|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02442 |
PLN02442 |
S-formylglutathione hydrolase |
2-281 |
2.28e-160 |
|
S-formylglutathione hydrolase
Pssm-ID: 178061 [Multi-domain] Cd Length: 283 Bit Score: 446.92 E-value: 2.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 2 ALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAP 81
Cdd:PLN02442 4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 82 DTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442 84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 161 KNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767977352 241 AACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
|
|
| fghA_ester_D |
TIGR02821 |
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ... |
6-280 |
2.04e-158 |
|
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]
Pssm-ID: 131868 Cd Length: 275 Bit Score: 441.91 E-value: 2.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 6 ISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSP 85
Cdd:TIGR02821 3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 86 RGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821 83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 166 YKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYpGSQLDILIDQGKDDQFlLDGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQF-LDEQLRPDAFEQACRA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 767977352 246 KKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
13-281 |
2.03e-113 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 326.79 E-value: 2.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 13 GGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627 1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 93 edeswdfGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG0627 71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 171 AFAPICNPVLCPWGKKAFSGYLGT-DQSKWKAYDATHLVKSYPGsQLDILIDQGKDDQFLLDGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218
|
250 260 270
....*....|....*....|....*....|..
gi 767977352 250 VVFRLQEGYdHSYYFIATFITDHIRHHAKYLN 281
Cdd:COG0627 219 HTYRERPGG-HSWYYWASFLEDHLPFLARALG 249
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
23-275 |
1.83e-82 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 248.14 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 23 SVELNCKMKFAVYLP-PKAETGKCPALYWLSGlTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGeDESWDFGt 101
Cdd:pfam00756 1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 102 gagfyVDATEDPWKTNYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLC 181
Cdd:pfam00756 78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 182 PWGKkafsgylgTDQSKWKAYDATHLVK--SYPGSQLDILIDQGKDDQFLLDgQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFLGD-QLPVEILEELAPNRELAeqLAYRGVGG 221
|
250 260
....*....|....*....|....*
gi 767977352 258 YDHSY-------YFIATFITDHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02442 |
PLN02442 |
S-formylglutathione hydrolase |
2-281 |
2.28e-160 |
|
S-formylglutathione hydrolase
Pssm-ID: 178061 [Multi-domain] Cd Length: 283 Bit Score: 446.92 E-value: 2.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 2 ALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAP 81
Cdd:PLN02442 4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 82 DTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442 84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 161 KNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767977352 241 AACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
|
|
| fghA_ester_D |
TIGR02821 |
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ... |
6-280 |
2.04e-158 |
|
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]
Pssm-ID: 131868 Cd Length: 275 Bit Score: 441.91 E-value: 2.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 6 ISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSP 85
Cdd:TIGR02821 3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 86 RGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821 83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 166 YKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYpGSQLDILIDQGKDDQFlLDGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQF-LDEQLRPDAFEQACRA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 767977352 246 KKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
13-281 |
2.03e-113 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 326.79 E-value: 2.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 13 GGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627 1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 93 edeswdfGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG0627 71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 171 AFAPICNPVLCPWGKKAFSGYLGT-DQSKWKAYDATHLVKSYPGsQLDILIDQGKDDQFLLDGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218
|
250 260 270
....*....|....*....|....*....|..
gi 767977352 250 VVFRLQEGYdHSYYFIATFITDHIRHHAKYLN 281
Cdd:COG0627 219 HTYRERPGG-HSWYYWASFLEDHLPFLARALG 249
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
23-275 |
1.83e-82 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 248.14 E-value: 1.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 23 SVELNCKMKFAVYLP-PKAETGKCPALYWLSGlTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGeDESWDFGt 101
Cdd:pfam00756 1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 102 gagfyVDATEDPWKTNYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLC 181
Cdd:pfam00756 78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 182 PWGKkafsgylgTDQSKWKAYDATHLVK--SYPGSQLDILIDQGKDDQFLLDgQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFLGD-QLPVEILEELAPNRELAeqLAYRGVGG 221
|
250 260
....*....|....*....|....*
gi 767977352 258 YDHSY-------YFIATFITDHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
22-262 |
3.18e-20 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 88.37 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 22 DSVELNCKMKFAVYLPP--KAETGKCPALYWLSGLTCTEQNFISKSGYHQSA----SEHGL---VVIAPDtsprgcNIKG 92
Cdd:COG2382 87 PSKALGRTRRVWVYLPPgyDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPD------GGDG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 93 EDESWDFGTGAGFyvdatedpwktnyrmYSYVTEELPQLINANFPV--DPQRMSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG2382 161 GDRGTEGPGNDAF---------------ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 171 afapicnpvlcpwgkkAFSGYLGTDQSKWKAYDATHLVK-SYPGSQLDILIDQGKDDQFLLDGQllpdNFIAACTEKKIP 249
Cdd:COG2382 226 ----------------SFSGSFWWPPGDADRGGWAELLAaGAPKKPLRFYLDVGTEDDLLEANR----ALAAALKAKGYD 285
|
250
....*....|...
gi 767977352 250 VVFRLQEGyDHSY 262
Cdd:COG2382 286 VEYREFPG-GHDW 297
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
34-278 |
1.59e-11 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 62.73 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 34 VYLPPKAetGKCPALYWLSGLTCTEQNFISksGYHQSASEHGLVVIAPDtsPRGC----NIKGEDESWDFGTGAGFyvdA 109
Cdd:COG1506 14 LYLPADG--KKYPVVVYVHGGPGSRDDSFL--PLAQALASRGYAVLAPD--YRGYgesaGDWGGDEVDDVLAAIDY---L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 110 TEDPWktnyrmysyvteelpqlinanfpVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPV----LCPWGK 185
Cdd:COG1506 85 AARPY-----------------------VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRsyygTTREYT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 186 KAFSGYLGTDQSKWKAYDATHLVKSYPGsqlDILIDQGKDDQFLLDGQLlpDNFIAACTEKKIPVVFRLQEGYDHSYYFI 265
Cdd:COG1506 142 ERLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQA--ERLYEALKKAGKPVELLVYPGEGHGFSGA 216
|
250
....*....|....*...
gi 767977352 266 ATF-----ITDHIRHHAK 278
Cdd:COG1506 217 GAPdylerILDFLDRHLK 234
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
34-261 |
1.11e-07 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 51.52 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 34 VYLPP--KAETGKCPALYWLSGltctEQNFISKSGYHQSASEHG-----LVVIA----PDTSPR-----GCNIKGEDESW 97
Cdd:COG2819 25 VYLPPgyDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGigngDDGERRlrdytPPPAPGYPGPG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 98 DFGTGAGFYVDatedpwktnyrmysYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYksvSAFApicn 177
Cdd:COG2819 101 GPGGGADAFLR--------------FLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLF---GRYI---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 178 pvlcpwgkkAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILI---DQGKDDQFLLDGQLLpDNFIAACTEKKIPVVFRL 254
Cdd:COG2819 160 ---------AISPSLWWDDGALLDEAEALLKRSPLPKRLYLSVgtlEGDSMDGMVDDARRL-AEALKAKGYPGLNVKFEV 229
|
....*..
gi 767977352 255 QEGYDHS 261
Cdd:COG2819 230 FPGETHG 236
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
30-176 |
1.96e-07 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 50.74 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 30 MKFAVYLPPKAETG-KCPALYWLSG-----------LTCTEQNFISKsgyhQSASEHGLVVIAPDTSprgcnikgEDESW 97
Cdd:COG4099 33 LPYRLYLPKGYDPGkKYPLVLFLHGagergtdnekqLTHGAPKFINP----ENQAKFPAIVLAPQCP--------EDDYW 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767977352 98 DFGTgagfYVDATEDpwktnyrMYSYVTeelpqlinANFPVDPQRMSIFGHSMGGHGALICALKNPGKYksvSAFAPIC 176
Cdd:COG4099 101 SDTK----ALDAVLA-------LLDDLI--------AEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPIC 157
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
69-263 |
9.87e-07 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 48.38 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 69 QSASEHGLVVIAPDtsPRGCNIKGEDeswdfgtgagFYVDATEDpWKTNyrmysyvteELPQLINA------NFPVDPQR 142
Cdd:pfam00326 8 QLLADRGYVVAIAN--GRGSGGYGEA----------FHDAGKGD-LGQN---------EFDDFIAAaeylieQGYTDPDR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 143 MSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVL-------------CPWGkkaFSGYLGTDQSKWKAYDATHLVK 209
Cdd:pfam00326 66 LAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVDWLAymsdtslpfteryMEWG---NPWDNEEGYDYLSPYSPADNVK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767977352 210 SYPgsqlDILIDQGkddqfLLDGQLLPDN---FIAACTEKKIPVVFRLQEGYDHSYY 263
Cdd:pfam00326 143 VYP----PLLLIHG-----LLDDRVPPWQslkLVAALQRKGVPFLLLIFPDEGHGIG 190
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
32-173 |
2.73e-06 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 47.69 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 32 FAVYLPPKAETGK-CPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIkgedeSWDFGTG-------- 102
Cdd:COG3509 39 YRLYVPAGYDGGApLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGR-----CWNWFDGrdqrrgrd 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767977352 103 -AGFYVDATEDpwktnyrmysyvteelpqlINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFA 173
Cdd:COG3509 114 dVAFIAALVDD-------------------LAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
73-159 |
8.48e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 40.09 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 73 EHGLVVIAPDTSprgcnikGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELpQLINANFP-----VDPQRMSIFG 147
Cdd:COG4188 87 SHGYVVAAPDHP-------GSNAADLSAALDGLADALDPEELWERPLDLSFVLDQL-LALNKSDPplagrLDLDRIGVIG 158
|
90
....*....|..
gi 767977352 148 HSMGGHGALICA 159
Cdd:COG4188 159 HSLGGYTALALA 170
|
|
| AXE1 |
pfam05448 |
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ... |
33-177 |
3.98e-03 |
|
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.
Pssm-ID: 398876 [Multi-domain] Cd Length: 316 Bit Score: 38.15 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 33 AVYLPPKAETGKCPALYwlsgltcteqNFIsksGYHQSASE---------HGLVVIAPDTspRGCNIKGEDESWDF--GT 101
Cdd:pfam05448 70 AWYVVPKESEEKHPAVV----------HFH---GYNGRRGDwhdmlhwaaHGYAVFVMDV--RGQGGLSEDDPRGPkgNT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 102 GAGFYVDATEDPWKTNYRmysYVTEELPQLIN--ANFP-VDPQRMSIFGHSMGGHGALICALKNPgKYKSVSAFAP-ICN 177
Cdd:pfam05448 135 YKGHITRGLLDRETYYYR---RVFLDAVRAVEivMSFPeVDEERIVVTGGSQGGALALAAAALSP-RIKAVVADYPfLSD 210
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
34-156 |
5.66e-03 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 37.59 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977352 34 VYLPPKAEtGKCPALYWLSGLTcteQNFISKSGYHQSASEHGLVVIAPDtsPRGCnikGEDEswdfgtgaGFYVDAtEDP 113
Cdd:COG1073 27 LYLPAGAS-KKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFD--YRGY---GESE--------GEPREE-GSP 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767977352 114 WKTNYR-MYSYVTEeLPQlinanfpVDPQRMSIFGHSMGGHGAL 156
Cdd:COG1073 89 ERRDARaAVDYLRT-LPG-------VDPERIGLLGISLGGGYAL 124
|
|
|