|
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 20259181 144 DLYLPSNNDGLKPVVVFVTGGAWIIGYKAWGSLLGMQLAE-RDIIVACLDYRNFPQGTISDMVTDASQGISFVCNNISAF 222
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 223 GGDPNRIYLMGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegee 302
Cdd:COG0657 82 GIDPDRIAVAGDSAGGHLAAALALRARDRGG---------PRPAAQVLIYPVLDL------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 303 sfeKFSPE-VRLKDpvvgkaaslLPPIILFHGSSDysIPCDESKTFTDALQAVGAKAELVLYSGKTHTdlFLQDPLRGGK 381
Cdd:COG0657 128 ---TASPLrADLAG---------LPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHG--FGLLAGLPEA 191
|
250
....*....|...
gi 20259181 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 20259181 143 LDLYLPSNNDGLKPVVVFVTGGAWIIGYKA----WGSLLGMQLAERDIIVACLDYRNFPQGTISDMVTDASQGISFVCNN 218
Cdd:pfam20434 1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEadmgFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 219 ISAFGGDPNRIYLMGQSAGAHIAACALLEQATKELKGEsiswtvsqIKAYFGLSGGYNL-YKLV-DHFhnrGLyrSIFLS 296
Cdd:pfam20434 81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGN--------VGDYTPESSKESFkVNAVvDFY---GP--TDLLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20259181 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 20259181 143 LDLYLP--SNNDGLKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYRNFPQGTISDMVTDAS-------Q 210
Cdd:cd00312 81 LNVYTPknTKPGNSLPVMVWIHGGGFMFGS---GSLYpgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPgnyglkdQ 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 20259181 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 20259181 144 DLYLPSNNDGLKPVVVFVTGGAWIIGYKAWGSLLGMQLAE-RDIIVACLDYRNFPQGTISDMVTDASQGISFVCNNISAF 222
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAArAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 223 GGDPNRIYLMGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegee 302
Cdd:COG0657 82 GIDPDRIAVAGDSAGGHLAAALALRARDRGG---------PRPAAQVLIYPVLDL------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 303 sfeKFSPE-VRLKDpvvgkaaslLPPIILFHGSSDysIPCDESKTFTDALQAVGAKAELVLYSGKTHTdlFLQDPLRGGK 381
Cdd:COG0657 128 ---TASPLrADLAG---------LPPTLIVTGEAD--PLVDESEALAAALRAAGVPVELHVYPGGGHG--FGLLAGLPEA 191
|
250
....*....|...
gi 20259181 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 20259181 143 LDLYLPSNNDGLKPVVVFVTGGAWIIGYKA----WGSLLGMQLAERDIIVACLDYRNFPQGTISDMVTDASQGISFVCNN 218
Cdd:pfam20434 1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDKEadmgFMTNTVKALLKAGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 219 ISAFGGDPNRIYLMGQSAGAHIAACALLEQATKELKGEsiswtvsqIKAYFGLSGGYNL-YKLV-DHFhnrGLyrSIFLS 296
Cdd:pfam20434 81 AAKYGIDTNKIALMGFSAGGHLALLAGLSNNNKEFEGN--------VGDYTPESSKESFkVNAVvDFY---GP--TDLLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20259181 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 20259181 145 LYLPSNNdGLKPVVVFVTGGAWIIgYKAWgSLLGMQLAERDIIVACLDYRNFPQGT---ISDMVTDASQGISFVcnnISA 221
Cdd:COG1506 14 LYLPADG-KKYPVVVYVHGGPGSR-DDSF-LPLAQALASRGYAVLAPDYRGYGESAgdwGGDEVDDVLAAIDYL---AAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 222 FGGDPNRIYLMGQSAGAHIAACALLEQAtkelkgesiswtvSQIKAYFGLSGGYNLYKLVDHFhnRGLYRSIFLSIMEGE 301
Cdd:COG1506 88 PYVDPDRIGIYGHSYGGYMALLAAARHP-------------DRFKAAVALAGVSDLRSYYGTT--REYTERLMGGPWEDP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20259181 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 20259181 144 DLYLPSNNDGLKPVVVFVTGGAwiiGYKAWGSLLGMQLAERDIIVACLDYRNFPQ--GTISDMVT----DASQGISFVcn 217
Cdd:COG1073 26 DLYLPAGASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFDYRGYGEseGEPREEGSperrDARAAVDYL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 218 nISAFGGDPNRIYLMGQSAGAHIAACALLEQatkelkgesiswtvSQIKAYFGLSGGYNLYKLVDHF--HNRGLYRSIFl 295
Cdd:COG1073 101 -RTLPGVDPERIGLLGISLGGGYALNAAATD--------------PRVKAVILDSPFTSLEDLAAQRakEARGAYLPGV- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 296 simegeesfeKFSPEVRLKD------PVVGKAASLLPPIILFHGSSDYSIPCDESKtftDALQAVGAKAELVLYSGKTHT 369
Cdd:COG1073 165 ----------PYLPNVRLASllndefDPLAKIEKISRPLLFIHGEKDEAVPFYMSE---DLYEAAAEPKELLIVPGAGHV 231
|
250 260
....*....|....*....|....*
gi 20259181 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 20259181 158 VVFVTGGAWIIGYKAWGSLLGMQLAER-DIIVACLDYR-----NFPQGtisdmVTDASQGISFVCNNISAFGGDPNRIYL 231
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEaGAVVVSVDYRlapehPFPAA-----YDDAYAALRWLAEQAAELGADPSRIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 232 MGQSAGAHIAACALLEQATKELkgesiswtvSQIKAYFGLSGGYNLYKLVDHFHNRGLYRSIFLSIMEGEESFEKFSPEV 311
Cdd:pfam07859 76 AGDSAGGNLAAAVALRARDEGL---------PKPAGQVLIYPGTDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20259181 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 20259181 142 RLDLYLP---SNNDGLKPVVVFVTGGAWIIGYkawGSLL-GMQLAER-DIIVACLDYR----------------NFPqgt 200
Cdd:pfam00135 87 YLNVYTPkelKENKNKLPVMVWIHGGGFMFGS---GSLYdGSYLAAEgDVIVVTINYRlgplgflstgddeapgNYG--- 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 20259181 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 20259181 145 LYL----PSNNDG-LKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYR-------NFPQgtisdmVTDAS 209
Cdd:COG2272 90 LYLnvwtPALAAGaKLPVMVWIHGGGFVSGS---GSEPlydGAALARRGVVVVTINYRlgalgflALPA------LSGES 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 20259181 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 20259181 143 LDLYLP--SNNDGLKPVVVFVTGGAWIIGYkawGSLL---GMQLAERDIIVACLDYRNFPQGTISDMVTDAS-------Q 210
Cdd:cd00312 81 LNVYTPknTKPGNSLPVMVWIHGGGFMFGS---GSLYpgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPgnyglkdQ 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 20259181 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 20259181 155 KPVVVFVTGGAWIIGYkaWGSLLGmQLAERDIIVACLDYRNF-----PQG---TISDMVTDASQGISFvcnnISAFGGDP 226
Cdd:COG2267 28 RGTVVLVHGLGEHSGR--YAELAE-ALAAAGYAVLAFDLRGHgrsdgPRGhvdSFDDYVDDLRAALDA----LRARPGLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 227 nrIYLMGQSAGAHIAACALLEQATKelkgesiswtvsqIKAYFGLSGGYNLYKLVdhFHNRGLYRSIFLsimegeesfek 306
Cdd:COG2267 101 --VVLLGHSMGGLIALLYAARYPDR-------------VAGLVLLAPAYRADPLL--GPSARWLRALRL----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 307 fspevrlkdpvVGKAASLLPPIILFHGSSDYSIPCDESKTFTDALqavGAKAELVLYSGKTHtdLFLQDPLRggkDELFD 386
Cdd:COG2267 153 -----------AEALARIDVPVLVLHGGADRVVPPEAARRLAARL---SPDVELVLLPGARH--ELLNEPAR---EEVLA 213
|
....*...
gi 20259181 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 20259181 99 MTKLLALtcyaMLLMPGFLQVAYSY--FFSKQVRRSIVYGdqprnrldLYLPSNNDGLK--PVVVFVTGGAW----IIGY 170
Cdd:COG4099 1 MKKLLLL----LLLLGCAAQDGFEArtFTDPSDGDTLPYR--------LYLPKGYDPGKkyPLVLFLHGAGErgtdNEKQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 171 KAWGSLLGMQLAERD----IIVA--CLDYRNFPQGTISDMVTDAsqgISFVcnnISAFGGDPNRIYLMGQSAGAHIAACA 244
Cdd:COG4099 69 LTHGAPKFINPENQAkfpaIVLApqCPEDDYWSDTKALDAVLAL---LDDL---IAEYRIDPDRIYLTGLSMGGYGTWDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 245 LLEQATKelkgesiswtvsqIKAYFGLSGGYNLyklvdhfhnrglyrsiflsimegeesfekfspevrlkdPVVGKAASL 324
Cdd:COG4099 143 AARYPDL-------------FAAAVPICGGGDP--------------------------------------ANAANLKKV 171
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 20259181 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 20259181 155 KPVVVFVTGGAWIIG-YkawgSLLGMQLAERDIIVACLDYRNF-----PQGTI---SDMVTDASQGISFVCNNisaFGGD 225
Cdd:pfam12146 4 RAVVVLVHGLGEHSGrY----AHLADALAAQGFAVYAYDHRGHgrsdgKRGHVpsfDDYVDDLDTFVDKIREE---HPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 226 PnrIYLMGQSAGAHIAACALLEQATKeLKG-------------------ESISWTVSQIKAYFGLSGGYNLYKLVDHFHN 286
Cdd:pfam12146 77 P--LFLLGHSMGGLIAALYALRYPDK-VDGlilsapalkikpylappilKLLAKLLGKLFPRLRVPNNLLPDSLSRDPEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 287 RGLYRS-----------IFLSIMEGEESFEKFSPEVRLkdpvvgkaasllpPIILFHGSSDYSIPCDESKTFTDALQAVG 355
Cdd:pfam12146 154 VAAYAAdplvhggisarTLYELLDAGERLLRRAAAITV-------------PLLLLHGGADRVVDPAGSREFYERAGSTD 220
|
250
....*....|...
gi 20259181 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 20259181 181 LAERDIIVACLDYR---------------NFPQGTISDMVTdasqGISFVcnnISAFGGDPNRIYLMGQSAGAHIAACAL 245
Cdd:pfam00326 10 LADRGYVVAIANGRgsggygeafhdagkgDLGQNEFDDFIA----AAEYL---IEQGYTDPDRLAIWGGSYGGYLTGAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 246 lEQATKELKG-----------ESISWTVSQIKAYFGLSG-------GYNLYKLVDHFHNRGLYrsiflsimegeesfekf 307
Cdd:pfam00326 83 -NQRPDLFKAavahvpvvdwlAYMSDTSLPFTERYMEWGnpwdneeGYDYLSPYSPADNVKVY----------------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20259181 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 20259181 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 20259181 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 20259181 221 AFGGDPNRIYLMGQSAGAHIAACALLEQATKelkgesiswtvsqIKAYFGLSGGYNlyklvdhfhnrglyrsiflsimeg 300
Cdd:COG0400 83 RYGIDPERIVLAGFSQGAAMALSLALRRPEL-------------LAGVVALSGYLP------------------------ 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20259181 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 20259181 97 RWMTKLLALTCyAMLLMPGFlqvaysyffSKQVRRSIVYGDQPRNR-LDLYLPSNNDGLKPV-VVFV------TGGAWII 168
Cdd:COG3509 2 RRLRRLAALAA-LLALLPAA---------AAAGDFERTFTVGGGTRtYRLYVPAGYDGGAPLpLVVAlhgcggSAADFAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259181 169 GYkawgsllGM-QLAERD-IIVACLD-YRNFPQGT------------------ISDMVTDAsqgisfvcnnISAFGGDPN 227
Cdd:COG3509 72 GT-------GLnALADREgFIVVYPEgTGRAPGRCwnwfdgrdqrrgrddvafIAALVDDL----------AARYGIDPK 134
|
170 180
....*....|....*....|.
gi 20259181 228 RIYLMGQSAG---AHIAACAL 245
Cdd:COG3509 135 RVYVTGLSAGgamAYRLACEY 155
|
|
| |
