|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
22-542 |
3.58e-147 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 433.66 E-value: 3.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 22 PKVTTPYGPIVGFEHKSTVTGSkYHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI--PSLRSELEEQVN 99
Cdd:pfam00135 3 PVVTTSLGRVRGKRLKVDGGKP-VYAFLGIPYAEPPVGELRFQPPEPPEPWTGV-RDATKFGPRCPqnGDLTSPGSSGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 100 YSEDCLFLNIVTPPDAKE--KKLPVLVFIHGGGFQFGDTSMIGYQKAADNFvskDIIFVSIQYRLGPLGFFTTGDSEIPG 177
Cdd:pfam00135 81 GSEDCLYLNVYTPKELKEnkNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEG---DVIVVTINYRLGPLGFLSTGDDEAPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 178 NMGLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRNVVDDSRKL 257
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 258 AKAAGCPQEDSKELRDCIEIRTVDELLDAMESIGELLPGPRTkKFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVSLE 335
Cdd:pfam00135 238 AKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYGSVPFV-PFGPVVDGDFLPEHPEELlkSGNFPKVPLLIGVTKDE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 336 SGLSVLYpvkLAKLLGVPKESWSTYSKDNLVDFIRSQVAVEQEFGTASARFsglveeFYLSGPMTGNSSFYLNAFANLLS 415
Cdd:pfam00135 317 GLLFAAY---ILDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALRE------EYLDWGDRDDPETSRRALVELLT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 416 DLQYNIPTLHEVELKLQHGWDTYLYIIDYDSETTKDPthPIKGPFHASELRYLFNFNGMDTIPFNDKDKKFENYFVNAIV 495
Cdd:pfam00135 388 DYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSLRYP--KWVGVDHGDELPYVFGTPFVGALLFTEEDEKLSRKMMTYWT 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17562340 496 NFINTGTPSTKALL--WPAVS-KSQPFanLLLNDKPSVQTSFRQEAYELW 542
Cdd:pfam00135 466 NFAKTGNPNGPEGLpkWPPYTdENGQY--LSIDLEPRVKQGLKAERCAFW 513
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
22-544 |
3.48e-107 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 330.70 E-value: 3.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 22 PKVTTPYGPIVGFEHKSTvtgskyHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI-PSLRSELEEQVNY 100
Cdd:COG2272 13 PVVRTEAGRVRGVVEGGV------RVFLGIPYAAPPVGELRWRAPQPVEPWTGV-RDATEFGPACPqPPRPGDPGGPAPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 101 SEDCLFLNIVTPPDAKEKKLPVLVFIHGGGFQFGDTSMIGYQkaADNFVSKDIIFVSIQYRLGPLGFF-----TTGDSEI 175
Cdd:COG2272 86 SEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGSGSEPLYD--GAALARRGVVVVTINYRLGALGFLalpalSGESYGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 176 PGNMGLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRnVVDDSR 255
Cdd:COG2272 164 SGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAE-AEAVGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 256 KLAKAAGCPQEDSKELRDcieiRTVDELLDAMESIGELLPGPRTkkFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVS 333
Cdd:COG2272 243 AFAAALGVAPATLAALRA----LPAEELLAAQAALAAEGPGGLP--FGPVVDGDVLPEDPLEAfaAGRAADVPLLIGTNR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 334 LEsglsvlypvklAKLLGVPKESWSTYSKDNLVDFIRsqvaveQEFGTASARfsgLVEEFYLSGPmtgnssfyLNAFANL 413
Cdd:COG2272 317 DE-----------GRLFAALLGDLGPLTAADYRAALR------RRFGDDADE---VLAAYPAASP--------AEALAAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 414 LSDLQYNIPTLHEVELKLQHGWDTYLYIIDYDSETTKDPTHpikGPFHASELRYLF-NFNGMDTIPFNDKDKKFENYFVN 492
Cdd:COG2272 369 ATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGL---GAFHGAELPFVFgNLDAPALTGLTPADRALSDQMQA 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17562340 493 AIVNFINTGTPSTKAL-LWPAVSKSQPfANLLLNDKPSVQTSFRQEA-YELWQS 544
Cdd:COG2272 446 YWVNFARTGDPNGPGLpEWPAYDPEDR-AVMVFDAEPRVVNDPDAEErLDLWDG 498
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
24-518 |
6.51e-102 |
|
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: 316.97 E-value: 6.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 24 VTTPYGPIVGfehkstVTGSKYHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI---PSLRSELEEQVNY 100
Cdd:cd00312 2 VVTPNGKVRG------VDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDV-LDATSYPPSCMqwdQLGGGLWNAKLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 101 SEDCLFLNIVTPPDAKE-KKLPVLVFIHGGGFQFGDTSMIGYQKAADNfvSKDIIFVSIQYRLGPLGFFTTGDSEIPGNM 179
Cdd:cd00312 75 SEDCLYLNVYTPKNTKPgNSLPVMVWIHGGGFMFGSGSLYPGDGLARE--GDNVIVVSINYRLGVLGFLSTGDIELPGNY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 180 GLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRNVVDDSRKLAK 259
Cdd:cd00312 153 GLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 260 AAGCPQEDSKELRDCIEIRTVDELLDAMES-IGELLPGPRTkkFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVSLES 336
Cdd:cd00312 233 LLGCNDTSSAELLDCLRSKSAEELLDATRKlLLFSYSPFLP--FGPVVDGDFIPDDPEELikEGKFAKVPLIIGVTKDEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 337 GLSVLY-PVKLAKLLGVPKESWSTYSKdnlvdfirsqvaveQEFGTASARFSGLVEEFYLSGPMTGNSSFylNAFANLLS 415
Cdd:cd00312 311 GYFAAMlLNFDAKLIIETNDRWLELLP--------------YLLFYADDALADKVLEKYPGDVDDSVESR--KNLSDMLT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 416 DLQYNIPTLHEVELKLQHGW-DTYLYIIDYDSETTKDPTHPIKGPFHASELRYLFNFNGMDTiPFNDKDKKFENYFVNAI 494
Cdd:cd00312 375 DLLFKCPARYFLAQHRKAGGsPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLKE-GLREEEEKLSRTMMKYW 453
|
490 500
....*....|....*....|....*.
gi 17562340 495 VNFINTGTPSTKALL--WPAVSKSQP 518
Cdd:cd00312 454 ANFAKTGNPNTEGNLvvWPAYTSESE 479
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
122-214 |
1.88e-05 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 47.02 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 122 VLVFIHGGGFQFG--DT------SMIGYQKAAdnfvskdiiFVSIQYRLGPLGFFTTGDSEIpgnmglwdqTLALQFLHE 193
Cdd:PRK10162 83 TLFYLHGGGFILGnlDThdrimrLLASYSGCT---------VIGIDYTLSPEARFPQAIEEI---------VAVCCYFHQ 144
|
90 100
....*....|....*....|.
gi 17562340 194 VLPDFGGDPDRITLAGHSAGA 214
Cdd:PRK10162 145 HAEDYGINMSRIGFAGDSAGA 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COesterase |
pfam00135 |
Carboxylesterase family; |
22-542 |
3.58e-147 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 433.66 E-value: 3.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 22 PKVTTPYGPIVGFEHKSTVTGSkYHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI--PSLRSELEEQVN 99
Cdd:pfam00135 3 PVVTTSLGRVRGKRLKVDGGKP-VYAFLGIPYAEPPVGELRFQPPEPPEPWTGV-RDATKFGPRCPqnGDLTSPGSSGLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 100 YSEDCLFLNIVTPPDAKE--KKLPVLVFIHGGGFQFGDTSMIGYQKAADNFvskDIIFVSIQYRLGPLGFFTTGDSEIPG 177
Cdd:pfam00135 81 GSEDCLYLNVYTPKELKEnkNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEG---DVIVVTINYRLGPLGFLSTGDDEAPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 178 NMGLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRNVVDDSRKL 257
Cdd:pfam00135 158 NYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 258 AKAAGCPQEDSKELRDCIEIRTVDELLDAMESIGELLPGPRTkKFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVSLE 335
Cdd:pfam00135 238 AKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYGSVPFV-PFGPVVDGDFLPEHPEELlkSGNFPKVPLLIGVTKDE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 336 SGLSVLYpvkLAKLLGVPKESWSTYSKDNLVDFIRSQVAVEQEFGTASARFsglveeFYLSGPMTGNSSFYLNAFANLLS 415
Cdd:pfam00135 317 GLLFAAY---ILDNVDILKALEEKLLRSLLIDLLYLLLVDLPEEISAALRE------EYLDWGDRDDPETSRRALVELLT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 416 DLQYNIPTLHEVELKLQHGWDTYLYIIDYDSETTKDPthPIKGPFHASELRYLFNFNGMDTIPFNDKDKKFENYFVNAIV 495
Cdd:pfam00135 388 DYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSLRYP--KWVGVDHGDELPYVFGTPFVGALLFTEEDEKLSRKMMTYWT 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17562340 496 NFINTGTPSTKALL--WPAVS-KSQPFanLLLNDKPSVQTSFRQEAYELW 542
Cdd:pfam00135 466 NFAKTGNPNGPEGLpkWPPYTdENGQY--LSIDLEPRVKQGLKAERCAFW 513
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
22-544 |
3.48e-107 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 330.70 E-value: 3.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 22 PKVTTPYGPIVGFEHKSTvtgskyHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI-PSLRSELEEQVNY 100
Cdd:COG2272 13 PVVRTEAGRVRGVVEGGV------RVFLGIPYAAPPVGELRWRAPQPVEPWTGV-RDATEFGPACPqPPRPGDPGGPAPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 101 SEDCLFLNIVTPPDAKEKKLPVLVFIHGGGFQFGDTSMIGYQkaADNFVSKDIIFVSIQYRLGPLGFF-----TTGDSEI 175
Cdd:COG2272 86 SEDCLYLNVWTPALAAGAKLPVMVWIHGGGFVSGSGSEPLYD--GAALARRGVVVVTINYRLGALGFLalpalSGESYGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 176 PGNMGLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRnVVDDSR 255
Cdd:COG2272 164 SGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAE-AEAVGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 256 KLAKAAGCPQEDSKELRDcieiRTVDELLDAMESIGELLPGPRTkkFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVS 333
Cdd:COG2272 243 AFAAALGVAPATLAALRA----LPAEELLAAQAALAAEGPGGLP--FGPVVDGDVLPEDPLEAfaAGRAADVPLLIGTNR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 334 LEsglsvlypvklAKLLGVPKESWSTYSKDNLVDFIRsqvaveQEFGTASARfsgLVEEFYLSGPmtgnssfyLNAFANL 413
Cdd:COG2272 317 DE-----------GRLFAALLGDLGPLTAADYRAALR------RRFGDDADE---VLAAYPAASP--------AEALAAL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 414 LSDLQYNIPTLHEVELKLQHGWDTYLYIIDYDSETTKDPTHpikGPFHASELRYLF-NFNGMDTIPFNDKDKKFENYFVN 492
Cdd:COG2272 369 ATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGL---GAFHGAELPFVFgNLDAPALTGLTPADRALSDQMQA 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17562340 493 AIVNFINTGTPSTKAL-LWPAVSKSQPfANLLLNDKPSVQTSFRQEA-YELWQS 544
Cdd:COG2272 446 YWVNFARTGDPNGPGLpEWPAYDPEDR-AVMVFDAEPRVVNDPDAEErLDLWDG 498
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
24-518 |
6.51e-102 |
|
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: 316.97 E-value: 6.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 24 VTTPYGPIVGfehkstVTGSKYHVFLGIRYGNPPDHIYRFQKPEPVEKWPHInHDATHFRASCI---PSLRSELEEQVNY 100
Cdd:cd00312 2 VVTPNGKVRG------VDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDV-LDATSYPPSCMqwdQLGGGLWNAKLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 101 SEDCLFLNIVTPPDAKE-KKLPVLVFIHGGGFQFGDTSMIGYQKAADNfvSKDIIFVSIQYRLGPLGFFTTGDSEIPGNM 179
Cdd:cd00312 75 SEDCLYLNVYTPKNTKPgNSLPVMVWIHGGGFMFGSGSLYPGDGLARE--GDNVIVVSINYRLGVLGFLSTGDIELPGNY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 180 GLWDQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALLYSPHSDHLFSQAIQLSGSIFSESNLDRNVVDDSRKLAK 259
Cdd:cd00312 153 GLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 260 AAGCPQEDSKELRDCIEIRTVDELLDAMES-IGELLPGPRTkkFHPYFDKDFFPYDIEKM--SRKAPKKRTMQGLVSLES 336
Cdd:cd00312 233 LLGCNDTSSAELLDCLRSKSAEELLDATRKlLLFSYSPFLP--FGPVVDGDFIPDDPEELikEGKFAKVPLIIGVTKDEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 337 GLSVLY-PVKLAKLLGVPKESWSTYSKdnlvdfirsqvaveQEFGTASARFSGLVEEFYLSGPMTGNSSFylNAFANLLS 415
Cdd:cd00312 311 GYFAAMlLNFDAKLIIETNDRWLELLP--------------YLLFYADDALADKVLEKYPGDVDDSVESR--KNLSDMLT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 416 DLQYNIPTLHEVELKLQHGW-DTYLYIIDYDSETTKDPTHPIKGPFHASELRYLFNFNGMDTiPFNDKDKKFENYFVNAI 494
Cdd:cd00312 375 DLLFKCPARYFLAQHRKAGGsPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLKE-GLREEEEKLSRTMMKYW 453
|
490 500
....*....|....*....|....*.
gi 17562340 495 VNFINTGTPSTKALL--WPAVSKSQP 518
Cdd:cd00312 454 ANFAKTGNPNTEGNLvvWPAYTSESE 479
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
109-264 |
4.40e-19 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 109 IVTPPDAKEKkLPVLVFIHGGGFQFGDTSMigYQKAADNFVS-KDIIFVSIQYRLGPlgffttgdsEIPgnmglWDQTL- 186
Cdd:COG0657 3 VYRPAGAKGP-LPVVVYFHGGGWVSGSKDT--HDPLARRLAArAGAAVVSVDYRLAP---------EHP-----FPAALe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 187 ----ALQFLHEVLPDFGGDPDRITLAGHSAGA--ASVSALLYSPHSDHLFSQAIQLSGSI-FSESNLDRNV--------- 250
Cdd:COG0657 66 dayaALRWLRANAAELGIDPDRIAVAGDSAGGhlAAALALRARDRGGPRPAAQVLIYPVLdLTASPLRADLaglpptliv 145
|
170 180
....*....|....*....|....
gi 17562340 251 -------VDDSRKLA---KAAGCP 264
Cdd:COG0657 146 tgeadplVDESEALAaalRAAGVP 169
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
109-273 |
1.27e-11 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 64.65 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 109 IVTPPDAKekKLPVLVFIHGGGFqfgdTSMIGYQKAADNFVSKDIIFVSIQYRlgplGFfttGDSEipGNMG---LWDQT 185
Cdd:COG1506 14 LYLPADGK--KYPVVVYVHGGPG----SRDDSFLPLAQALASRGYAVLAPDYR----GY---GESA--GDWGgdeVDDVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 186 LALQFLHEvLPDFggDPDRITLAGHSAGAASVSALLysPHSDHLFSQAIQLSGSifseSNLDRNVVDDSRKLAKAAGCPQ 265
Cdd:COG1506 79 AAIDYLAA-RPYV--DPDRIGIYGHSYGGYMALLAA--ARHPDRFKAAVALAGV----SDLRSYYGTTREYTERLMGGPW 149
|
....*...
gi 17562340 266 EDSKELRD 273
Cdd:COG1506 150 EDPEAYAA 157
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
107-221 |
2.69e-09 |
|
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: 57.58 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 107 LNIVTPPDAKeKKLPVLVFIHGGGFQFGD-TSMIGYQKAADN-FVSKDIIFVSIQYRLgplgfftTGDSEIPGNMGlwDQ 184
Cdd:pfam20434 1 LDIYLPKNAK-GPYPVVIWIHGGGWNSGDkEADMGFMTNTVKaLLKAGYAVASINYRL-------STDAKFPAQIQ--DV 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 17562340 185 TLALQFLHEVLPDFGGDPDRITLAGHSAGA--ASVSALL 221
Cdd:pfam20434 71 KAAIRFLRANAAKYGIDTNKIALMGFSAGGhlALLAGLS 109
|
|
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
123-221 |
3.85e-09 |
|
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: 56.84 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 123 LVFIHGGGFQFGDTSMigyqkaADNFVSK-----DIIFVSIQYRLGPlgffttgDSEIPGNMglwDQTL-ALQFLHEVLP 196
Cdd:pfam07859 1 LVYFHGGGFVLGSADT------HDRLCRRlaaeaGAVVVSVDYRLAP-------EHPFPAAY---DDAYaALRWLAEQAA 64
|
90 100
....*....|....*....|....*..
gi 17562340 197 DFGGDPDRITLAGHSAGA--ASVSALL 221
Cdd:pfam07859 65 ELGADPSRIAVAGDSAGGnlAAAVALR 91
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
121-240 |
6.98e-08 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 52.99 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 121 PVLVFIHGGGfqfGD-TSMIGYqkaADNFVSKDIIFVSIQ--YRLGPLGF--FTTGDSEIPGNMGLWDQTLAL--QFLHE 193
Cdd:COG0400 6 PLVVLLHGYG---GDeEDLLPL---APELALPGAAVLAPRapVPEGPGGRawFDLSFLEGREDEEGLAAAAEAlaAFIDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17562340 194 VLPDFGGDPDRITLAGHSAGAA-SVSALLYSPhsdHLFSQAIQLSGSI 240
Cdd:COG0400 80 LEARYGIDPERIVLAGFSQGAAmALSLALRRP---ELLAGVVALSGYL 124
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
107-261 |
7.26e-08 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 54.47 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 107 LNIVTPP--DAKEKKLPVLVFIHGGG------FQFGDTsmigyQKAADNFVS----KDIIFVSIQYRLGPlgfftTGDSE 174
Cdd:COG2382 97 VWVYLPPgyDNPGKKYPVLYLLDGGGgdeqdwFDQGRL-----PTILDNLIAagkiPPMIVVMPDGGDGG-----DRGTE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 175 IPGNMGLWDqtlalQFLHEVLP------DFGGDPDRITLAGHSAGA-ASVSALLYSPhsdHLFSQAIQLSGSiFSESNLD 247
Cdd:COG2382 167 GPGNDAFER-----FLAEELIPfveknyRVSADPEHRAIAGLSMGGlAALYAALRHP---DLFGYVGSFSGS-FWWPPGD 237
|
170
....*....|....
gi 17562340 248 RNVVDDSRKLAKAA 261
Cdd:COG2382 238 ADRGGWAELLAAGA 251
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
111-221 |
1.58e-07 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 53.57 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 111 TPPDAK-EKKLPVLVFIHGGGfqfgdTSMIGYQKAADNFVSKDIIFVSIQY---RLGPLGFFTTGDSEIPGNMGLWDQTL 186
Cdd:COG4188 52 APADAPaGGPFPLVVLSHGLG-----GSREGYAYLAEHLASHGYVVAAPDHpgsNAADLSAALDGLADALDPEELWERPL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17562340 187 ALQF-------LHEVLPDFGG--DPDRITLAGHSAGAASVSALL 221
Cdd:COG4188 127 DLSFvldqllaLNKSDPPLAGrlDLDRIGVIGHSLGGYTALALA 170
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
111-214 |
5.66e-06 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 47.65 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 111 TPPD-AKEKKLPVLVFIHGGGfQFGDTSMIGYQKAADNFVSKDI------IFVSIQYRLGplGFFTTGDSEipgnmglwd 183
Cdd:COG4099 39 LPKGyDPGKKYPLVLFLHGAG-ERGTDNEKQLTHGAPKFINPENqakfpaIVLAPQCPED--DYWSDTKAL--------- 106
|
90 100 110
....*....|....*....|....*....|.
gi 17562340 184 qTLALQFLHEVLPDFGGDPDRITLAGHSAGA 214
Cdd:COG4099 107 -DAVLALLDDLIAEYRIDPDRIYLTGLSMGG 136
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
122-214 |
1.88e-05 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 47.02 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 122 VLVFIHGGGFQFG--DT------SMIGYQKAAdnfvskdiiFVSIQYRLGPLGFFTTGDSEIpgnmglwdqTLALQFLHE 193
Cdd:PRK10162 83 TLFYLHGGGFILGnlDThdrimrLLASYSGCT---------VIGIDYTLSPEARFPQAIEEI---------VAVCCYFHQ 144
|
90 100
....*....|....*....|.
gi 17562340 194 VLPDFGGDPDRITLAGHSAGA 214
Cdd:PRK10162 145 HAEDYGINMSRIGFAGDSAGA 165
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
107-213 |
2.49e-03 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 39.82 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 107 LNIVTPPDAKEKKLPVLVFIHGGGfqfGD----TSMIGYQKAADNfvsKDIIFVSIQyrLGPLGFFT--TGDSEIPGNMg 180
Cdd:COG0627 20 VSVYLPPGYDGRPLPVLYLLHGLT---GThenwTRKTGAQRLAAE---LGVIVVMPD--GGQASFYVdwTQGPAGHYRW- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17562340 181 lWDqtlalqFLHEVLPDF-------GGDPDRITLAGHSAG 213
Cdd:COG0627 91 -ET------YLTEELPPLieanfpvSADRERRAIAGLSMG 123
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
359-412 |
3.85e-03 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 40.00 E-value: 3.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17562340 359 TYSKDNLVDFIRSQ----VAVEQEFGTASARFSGLVEEFYLSGPMTGN--------SSFYLNAFAN 412
Cdd:cd14937 54 SYAKDAMTDFINTKtnqsIIISGESGSGKTEASKLVIKYYLSGVKEDNeisntlwdSNFILEAFGN 119
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
113-215 |
4.41e-03 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 39.13 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 113 PDAKEKKLPVLVFIHGGGfqfgdTSMIGYQKAADNFVSKDIIFVSIQYRlgplGFfttGDSE-IPGNMGLWDQT---LAL 188
Cdd:COG1073 30 PAGASKKYPAVVVAHGNG-----GVKEQRALYAQRLAELGFNVLAFDYR----GY---GESEgEPREEGSPERRdarAAV 97
|
90 100
....*....|....*....|....*..
gi 17562340 189 QFLHEVLpdfGGDPDRITLAGHSAGAA 215
Cdd:COG1073 98 DYLRTLP---GVDPERIGLLGISLGGG 121
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
111-221 |
7.80e-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: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562340 111 TPPDA-KEKKLPVLVFIHGGGfQFGDTSMIGY--QKAAD--NFVskdIIFVSiQYRLGPLG---FFTTGDSEIPGNmglw 182
Cdd:COG3509 43 VPAGYdGGAPLPLVVALHGCG-GSAADFAAGTglNALADreGFI---VVYPE-GTGRAPGRcwnWFDGRDQRRGRD---- 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 17562340 183 DQTLALQFLHEVLPDFGGDPDRITLAGHSAGAASVSALL 221
Cdd:COG3509 114 DVAFIAALVDDLAARYGIDPKRVYVTGLSAGGAMAYRLA 152
|
|
| |
