|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
44-243 |
5.75e-22 |
|
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: 91.22 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 44 KLAYRKLKGKSPGVVFLPGFA--SHMGGQKAEALEEfckslGHSCLRFDYSGCGSSEGELTNYTIGAWKKDVLYVLDELV 121
Cdd:COG0596 13 RLHYREAGPDGPPVVLLHGLPgsSYEWRPLIPALAA-----GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 122 EGPQILVGSSMGGWLMLLAALARPEKTAALVGISTAADHFVTAFNAlpietkkeieeqgfwkfpTKHNEEGFYTLsLDFL 201
Cdd:COG0596 88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR------------------PGLAPEALAAL-LRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1030311298 202 KEAENHCILHspiPVSCPVRLVHGLKDSDVPWHVSMQVAERV 243
Cdd:COG0596 149 ARTDLRERLA---RITVPTLVIWGEKDPIVPPALARRLAELL 187
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
57-170 |
3.01e-11 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 62.14 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHMGGQK--AEALEEfcksLGHSCLRFDYSGCGSSEG--ELTNYTIGAWKKDVLYVLDELVEGPQILVGSSM 132
Cdd:pfam00561 3 VLLLHGLPGSSDLWRklAPALAR----DGFRVIALDLRGFGKSSRpkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1030311298 133 GGWLMLLAALARPEKTAALVGISTAADHFVTAFNALPI 170
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFI 116
|
|
| hydr2_PEP |
TIGR03101 |
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ... |
57-152 |
5.44e-07 |
|
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.
Pssm-ID: 274428 Cd Length: 266 Bit Score: 49.82 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHMG-GQKAEAL--EEFCKsLGHSCLRFDYSGCGSSEGELTNYTIGAWKKDVLYV---LDELVEGPQILVGS 130
Cdd:TIGR03101 28 VIYLPPFAEEMNkSRRMVALqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
|
90 100
....*....|....*....|..
gi 1030311298 131 SMGGWLMLLAALARPEKTAALV 152
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
|
|
| PLN02578 |
PLN02578 |
hydrolase |
90-201 |
2.67e-06 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 47.91 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 90 DYSGCGSSEGELTNYTIGAWKKDVLYVLDELVEGPQILVGSSMGGWLMLLAALARPEKTAALVGISTAADhfvtaFNALP 169
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQ-----FGSES 193
|
90 100 110
....*....|....*....|....*....|....
gi 1030311298 170 IETKKEI--EEQGFWKFPTKHNEEGFYTLSLDFL 201
Cdd:PLN02578 194 REKEEAIvvEETVLTRFVVKPLKEWFQRVVLGFL 227
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
117-154 |
3.95e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 44.16 E-value: 3.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1030311298 117 LDELVE--GPQILVGSSMGGWLMLLAALARPEKTAALVGI 154
Cdd:cd12808 180 YDALLDrvGPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
44-243 |
5.75e-22 |
|
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: 91.22 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 44 KLAYRKLKGKSPGVVFLPGFA--SHMGGQKAEALEEfckslGHSCLRFDYSGCGSSEGELTNYTIGAWKKDVLYVLDELV 121
Cdd:COG0596 13 RLHYREAGPDGPPVVLLHGLPgsSYEWRPLIPALAA-----GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 122 EGPQILVGSSMGGWLMLLAALARPEKTAALVGISTAADHFVTAFNAlpietkkeieeqgfwkfpTKHNEEGFYTLsLDFL 201
Cdd:COG0596 88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRR------------------PGLAPEALAAL-LRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1030311298 202 KEAENHCILHspiPVSCPVRLVHGLKDSDVPWHVSMQVAERV 243
Cdd:COG0596 149 ARTDLRERLA---RITVPTLVIWGEKDPIVPPALARRLAELL 187
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
50-281 |
3.85e-21 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 89.62 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 50 LKGKSPGVVFLPGFASHMggQKAEALEEFCKSLGHSCLRFDYSGCGSSEGELTNYTIGAWKKDVLYVLDELVEG--PQIL 127
Cdd:COG1647 11 LEGGRKGVLLLHGFTGSP--AEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 128 VGSSMGGWLMLLAALARPEkTAALVGISTAAD------------HFVTAFNALPIETKKEIEEQGFW--KFPTKHNEEgF 193
Cdd:COG1647 89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALKiddpsapllpllKYLARSLRGIGSDIEDPEVAEYAydRTPLRALAE-L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 194 YTLSLDFLKEAENhcilhspipVSCPVRLVHGLKDSDVPWHVSMQVAERVLSNDVDVVLRKHGQHRMSEKEDIKLMVYTI 273
Cdd:COG1647 167 QRLIREVRRDLPK---------ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITLDKDREEVAEEI 237
|
....*...
gi 1030311298 274 DDLIDKLT 281
Cdd:COG1647 238 LDFLERLA 245
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
51-274 |
1.43e-17 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 79.68 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 51 KGKSPGVVFLPGFashmGGQKAEALEEFCKSL---GHSCLRFDYSGCGSSEGELTNYTIgawkKDVLYVLDELVEGPQI- 126
Cdd:COG1506 20 GKKYPVVVYVHGG----PGSRDDSFLPLAQALasrGYAVLAPDYRGYGESAGDWGGDEV----DDVLAAIDYLAARPYVd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 127 -----LVGSSMGGWLMLLAALARPEKTAALVGISTAADhFVTAFNALPIETkkEIEEQGFWKfptkhNEEGFYTLSLdfL 201
Cdd:COG1506 92 pdrigIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD-LRSYYGTTREYT--ERLMGGPWE-----DPEAYAARSP--L 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1030311298 202 KEAENhcilhspipVSCPVRLVHGLKDSDVPWHVSMQVAERVLSNDVDVVLR--KHGQHRMSEKEDIKLMVYTID 274
Cdd:COG1506 162 AYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLvyPGEGHGFSGAGAPDYLERILD 227
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
31-258 |
1.71e-17 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 79.28 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 31 KTTIQYATRADLPKLAYRKLKGKSPG---VVFLPGFASHMGGQK--AEALEEfcksLGHSCLRFDYSGCGSSEGELTNY- 104
Cdd:COG2267 2 TRRLVTLPTRDGLRLRGRRWRPAGSPrgtVVLVHGLGEHSGRYAelAEALAA----AGYAVLAFDLRGHGRSDGPRGHVd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 105 TIGAWKKDVLYVLDELVE---GPQILVGSSMGGWLMLLAALARPEKTAALVGISTAadhfvtafnalpietkkeieeqgf 181
Cdd:COG2267 78 SFDDYVDDLRAALDALRArpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA------------------------ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030311298 182 wkfptkHNEEGFYTLSLDFLKEAEnhciLHSPIP-VSCPVRLVHGLKDSDVPWHVSMQVAERvLSNDVDVVLRKHGQH 258
Cdd:COG2267 134 ------YRADPLLGPSARWLRALR----LAEALArIDVPVLVLHGGADRVVPPEAARRLAAR-LSPDVELVLLPGARH 200
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
51-246 |
1.16e-11 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 63.40 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 51 KGKSPGVVFLPGFASH--MGGQKAEALEEfcksLGHSCLRFDYSGCGSSEGELTNYTIgAWKKDVLYVLDELVEGPQ--- 125
Cdd:COG1073 34 SKKYPAVVVAHGNGGVkeQRALYAQRLAE----LGFNVLAFDYRGYGESEGEPREEGS-PERRDARAAVDYLRTLPGvdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 126 ---ILVGSSMGGWLMLLAAlARPEKTAALVGISTAADhfVTAFNAlpiETKKEIEEQGFWKFPTKHNE--EGFYTLSLDF 200
Cdd:COG1073 109 eriGLLGISLGGGYALNAA-ATDPRVKAVILDSPFTS--LEDLAA---QRAKEARGAYLPGVPYLPNVrlASLLNDEFDP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1030311298 201 LKEAENhcilhspipVSCPVRLVHGLKDSDVPWHVSMQVAERVLSN 246
Cdd:COG1073 183 LAKIEK---------ISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP 219
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
57-170 |
3.01e-11 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 62.14 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHMGGQK--AEALEEfcksLGHSCLRFDYSGCGSSEG--ELTNYTIGAWKKDVLYVLDELVEGPQILVGSSM 132
Cdd:pfam00561 3 VLLLHGLPGSSDLWRklAPALAR----DGFRVIALDLRGFGKSSRpkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1030311298 133 GGWLMLLAALARPEKTAALVGISTAADHFVTAFNALPI 170
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFI 116
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
57-169 |
2.40e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 53.25 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFashmgGQKAEALEEFCKSlGHSCLRFDYSGCGSSEGELTNYTIGAwkkDVLYVLDELVEGPQ-ILVGSSMGGW 135
Cdd:pfam12697 1 VVLVHGA-----GLSAAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLADLA---DLAALLDELGAARPvVLVGHSLGGA 71
|
90 100 110
....*....|....*....|....*....|....
gi 1030311298 136 LMLLAALARPEKTAALVGISTAADHFVTAFNALP 169
Cdd:pfam12697 72 VALAAAAAALVVGVLVAPLAAPPGLLAALLALLA 105
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
79-165 |
2.52e-08 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 52.86 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 79 CKSLGHSCLRFDYSGCGSSEGELTNyTIGAwKKDVLYVLDELVE---GPQILVGSSMGGWLMLLAALARPEkTAALVGIS 155
Cdd:COG2945 51 LVAAGFAVLRFNFRGVGRSEGEFDE-GRGE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127
|
90
....*....|
gi 1030311298 156 TAADHFVTAF 165
Cdd:COG2945 128 PPVNRYDFSF 137
|
|
| hydr2_PEP |
TIGR03101 |
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ... |
57-152 |
5.44e-07 |
|
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.
Pssm-ID: 274428 Cd Length: 266 Bit Score: 49.82 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHMG-GQKAEAL--EEFCKsLGHSCLRFDYSGCGSSEGELTNYTIGAWKKDVLYV---LDELVEGPQILVGS 130
Cdd:TIGR03101 28 VIYLPPFAEEMNkSRRMVALqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
|
90 100
....*....|....*....|..
gi 1030311298 131 SMGGWLMLLAALARPEKTAALV 152
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
57-157 |
1.09e-06 |
|
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: 48.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHMGgqkaeALEEFCKSL---GHSCLRFDYSGCGSSEGELTNYT-IGAWKKDVLYVLDELVEG----PQILV 128
Cdd:pfam12146 7 VVLVHGLGEHSG-----RYAHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLL 81
|
90 100
....*....|....*....|....*....
gi 1030311298 129 GSSMGGWLMLLAALARPEKTAALVGISTA 157
Cdd:pfam12146 82 GHSMGGLIAALYALRYPDKVDGLILSAPA 110
|
|
| PLN02578 |
PLN02578 |
hydrolase |
90-201 |
2.67e-06 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 47.91 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 90 DYSGCGSSEGELTNYTIGAWKKDVLYVLDELVEGPQILVGSSMGGWLMLLAALARPEKTAALVGISTAADhfvtaFNALP 169
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQ-----FGSES 193
|
90 100 110
....*....|....*....|....*....|....
gi 1030311298 170 IETKKEI--EEQGFWKFPTKHNEEGFYTLSLDFL 201
Cdd:PLN02578 194 REKEEAIvvEETVLTRFVVKPLKEWFQRVVLGFL 227
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
111-256 |
2.46e-05 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 44.14 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 111 KDVLYVLDELVEGPQI------LVGSSMGGWLMLLAALARPEKTAALVGISTAADhfVTAFnalpiETKKEI---EEQGF 181
Cdd:pfam00326 46 DDFIAAAEYLIEQGYTdpdrlaIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVD--WLAY-----MSDTSLpftERYME 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 182 WKFPTKhNEEGFYTLS-LDFLKEaenhcilhspIPVSCPVRLVHGLKDSDVP-WHvSMQVAERVLSNDVDVVLR-----K 254
Cdd:pfam00326 119 WGNPWD-NEEGYDYLSpYSPADN----------VKVYPPLLLIHGLLDDRVPpWQ-SLKLVAALQRKGVPFLLLifpdeG 186
|
..
gi 1030311298 255 HG 256
Cdd:pfam00326 187 HG 188
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
117-154 |
3.95e-05 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 44.16 E-value: 3.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1030311298 117 LDELVE--GPQILVGSSMGGWLMLLAALARPEKTAALVGI 154
Cdd:cd12808 180 YDALLDrvGPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
57-156 |
9.68e-05 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 40.58 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 57 VVFLPGFASHmgGQKAEALEEFCKSLGHSCLRFDYSGcgssegelTNYTIGAWKKDVLYVLDELVE---GPQI-LVGSSM 132
Cdd:COG1075 8 VVLVHGLGGS--AASWAPLAPRLRAAGYPVYALNYPS--------TNGSIEDSAEQLAAFVDAVLAatgAEKVdLVGHSM 77
|
90 100
....*....|....*....|....*.
gi 1030311298 133 GGWL--MLLAALARPEKTAALVGIST 156
Cdd:COG1075 78 GGLVarYYLKRLGGAAKVARVVTLGT 103
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
39-157 |
1.24e-04 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 43.01 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 39 RADLPK--LAYRKL-KGKSPGVVFLPGFashmGGQKA------EALEEfckslGHSCLRFDYSGCGSSEGELTNYTIGAW 109
Cdd:PRK14875 113 KARIGGrtVRYLRLgEGDGTPVVLIHGF----GGDLNnwlfnhAALAA-----GRPVIALDLPGHGASSKAVGAGSLDEL 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1030311298 110 KKDVLYVLDELVEGPQILVGSSMGGWLMLLAALARPEKTAALVGISTA 157
Cdd:PRK14875 184 AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPA 231
|
|
| PRK10673 |
PRK10673 |
esterase; |
111-215 |
6.15e-04 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 40.48 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 111 KDVLYVLDELVEGPQILVGSSMGGWL-MLLAALArPEKTAALVGISTAA--------DHFVTAFNALP---IETKKE--- 175
Cdd:PRK10673 69 QDLLDTLDALQIEKATFIGHSMGGKAvMALTALA-PDRIDKLVAIDIAPvdyhvrrhDEIFAAINAVSeagATTRQQaaa 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1030311298 176 -----IEEQGFWKFPTKHNEEGFYTLSLDFLKEAENHCILHSPIP 215
Cdd:PRK10673 148 imrqhLNEEGVIQFLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIP 192
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
33-150 |
7.47e-04 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 39.95 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 33 TIQYATRADLP---KLAYRKLKGKSPGVVFLPGFashmGG------QKAEALEEfcksLGHSCL---RFDYSGCGSSEGE 100
Cdd:COG0412 5 TVTIPTPDGVTlpgYLARPAGGGPRPGVVVLHEI----FGlnphirDVARRLAA----AGYVVLapdLYGRGGPGDDPDE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030311298 101 LTNY----TIGAWKKDVLYVLDELVEGPQI------LVGSSMGGWLMLLAALARPEKTAA 150
Cdd:COG0412 77 ARALmgalDPELLAADLRAALDWLKAQPEVdagrvgVVGFCFGGGLALLAAARGPDLAAA 136
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
123-154 |
2.32e-03 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214008 Cd Length: 280 Bit Score: 38.75 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|..
gi 1030311298 123 GPQILVGSSMGGWLMLLAALARPEKTAALVGI 154
Cdd:cd12809 171 GPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
|
|
| |
