|
Name |
Accession |
Description |
Interval |
E-value |
| fghA_ester_D |
TIGR02821 |
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ... |
2-276 |
5.70e-136 |
|
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: 384.90 E-value: 5.70e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 2 QLLQKNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGkPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPD 81
Cdd:TIGR02821 1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAG-PVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 82 TSPRGGQVA-VGDNWDLGQGAGFYINATEAPWSEHYQMESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKY 160
Cdd:TIGR02821 80 TSPRGTGIAgEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 161 PEKFKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVsKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQAC 239
Cdd:TIGR02821 160 PDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLV-ADGGRHSTILIDQGTADQFLdEQLRPDAFEQAC 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 691055762 240 LKAGQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
|
|
| PLN02442 |
PLN02442 |
S-formylglutathione hydrolase |
6-278 |
2.79e-116 |
|
S-formylglutathione hydrolase
Pssm-ID: 178061 [Multi-domain] Cd Length: 283 Bit Score: 335.59 E-value: 2.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 6 KNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGKpCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPR 85
Cdd:PLN02442 10 VNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGK-VPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 86 GGQV-AVGDNWDLGQGAGFYINATEAPWsEHYQMESYLIDELYPLILKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEK 163
Cdd:PLN02442 89 GLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYLKNPDK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 164 FKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVSKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQACLKA 242
Cdd:PLN02442 168 YKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLkEQLLPENFEEACKEA 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 691055762 243 GQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQLEK 278
Cdd:PLN02442 248 GAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
12-276 |
1.80e-96 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 283.65 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 12 GEQRIYQFDSQLLKGSTKFGVYLPPAAlEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDtsprGGQvav 91
Cdd:COG0627 2 GRVVRVTVPSPALGREMPVSVYLPPGY-DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----GGQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 92 gdnwdlgqgAGFYINATEAPwSEHYQMESYLIDELYPLILKSFPVNAQ--QVGIFGHSMGGHGALTLAFKYPEKFKSVSA 169
Cdd:COG0627 74 ---------ASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADreRRAIAGLSMGGHGALTLALRHPDLFRAVAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 170 FAPICAPTECAWGEKAFSHYLGT-DRDSWLAHDATALVSKNGAVFnEILVDQGLDDQ-FYEQVHpeKFKQACLKAGQPLT 247
Cdd:COG0627 144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGL-PLYIDCGTADPfFLEANR--QLHAALRAAGIPHT 220
|
250 260
....*....|....*....|....*....
gi 691055762 248 LRQHAGYdHGYYFIQTFMDEHLQFHAIQL 276
Cdd:COG0627 221 YRERPGG-HSWYYWASFLEDHLPFLARAL 248
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
21-271 |
7.74e-50 |
|
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: 164.94 E-value: 7.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 21 SQLLKGSTKFGVYLPPAALEGKPCSTLFYLAGlTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQVAVGDNWDLGQg 100
Cdd:pfam00756 1 SNSLGREMKVQVYLPEDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRGL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 101 agfyiNATEAPWSEHYqmESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECA 180
Cdd:pfam00756 79 -----NATEGPGAYAY--ETFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 181 WGEkafshylgTDRDSWLAHDATALVsKNGAVFNE---ILVDQGLDDQFY-EQVHPEKFKQACLKAGQP--LTLRQHAGY 254
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLA-VALSANNTrlrIYLDVGTREDFLgDQLPVEILEELAPNRELAeqLAYRGVGGY 222
|
250 260
....*....|....*....|....
gi 691055762 255 DHGY-------YFIQTFMDEHLQF 271
Cdd:pfam00756 223 DHEYygghdwaYWRAQLIAALIDL 246
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| fghA_ester_D |
TIGR02821 |
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ... |
2-276 |
5.70e-136 |
|
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: 384.90 E-value: 5.70e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 2 QLLQKNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGkPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPD 81
Cdd:TIGR02821 1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAG-PVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 82 TSPRGGQVA-VGDNWDLGQGAGFYINATEAPWSEHYQMESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKY 160
Cdd:TIGR02821 80 TSPRGTGIAgEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 161 PEKFKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVsKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQAC 239
Cdd:TIGR02821 160 PDRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLV-ADGGRHSTILIDQGTADQFLdEQLRPDAFEQAC 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 691055762 240 LKAGQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
|
|
| PLN02442 |
PLN02442 |
S-formylglutathione hydrolase |
6-278 |
2.79e-116 |
|
S-formylglutathione hydrolase
Pssm-ID: 178061 [Multi-domain] Cd Length: 283 Bit Score: 335.59 E-value: 2.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 6 KNRCFEGEQRIYQFDSQLLKGSTKFGVYLPPAALEGKpCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPR 85
Cdd:PLN02442 10 VNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGK-VPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 86 GGQV-AVGDNWDLGQGAGFYINATEAPWsEHYQMESYLIDELYPLILKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEK 163
Cdd:PLN02442 89 GLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYLKNPDK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 164 FKSVSAFAPICAPTECAWGEKAFSHYLGTDRDSWLAHDATALVSKNGAVFNEILVDQGLDDQFY-EQVHPEKFKQACLKA 242
Cdd:PLN02442 168 YKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLkEQLLPENFEEACKEA 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 691055762 243 GQPLTLRQHAGYDHGYYFIQTFMDEHLQFHAIQLEK 278
Cdd:PLN02442 248 GAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALKS 283
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
12-276 |
1.80e-96 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 283.65 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 12 GEQRIYQFDSQLLKGSTKFGVYLPPAAlEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDtsprGGQvav 91
Cdd:COG0627 2 GRVVRVTVPSPALGREMPVSVYLPPGY-DGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----GGQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 92 gdnwdlgqgAGFYINATEAPwSEHYQMESYLIDELYPLILKSFPVNAQ--QVGIFGHSMGGHGALTLAFKYPEKFKSVSA 169
Cdd:COG0627 74 ---------ASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADreRRAIAGLSMGGHGALTLALRHPDLFRAVAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 170 FAPICAPTECAWGEKAFSHYLGT-DRDSWLAHDATALVSKNGAVFnEILVDQGLDDQ-FYEQVHpeKFKQACLKAGQPLT 247
Cdd:COG0627 144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGL-PLYIDCGTADPfFLEANR--QLHAALRAAGIPHT 220
|
250 260
....*....|....*....|....*....
gi 691055762 248 LRQHAGYdHGYYFIQTFMDEHLQFHAIQL 276
Cdd:COG0627 221 YRERPGG-HSWYYWASFLEDHLPFLARAL 248
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
21-271 |
7.74e-50 |
|
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: 164.94 E-value: 7.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 21 SQLLKGSTKFGVYLPPAALEGKPCSTLFYLAGlTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQVAVGDNWDLGQg 100
Cdd:pfam00756 1 SNSLGREMKVQVYLPEDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRGL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 101 agfyiNATEAPWSEHYqmESYLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECA 180
Cdd:pfam00756 79 -----NATEGPGAYAY--ETFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 181 WGEkafshylgTDRDSWLAHDATALVsKNGAVFNE---ILVDQGLDDQFY-EQVHPEKFKQACLKAGQP--LTLRQHAGY 254
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLA-VALSANNTrlrIYLDVGTREDFLgDQLPVEILEELAPNRELAeqLAYRGVGGY 222
|
250 260
....*....|....*....|....
gi 691055762 255 DHGY-------YFIQTFMDEHLQF 271
Cdd:pfam00756 223 DHEYygghdwaYWRAQLIAALIDL 246
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
12-271 |
2.33e-20 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 88.76 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 12 GEQRIYQFDSQLLKGSTKFGVYLPPAALE-GKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQL-------SLILITPDTS 83
Cdd:COG2382 79 GTVETVTYPSKALGRTRRVWVYLPPGYDNpGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDNLiaagkipPMIVVMPDGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 84 PRGGqvavgDNWDLGQGAGFyinateapwsehyqmESYLIDELYPLILKSFPV--NAQQVGIFGHSMGGHGALTLAFKYP 161
Cdd:COG2382 159 DGGD-----RGTEGPGNDAF---------------ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALRHP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 162 EKFKSVSAFAPICAPTEcawgekafshyLGTDRDSWLAHDATALVSKNGAVFneilVDQGLDDQFYEQVhpEKFKQACLK 241
Cdd:COG2382 219 DLFGYVGSFSGSFWWPP-----------GDADRGGWAELLAAGAPKKPLRFY----LDVGTEDDLLEAN--RALAAALKA 281
|
250 260 270
....*....|....*....|....*....|
gi 691055762 242 AGQPLTLRQHAGyDHGYYFIQTFMDEHLQF 271
Cdd:COG2382 282 KGYDVEYREFPG-GHDWAVWRAALPDFLPW 310
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
136-270 |
2.92e-10 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 58.87 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 136 VNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAPTECAWGEKAFS-HYLGT---DRDSWLAHDATALVSK-NG 210
Cdd:COG1506 90 VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTeRLMGGpweDPEAYAARSPLAYADKlKT 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 691055762 211 AVfneiLVDQGLDDqfyEQVHP---EKFKQACLKAGQPLTLRQHAGYDHGYYF---------IQTFMDEHLQ 270
Cdd:COG1506 170 PL----LLIHGEAD---DRVPPeqaERLYEALKKAGKPVELLVYPGEGHGFSGagapdylerILDFLDRHLK 234
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
92-175 |
3.36e-09 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 55.74 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 92 GDNWD--LGQGAGFYINATE---------AP-------WSEHYQMEsyLIDELYPLILKSFPVNAQQVGIFGHSMGGHGA 153
Cdd:COG4099 62 GTDNEkqLTHGAPKFINPENqakfpaivlAPqcpeddyWSDTKALD--AVLALLDDLIAEYRIDPDRIYLTGLSMGGYGT 139
|
90 100
....*....|....*....|..
gi 691055762 154 LTLAFKYPEKFksvSAFAPICA 175
Cdd:COG4099 140 WDLAARYPDLF---AAAVPICG 158
|
|
| YbbA |
COG2819 |
Predicted hydrolase of the alpha/beta superfamily [General function prediction only]; |
121-172 |
1.78e-08 |
|
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
Pssm-ID: 442067 [Multi-domain] Cd Length: 250 Bit Score: 53.84 E-value: 1.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 691055762 121 YLIDELYPLILKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAP 172
Cdd:COG2819 112 FLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
32-182 |
4.61e-06 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 46.92 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 32 VYLPPAALEGKPCSTLFYLAGLTCTEETFAIKAHAQHMAAQLSLILITPDTSPRGGQ----VAVGDNWDLGQG-AGFyIN 106
Cdd:COG3509 41 LYVPAGYDGGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGrcwnWFDGRDQRRGRDdVAF-IA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 107 AteapwsehyqmesyLIDELypliLKSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFA---PICAPTE-CAWG 182
Cdd:COG3509 120 A--------------LVDDL----AARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAglpYGAASDAaCAPG 181
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
120-157 |
2.04e-04 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 42.02 E-value: 2.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 691055762 120 SYLIDELYPLILKSFP----VNAQQVGIFGHSMGGHGALTLA 157
Cdd:COG4188 129 SFVLDQLLALNKSDPPlagrLDLDRIGVIGHSLGGYTALALA 170
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
143-176 |
1.29e-03 |
|
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: 39.51 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....
gi 691055762 143 IFGHSMGGHGALTLAFKYPEKFKSVSAFAPICAP 176
Cdd:pfam12146 80 LLGHSMGGLIAALYALRYPDKVDGLILSAPALKI 113
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
131-180 |
1.44e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 39.18 E-value: 1.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 691055762 131 LKSFP-VNAQQVGIFGHSMGGHGALTLAFKYPEkFKSVSAFAPICAPTECA 180
Cdd:COG0412 100 LKAQPeVDAGRVGVVGFCFGGGLALLAAARGPD-LAAAVSFYGGLPADDLL 149
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
121-270 |
1.71e-03 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 38.75 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 121 YLIDELYplilksfpVNAQQVGIFGHSMGGHGALTLAFKYPEKFKSVSAFAPIC------APTECAWGEKAFSHylGTDR 194
Cdd:pfam00326 54 YLIEQGY--------TDPDRLAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVdwlaymSDTSLPFTERYMEW--GNPW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 195 DSWLAHDATALVS--KNGAVFNEILVDQGLDDqfyEQVHP---EKFKQACLKAGQPLTLRQHAGYDHGYY---------- 259
Cdd:pfam00326 124 DNEEGYDYLSPYSpaDNVKVYPPLLLIHGLLD---DRVPPwqsLKLVAALQRKGVPFLLLIFPDEGHGIGkprnkveeya 200
|
170
....*....|.
gi 691055762 260 FIQTFMDEHLQ 270
Cdd:pfam00326 201 RELAFLLEYLG 211
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
113-167 |
5.28e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 37.29 E-value: 5.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 691055762 113 SEHYQMESY------LIDELyplilksfpvNAQQVGIFGHSMGGHGALTLAFKYPEKFKSV 167
Cdd:COG0596 67 AGGYTLDDLaddlaaLLDAL----------GLERVVLVGHSMGGMVALELAARHPERVAGL 117
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
132-259 |
5.64e-03 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 37.16 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691055762 132 KSFPVNAQQVGIFGHSMGGHGALTLAFKYPEKFKS-VSAFAPICAPTecawgekafshylgTDRDSWLAHDATALVSkng 210
Cdd:COG0657 79 AELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPrPAAQVLIYPVL--------------DLTASPLRADLAGLPP--- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 691055762 211 avfneILVDQGLDDQFYEQVhpEKFKQACLKAGQPLTLRQHAGYDHGYY 259
Cdd:COG0657 142 -----TLIVTGEADPLVDES--EALAAALRAAGVPVELHVYPGGGHGFG 183
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
145-172 |
9.66e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 37.23 E-value: 9.66e-03
10 20
....*....|....*....|....*...
gi 691055762 145 GHSMGGHGALTLAFKYPEKFKSVSAFAP 172
Cdd:PRK14875 203 GHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
|