHQIHSYPGAGH 185
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
315-368 1.27e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 219983728 315 DPVVGKAASLLPPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSGKTH 368
Cdd:COG0412  146 DDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGH 199
YpfH COG0400
Predicted esterase [General function prediction only];
221-365 1.27e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 221 AFGGDPNRIYLMGQSAGAHIAACALLEQATKelkgesiswtvsqIKAYFGLSGGYNlyklvdhfhnrglyrsiflsimeg 300
Cdd:COG0400   83 RYGIDPERIVLAGFSQGAAMALSLALRRPEL-------------LAGVVALSGYLP------------------------ 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219983728 301 eesfekfsPEVRLKDPvvgKAASLLPPIILFHGSSDYSIPCDESKTFTDALQAVGAKAELVLYSG 365
Cdd:COG0400  126 --------GEEALPAP---EAALAGTPVFLAHGTQDPVIPVERAREAAEALEAAGADVTYREYPG 179
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 97-245 5.94e-03

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.45  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728  97 RWMTKLLALTCyAMLLMPGFlqvaysyffSKQVRRSIVYGDQPRNR-LDLYLPSNNDGLKPV-VVFV------TGGAWII 168
Cdd:COG3509    2 RRLRRLAALAA-LLALLPAA---------AAAGDFERTFTVGGGTRtYRLYVPAGYDGGAPLpLVVAlhgcggSAADFAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219983728 169 GYkawgsllGM-QLAERD-IIVACLD-YRNFPQGT------------------ISDMVTDAsqgisfvcnnISAFGGDPN 227
Cdd:COG3509   72 GT-------GLnALADREgFIVVYPEgTGRAPGRCwnwfdgrdqrrgrddvafIAALVDDL----------AARYGIDPK 134

                        170       180
                 ....*....|....*....|.
gi 219983728 228 RIYLMGQSAG---AHIAACAL 245
Cdd:COG3509  135 RVYVTGLSAGgamAYRLACEY 155
 
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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