|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
1-254 |
0e+00 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 532.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 1 MKLNSRTQSAQNPHNNSPVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPEMTYAAMAQDLLDTLDDRQI 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 81 EKATFIGHSMGGKAVMALTALAPERIAGLVAIDIAPVDYHVRRHDEIFNAINAVTDAGAASRQQAATVMREHLQEEGVIQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 161 FLLKSFVDGQWRFNVPVLWDQYPHIVGWQTVPAWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 695765792 241 PEAVLRAIRRYLTA 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
3.90e-41 |
|
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: 140.52 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPE-MTYAAMAQDLLDTLDDRQIEKATFIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 97 ALTALAPERIAGLVAIDiapvdyhvrrhdeifnainavtdagaasrqQAATVMREHLQEEGVIQFLLKSFVDGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765792 177 vlwdqyphivgWQTVPAWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLTAL 255
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
18-241 |
4.63e-24 |
|
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: 96.80 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDL-VNDYDILQVDMRNHGLSPRSPE------MTYAAMAQDLLDTLDdrqIEKATFIGHSM 90
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAqddyrtDDLAEDLEYILEALG---LEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 91 GGKAVMALTALAPERIAGLVAIDIAPVDYHVRRHDEIFNAI-----------NAVTDAGAASRQQAATVMREHLQEEGVI 159
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffdgfvadFAPNPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 160 QFLLKSFVDGQWRFNVPVLWDQyPHIVGWQTVP------AWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAG 233
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237
|
....*...
gi 695765792 234 HWVHAEKP 241
Cdd:pfam00561 238 HFAFLEGP 245
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
39-253 |
1.04e-14 |
|
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 131480 [Multi-domain] Cd Length: 251 Bit Score: 71.62 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 39 LVNDYDILQVDMRNHGLSPrSPEMTY--AAMAQDLLDTLDDRQIEKATFIGHSMGGKAVMALTALAPERIAGLVAIDIAP 116
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSD-APEGPYsiEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 117 vdyhvrrhdeifnAINavTDAGAASRqqAATVMREHLQE--EGVIQfllKSFVDGqWRFNVPVLWDQYPHIVGWQTVPAW 194
Cdd:TIGR02427 115 -------------KIG--TPESWNAR--IAAVRAEGLAAlaDAVLE---RWFTPG-FREAHPARLDLYRNMLVRQPPDGY 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765792 195 PH-------------------PTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLT 253
Cdd:TIGR02427 174 AGccaairdadfrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
65-112 |
2.63e-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: 38.36 E-value: 2.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 695765792 65 AAMAQDLLDtlddrQIEKATFIGHSMGGKAVMALTALAPERIAGLVAI 112
Cdd:cd12809 160 RAAGCALLD-----IIGPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
1-254 |
0e+00 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 532.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 1 MKLNSRTQSAQNPHNNSPVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPEMTYAAMAQDLLDTLDDRQI 80
Cdd:PRK10673 1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 81 EKATFIGHSMGGKAVMALTALAPERIAGLVAIDIAPVDYHVRRHDEIFNAINAVTDAGAASRQQAATVMREHLQEEGVIQ 160
Cdd:PRK10673 81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 161 FLLKSFVDGQWRFNVPVLWDQYPHIVGWQTVPAWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
|
250
....*....|....
gi 695765792 241 PEAVLRAIRRYLTA 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
18-255 |
3.90e-41 |
|
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: 140.52 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPE-MTYAAMAQDLLDTLDDRQIEKATFIGHSMGGKAVM 96
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 97 ALTALAPERIAGLVAIDiapvdyhvrrhdeifnainavtdagaasrqQAATVMREHLQEEGVIQFLLKSFVDGQWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695765792 177 vlwdqyphivgWQTVPAWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLTAL 255
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
18-241 |
4.63e-24 |
|
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: 96.80 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDL-VNDYDILQVDMRNHGLSPRSPE------MTYAAMAQDLLDTLDdrqIEKATFIGHSM 90
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRPKAqddyrtDDLAEDLEYILEALG---LEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 91 GGKAVMALTALAPERIAGLVAIDIAPVDYHVRRHDEIFNAI-----------NAVTDAGAASRQQAATVMREHLQEEGVI 159
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffdgfvadFAPNPLGRLVAKLLALLLLRLRLLKALP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 160 QFLLKSFVDGQWRFNVPVLWDQyPHIVGWQTVP------AWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAG 233
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGAL-LFIETWSTELrakflgRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237
|
....*...
gi 695765792 234 HWVHAEKP 241
Cdd:pfam00561 238 HFAFLEGP 245
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
18-254 |
8.21e-19 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 84.61 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLS-PRSPEMTYAAMAQDLLDTLDDRQIEKATFIGHSMGGKAVM 96
Cdd:PRK14875 133 PVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVAL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 97 ALTALAPERIAGLVAidIAP--------VDYhvrrhdeIFNAINA-------------VTDAGAASRQQAATVMREhLQE 155
Cdd:PRK14875 213 RLAARAPQRVASLTL--IAPaglgpeinGDY-------IDGFVAAesrrelkpvlellFADPALVTRQMVEDLLKY-KRL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 156 EGVIQFLLK----SFVDGQWRFNV-PVLWD-QYPHIVGW----QTVPAwPHptlfipGGNSPyvtddyrdtllaqfPQAR 225
Cdd:PRK14875 283 DGVDDALRAladaLFAGGRQRVDLrDRLASlAIPVLVIWgeqdRIIPA-AH------AQGLP--------------DGVA 341
|
250 260
....*....|....*....|....*....
gi 695765792 226 AHVIAGAGHWVHAEKPEAVLRAIRRYLTA 254
Cdd:PRK14875 342 VHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
18-254 |
9.74e-15 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 71.19 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLV-NDYDILQVDMRNHGLSPRSPEM--TYAAMAQDL---LDTLDDRQIEKATFIGHSMG 91
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 92 GKAVMALTALAPERIAGLVAidIAPvdyhvrrhdeifnAINAVTDAGAASRQQAATVMREHLqeegviqfllksfvdgqw 171
Cdd:COG2267 110 GLIALLYAARYPDRVAGLVL--LAP-------------AYRADPLLGPSARWLRALRLAEAL------------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 172 rfnvpvlwdqyphivgwqtvPAWPHPTLFIPGGNSPYV-TDDYRDTLLAQFPQARAHVIAGAGHWVHAEKP-EAVLRAIR 249
Cdd:COG2267 157 --------------------ARIDVPVLVLHGGADRVVpPEAARRLAARLSPDVELVLLPGARHELLNEPArEEVLAAIL 216
|
....*
gi 695765792 250 RYLTA 254
Cdd:COG2267 217 AWLER 221
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
39-253 |
1.04e-14 |
|
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 131480 [Multi-domain] Cd Length: 251 Bit Score: 71.62 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 39 LVNDYDILQVDMRNHGLSPrSPEMTY--AAMAQDLLDTLDDRQIEKATFIGHSMGGKAVMALTALAPERIAGLVAIDIAP 116
Cdd:TIGR02427 36 LTPDFRVLRYDKRGHGLSD-APEGPYsiEDLADDVLALLDHLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 117 vdyhvrrhdeifnAINavTDAGAASRqqAATVMREHLQE--EGVIQfllKSFVDGqWRFNVPVLWDQYPHIVGWQTVPAW 194
Cdd:TIGR02427 115 -------------KIG--TPESWNAR--IAAVRAEGLAAlaDAVLE---RWFTPG-FREAHPARLDLYRNMLVRQPPDGY 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765792 195 PH-------------------PTLFIPGGNSPYVTDDYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLT 253
Cdd:TIGR02427 174 AGccaairdadfrdrlgaiavPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
19-247 |
5.28e-14 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 69.04 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 19 VVLVHGLFGSLDNLGILARDlvnDYDILQVDMRNHGLSPRSPEmTYAAMAQDLLDTLDDRQIEKATFIGHSMGGKAVMAL 98
Cdd:pfam12697 1 VVLVHGAGLSAAPLAALLAA---GVAVLAPDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 99 TALAPeriagLVAIDIAPVDYHVRRHDEIFNAINAVTDAGAASRQQAATVMREHlqeegviqFLLKSFVDGQWRFNVPVL 178
Cdd:pfam12697 77 AAAAL-----VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARG--------FLDDLPADAEWAAALARL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765792 179 wDQYPHIVGWQTVPAWPH--PTLFIPGGNSPYVTDDYRDtLLAQFPQARAHVIAGAGHWVHaEKPEAVLRA 247
Cdd:pfam12697 144 -AALLAALALLPLAAWRDlpVPVLVLAEEDRLVPELAQR-LLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
18-141 |
2.58e-12 |
|
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.
Pssm-ID: 369540 Cd Length: 233 Bit Score: 64.31 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHG---LSPRSPEMTYAAMAQD---LLDTLD--------------- 76
Cdd:pfam07819 6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNgfhLDFFSVDFNEELSAFHgrtLLDQAEylndairyilslyas 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765792 77 -DRQIEKATFIGHSMGGK---AVMALTALAPERIAGLVAIDiAPVDYHVRRHD----EIFNAINAVTDAGAAS 141
Cdd:pfam07819 86 gRPGPTSVILIGHSMGGIvarAALTLPNYIPQSVNTIITLS-SPHAKPPLTFDgdilKFYERLNAFWRKLYND 157
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
19-116 |
2.40e-08 |
|
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: 52.99 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 19 VVLVHGLFGSLDNLGILARDLV-NDYDILQVDMRNHGLSP--RSPEMTYAAMAQDL---LDTLDDRQIEKATFI-GHSMG 91
Cdd:pfam12146 7 VVLVHGLGEHSGRYAHLADALAaQGFAVYAYDHRGHGRSDgkRGHVPSFDDYVDDLdtfVDKIREEHPGLPLFLlGHSMG 86
|
90 100
....*....|....*....|....*....
gi 695765792 92 GKAVMALTALAPERIAGLV----AIDIAP 116
Cdd:pfam12146 87 GLIAALYALRYPDKVDGLIlsapALKIKP 115
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
19-252 |
3.42e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 52.71 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 19 VVLVHGLFGSLDN-LGILARDLVND-YDILQVDMRNHGLSPRSPEMTYAAMAQDLLDTLDDRQIEKATFI---GHSMGGK 93
Cdd:COG1506 26 VVYVHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIgiyGHSYGGY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 94 AVMALTALAPERIAGLVAIdiapvdyhvrrhdeifnaiNAVTDAgaasrqqaATVMREHLQEEGVIQFLLKSFVDGQWRF 173
Cdd:COG1506 106 MALLAAARHPDRFKAAVAL-------------------AGVSDL--------RSYYGTTREYTERLMGGPWEDPEAYAAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 174 NvPVLWdqyphivgwqtVPAWPHPTLFIPGGNSPYV----TDDYRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIR 249
Cdd:COG1506 159 S-PLAY-----------ADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERIL 226
|
...
gi 695765792 250 RYL 252
Cdd:COG1506 227 DFL 229
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
18-112 |
6.93e-07 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 46.75 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLDNLGILARDLVND-YDILQVdmrNHGLSPRSPEMTYAAMAQDLLDTLDDRQIEKATFIGHSMGGkaVM 96
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRLRAAgYPVYAL---NYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGG--LV 81
|
90 100
....*....|....*....|
gi 695765792 97 ALTALA----PERIAGLVAI 112
Cdd:COG1075 82 ARYYLKrlggAAKVARVVTL 101
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
13-252 |
6.81e-06 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 46.06 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 13 PHNNSP----VVLVHGLFGSLDNLGILARDLV-NDYDILQVDMRNHGLS---PR---SPEMTYAAMAQDLLDTLDDRQIE 81
Cdd:COG1073 30 PAGASKkypaVVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESegePReegSPERRDARAAVDYLRTLPGVDPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 82 KATFIGHSMGGKAVMALTALAPeRIAGLVaidiapvdyhvrrhdeifnAINAVTDAGAASRQQAATVMREHLqeeGVIQF 161
Cdd:COG1073 110 RIGLLGISLGGGYALNAAATDP-RVKAVI-------------------LDSPFTSLEDLAAQRAKEARGAYL---PGVPY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 162 L----LKSFVDgqwrfnvpvlwDQYPHIvgwQTVPAWPHPTLFIPGGNSPYVTDDYRDTLLAQFPQARA-HVIAGAGH-- 234
Cdd:COG1073 167 LpnvrLASLLN-----------DEFDPL---AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvd 232
|
250 260
....*....|....*....|.
gi 695765792 235 --WVHAEKPEAVLRA-IRRYL 252
Cdd:COG1073 233 lyDRPEEEYFDKLAEfFKKNL 253
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
18-123 |
1.38e-05 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 45.50 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLVHGLFGSLD----NLGILARDlvndYDILQVDMRNHGLS--------PRSPEMTYAAMAQDLLDTLDDRQIEKATF 85
Cdd:PLN02824 31 ALVLVHGFGGNADhwrkNTPVLAKS----HRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAFV 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 695765792 86 IGHSMGGKAVMALTALAPERIAGLVAIDIAPVDYHVRR 123
Cdd:PLN02824 107 ICNSVGGVVGLQAAVDAPELVRGVMLINISLRGLHIKK 144
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
19-119 |
2.07e-05 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 44.55 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 19 VVLVHGLFGSLDNLGILARDLV-NDYDILQVDMRNHGLSPRS-PEMTYAAMAQDLLDTLDD--RQIEKATFIGHSMGGKA 94
Cdd:COG1647 18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEIlkAGYDKVIVIGLSMGGLL 97
|
90 100
....*....|....*....|....*
gi 695765792 95 VMALTALAPErIAGLVAIDiAPVDY 119
Cdd:COG1647 98 ALLLAARYPD-VAGLVLLS-PALKI 120
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
9-257 |
2.39e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 41.75 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 9 SAQNPHNNSPVVLVHGLFGSLD----NLGILARDlvndYDILQVDMRNHGLSPRSPEMTYA--AMAQDLLDTLDDrQIEK 82
Cdd:PLN02679 81 SPEVTSSGPPVLLVHGFGASIPhwrrNIGVLAKN----YTVYAIDLLGFGASDKPPGFSYTmeTWAELILDFLEE-VVQK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 83 AT-FIGHSMGGKA-VMALTALAPERIAGLVAIDIA------------------P----VDY-------------HVRRHD 125
Cdd:PLN02679 156 PTvLIGNSVGSLAcVIAASESTRDLVRGLVLLNCAggmnnkavvddwriklllPllwlIDFllkqrgiasalfnRVKQRD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 126 EIFNAINAVTDAGAASRQQAATVMREHLQEEGViqflLKSFVDgqwrfnvpvlwdqyphIVgwqTVPAWPHPTLFIP--- 202
Cdd:PLN02679 236 NLKNILLSVYGNKEAVDDELVEIIRGPADDEGA----LDAFVS----------------IV---TGPPGPNPIKLIPris 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695765792 203 -------GGNSPYVTDD-----YRDTLLAQFPQARAHVIAGAGHWVHAEKPEAVLRAIRRYLTALQA 257
Cdd:PLN02679 293 lpilvlwGDQDPFTPLDgpvgkYFSSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQLPS 359
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
65-112 |
2.63e-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: 38.36 E-value: 2.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 695765792 65 AAMAQDLLDtlddrQIEKATFIGHSMGGKAVMALTALAPERIAGLVAI 112
Cdd:cd12809 160 RAAGCALLD-----IIGPAILITHSQGGPFGWLAADARPDLVKAIVAI 202
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
16-116 |
3.97e-03 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 37.69 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 16 NSPVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPEMTYAAMAQDLLDTLDDrqieKATFIGHSMGGKAV 95
Cdd:PRK10349 13 NVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPD----KAIWLGWSLGGLVA 88
|
90 100
....*....|....*....|.
gi 695765792 96 MALTALAPERIAGLVAIDIAP 116
Cdd:PRK10349 89 SQIALTHPERVQALVTVASSP 109
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
18-98 |
4.70e-03 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 37.78 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 18 PVVLV-HGLFGSLDNLGILARDLV-----------NDYDILQVDMRNHGLSPRSPEMTYAAMAQDL---LDTLDDRQIEK 82
Cdd:COG4188 63 PLVVLsHGLGGSREGYAYLAEHLAshgyvvaapdhPGSNAADLSAALDGLADALDPEELWERPLDLsfvLDQLLALNKSD 142
|
90 100
....*....|....*....|....*..
gi 695765792 83 ATF-----------IGHSMGGKAVMAL 98
Cdd:COG4188 143 PPLagrldldrigvIGHSLGGYTALAL 169
|
|
| PLN02578 |
PLN02578 |
hydrolase |
17-115 |
6.24e-03 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 37.51 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 17 SPVVLVHGLFGSLDNLGILARDLVNDYDILQVDMRNHGLSPRSPeMTYAAM--AQDLLDTLDDRQIEKATFIGHSMGGKA 94
Cdd:PLN02578 87 LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKAL-IEYDAMvwRDQVADFVKEVVKEPAVLVGNSLGGFT 165
|
90 100
....*....|....*....|.
gi 695765792 95 VMALTALAPERIAGLVAIDIA 115
Cdd:PLN02578 166 ALSTAVGYPELVAGVALLNSA 186
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
10-118 |
8.85e-03 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 36.66 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765792 10 AQNPHNNSP-VVLVHGLFGSLDN--LGILARDLV-NDYDILQVDMRNHGLSP-RSPEMTYAAMAQDL---LDTLDDRQIE 81
Cdd:COG0429 54 SDPPAPSKPlVVLLHGLEGSSDShyARGLARALYaRGWDVVRLNFRGCGGEPnLLPRLYHSGDTEDLvwvLAHLRARYPY 133
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 695765792 82 KATF-IGHSMGGKAV---MALTALAPERIAGLVAIDiAPVD 118
Cdd:COG0429 134 APLYaVGFSLGGNLLlkyLGEQGDDAPPLKAAVAVS-PPLD 173
|
|
| |
