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Conserved domains on  [gi|1243381661|gb|ATC39681|]
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alpha/beta hydrolase [Elizabethkingia anophelis Ag1]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 1001822)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
Gene Ontology:  GO:0016787
PubMed:  12369917|15381402|1409539
SCOP:  3000102

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 super family cl30399
esterase;
16-257 5.78e-65

esterase;


The actual alignment was detected with superfamily member PRK10673:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 203.04  E-value: 5.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGGKVVM 95
Cdd:PRK10673   17 SPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  96 QYAITNPEKVEKLIVADMAPKAYPPH-HQGIFKALNSVDLNQVTSRQEVEEELKKYIPEIGVIQFLLKNLYWTEdkklsW 174
Cdd:PRK10673   97 ALTALAPDRIDKLVAIDIAPVDYHVRrHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQFLLKSFVDGE-----W 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 175 RFNLHVLTDKYTTFVtNAVKYGVYNGPVLFLAGANSNYILPQ--DGLLirQQFPNSEVKKIANAGHWVQAENPKDFNAAV 252
Cdd:PRK10673  172 RFNVPVLWDQYPHIV-GWEKIPAWPHPALFIRGGNSPYVTEAyrDDLL--AQFPQARAHVIAGAGHWVHAEKPDAVLRAI 248


                  ....*
gi 1243381661 253 KEFLT 257
Cdd:PRK10673  249 RRYLN 253
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
16-257 5.78e-65

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 203.04  E-value: 5.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGGKVVM 95
Cdd:PRK10673   17 SPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  96 QYAITNPEKVEKLIVADMAPKAYPPH-HQGIFKALNSVDLNQVTSRQEVEEELKKYIPEIGVIQFLLKNLYWTEdkklsW 174
Cdd:PRK10673   97 ALTALAPDRIDKLVAIDIAPVDYHVRrHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQFLLKSFVDGE-----W 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 175 RFNLHVLTDKYTTFVtNAVKYGVYNGPVLFLAGANSNYILPQ--DGLLirQQFPNSEVKKIANAGHWVQAENPKDFNAAV 252
Cdd:PRK10673  172 RFNVPVLWDQYPHIV-GWEKIPAWPHPALFIRGGNSPYVTEAyrDDLL--AQFPQARAHVIAGAGHWVHAEKPDAVLRAI 248


                  ....*
gi 1243381661 253 KEFLT 257
Cdd:PRK10673  249 RRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-258 1.76e-42

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: 143.99  E-value: 1.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661   4 LHSKIYGQDktGTPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEE-MTIDAMVNDVQVYMDYYGLEKV 82
Cdd:COG0596    14 LHYREAGPD--GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  83 YLLGHSLGGKVVMQYAITNPEKVEKLIVADmapkaypphhqgifkalnsvdlnqvtsrqEVEEELKKYIPEIGVIQFLLK 162
Cdd:COG0596    92 VLVGHSMGGMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAPEALA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 163 NLYwtedkKLSWRFNLHVLTDKYTTfvtnavkygvyngPVLFLAGANSNYILPQDGLLIRQQFPNSEVKKIANAGHWVQA 242
Cdd:COG0596   143 ALL-----RALARTDLRERLARITV-------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204

                         250
                  ....*....|....*.
gi 1243381661 243 ENPKDFNAAVKEFLTQ 258
Cdd:COG0596   205 EQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-245 3.20e-26

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: 102.58  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKSFHS---EEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGG 91
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  92 KVVMQYAITNPEKVEKLIVadMAPKAYPPhhqgifkALNSVDLNQVTSRQEVEEELKKYIPEIGVIQFLLKNLYWTE--- 168
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVL--LGALDPPH-------ELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLlrl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 169 -----DKKLSWRF---------------NLHVLTDKYTTFvtnAVKYGVYNGPVLFLAGANSNYILPQDGLLIRQQFPNS 228
Cdd:pfam00561 152 rllkaLPLLNKRFpsgdyalakslvtgaLLFIETWSTELR---AKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNA 228

                         250
                  ....*....|....*..
gi 1243381661 229 EVKKIANAGHWVQAENP 245
Cdd:pfam00561 229 RLVVIPDAGHFAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 16-257 1.40e-18

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 82.26  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVF-HGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQVY----MDYYGLEKVYLLGHSLG 90
Cdd:TIGR03695   2 KPVLVFlHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlatlLDQLGIEPFFLVGYSMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  91 GKVVMQYAITNPEKVEKLIVADMAPkaypphhqGIfkalnsVDLNQVTSRQEVEEELKKYIPEIGVIQFL---------- 160
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLILESGSP--------GL------QTEEERAARRQNDEQLAQRFEQEGLEAFLddwyqqplfa 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 161 -LKNLywTEDKK---LSWRFNLHVLTdkyttfVTNAVK-YGVYNGP------------VLFLAGAN-SNYIlpQDGLLIR 222
Cdd:TIGR03695 148 sQKNL--PPEQRqalRAERLANNPEG------LAKMLRaTGLGKQPslwpklqalkipVLYLCGERdEKFV--QIAKEMQ 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1243381661 223 QQFPNSEVKKIANAGHWVQAENPKDFNAAVKEFLT 257
Cdd:TIGR03695 218 KLIPNLTLHIIPNAGHNIHLENPEAFAKILLAFLE 252
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
16-257 5.78e-65

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 203.04  E-value: 5.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGGKVVM 95
Cdd:PRK10673   17 SPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  96 QYAITNPEKVEKLIVADMAPKAYPPH-HQGIFKALNSVDLNQVTSRQEVEEELKKYIPEIGVIQFLLKNLYWTEdkklsW 174
Cdd:PRK10673   97 ALTALAPDRIDKLVAIDIAPVDYHVRrHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQFLLKSFVDGE-----W 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 175 RFNLHVLTDKYTTFVtNAVKYGVYNGPVLFLAGANSNYILPQ--DGLLirQQFPNSEVKKIANAGHWVQAENPKDFNAAV 252
Cdd:PRK10673  172 RFNVPVLWDQYPHIV-GWEKIPAWPHPALFIRGGNSPYVTEAyrDDLL--AQFPQARAHVIAGAGHWVHAEKPDAVLRAI 248


                  ....*
gi 1243381661 253 KEFLT 257
Cdd:PRK10673  249 RRYLN 253
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-258 1.76e-42

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: 143.99  E-value: 1.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661   4 LHSKIYGQDktGTPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEE-MTIDAMVNDVQVYMDYYGLEKV 82
Cdd:COG0596    14 LHYREAGPD--GPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLERV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  83 YLLGHSLGGKVVMQYAITNPEKVEKLIVADmapkaypphhqgifkalnsvdlnqvtsrqEVEEELKKYIPEIGVIQFLLK 162
Cdd:COG0596    92 VLVGHSMGGMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAPEALA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 163 NLYwtedkKLSWRFNLHVLTDKYTTfvtnavkygvyngPVLFLAGANSNYILPQDGLLIRQQFPNSEVKKIANAGHWVQA 242
Cdd:COG0596   143 ALL-----RALARTDLRERLARITV-------------PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204

                         250
                  ....*....|....*.
gi 1243381661 243 ENPKDFNAAVKEFLTQ 258
Cdd:COG0596   205 EQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-245 3.20e-26

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: 102.58  E-value: 3.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKSFHS---EEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGG 91
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  92 KVVMQYAITNPEKVEKLIVadMAPKAYPPhhqgifkALNSVDLNQVTSRQEVEEELKKYIPEIGVIQFLLKNLYWTE--- 168
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVL--LGALDPPH-------ELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLlrl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 169 -----DKKLSWRF---------------NLHVLTDKYTTFvtnAVKYGVYNGPVLFLAGANSNYILPQDGLLIRQQFPNS 228
Cdd:pfam00561 152 rllkaLPLLNKRFpsgdyalakslvtgaLLFIETWSTELR---AKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNA 228

                         250
                  ....*....|....*..
gi 1243381661 229 EVKKIANAGHWVQAENP 245
Cdd:pfam00561 229 RLVVIPDAGHFAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 16-257 1.40e-18

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 82.26  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  16 TPLLVF-HGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQVY----MDYYGLEKVYLLGHSLG 90
Cdd:TIGR03695   2 KPVLVFlHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlatlLDQLGIEPFFLVGYSMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  91 GKVVMQYAITNPEKVEKLIVADMAPkaypphhqGIfkalnsVDLNQVTSRQEVEEELKKYIPEIGVIQFL---------- 160
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLILESGSP--------GL------QTEEERAARRQNDEQLAQRFEQEGLEAFLddwyqqplfa 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 161 -LKNLywTEDKK---LSWRFNLHVLTdkyttfVTNAVK-YGVYNGP------------VLFLAGAN-SNYIlpQDGLLIR 222
Cdd:TIGR03695 148 sQKNL--PPEQRqalRAERLANNPEG------LAKMLRaTGLGKQPslwpklqalkipVLYLCGERdEKFV--QIAKEMQ 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1243381661 223 QQFPNSEVKKIANAGHWVQAENPKDFNAAVKEFLT 257
Cdd:TIGR03695 218 KLIPNLTLHIIPNAGHNIHLENPEAFAKILLAFLE 252
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 15-108 1.58e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 72.28  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  15 GTPLLVFHGLFGMLDNWgSFGRE-FGELMPVHLIDLRNHGKSFHS-EEMTIDAMVNDVQVYMDYYGLEKVYLLGHSLGGK 92
Cdd:PRK14875  131 GTPVVLIHGFGGDLNNW-LFNHAaLAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGA 209

                          90
                  ....*....|....*.
gi 1243381661  93 VVMQYAITNPEKVEKL 108
Cdd:PRK14875  210 VALRLAARAPQRVASL 225
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
11-258 1.62e-14

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.42  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  11 QDKTGTPLLVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKS--FHSEEMTIDAMVNDVQVYMDYYGLE---KVYL 84
Cdd:COG2267    24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSdgPRGHVDSFDDYVDDLRAALDALRARpglPVVL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  85 LGHSLGGKVVMQYAITNPEKVEKLIVADMAPKAYPphhqgifkalnsvdLNQVTSRQEVEEELKKYIPEIGViqfllknl 164
Cdd:COG2267   104 LGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADP--------------LLGPSARWLRALRLAEALARIDV-------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 165 ywtedkklswrfnlhvltdkyttfvtnavkygvyngPVLFLAGANSNYILPQDGLLIRQQF-PNSEVKKIANAGHWVQAE 243
Cdd:COG2267   162 ------------------------------------PVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNE 205

                         250
                  ....*....|....*.
gi 1243381661 244 -NPKDFNAAVKEFLTQ 258
Cdd:COG2267   206 pAREEVLAAILAWLER 221
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 14-132 2.58e-09

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: 55.83  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  14 TGTPLLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGK---SFHS----EEMTidAM----VNDVQVYMDY------ 76
Cdd:pfam07819   3 SGIPVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGfhlDFFSvdfnEELS--AFhgrtLLDQAEYLNDairyil 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243381661  77 -------YGLEKVYLLGHSLGGKV---VMQYAITNPEKVEKLIVADmAPKAYPP-----HHQGIFKALNSV 132
Cdd:pfam07819  81 slyasgrPGPTSVILIGHSMGGIVaraALTLPNYIPQSVNTIITLS-SPHAKPPltfdgDILKFYERLNAF 150
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 44-120 3.63e-09

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: 55.68  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  44 VHLIDLRNHGKSF----HSEEMtiDAMVNDVQVYMDY----YGLEKVYLLGHSLGGKVVMQYAITNPEKVEKLIVA---- 111
Cdd:pfam12146  34 VYAYDHRGHGRSDgkrgHVPSF--DDYVDDLDTFVDKireeHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSapal 111


                  ....*....
gi 1243381661 112 DMAPKAYPP 120
Cdd:pfam12146 112 KIKPYLAPP 120
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 18-251 1.19e-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: 53.63  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  18 LLVFHGLFgmlDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEmTIDAMVNDVQVYMDYYGLEKVYLLGHSLGGKVVMQY 97
Cdd:pfam12697   1 VVLVHGAG---LSAAPLAALLAAGVAVLAPDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  98 AitNPEKVEKLIVADMAPKayPPHHQGIFKALNSVDLNQVTSRqeveeelkkYIPEIGVIQFLLKNlywtEDKKLSWRFN 177
Cdd:pfam12697  77 A--AAALVVGVLVAPLAAP--PGLLAALLALLARLGAALAAPA---------WLAAESLARGFLDD----LPADAEWAAA 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243381661 178 LHVLTDKYTTFVTNAV-KYGVYNGPVLFLAGAnsNYILPQDGLLIRQQFPNSEVKKIANAGHWVQaENPKDFNAA 251
Cdd:pfam12697 140 LARLAALLAALALLPLaAWRDLPVPVLVLAEE--DRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 15-110 7.23e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 51.76  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  15 GTPLLVF-HGLFGMLDNW---GSFGREFgelmPVHLIDLRNHGksfHSEEMTID--AMVND-VQVYMDYYGLEKVYLLGH 87
Cdd:PRK11126    1 GLPWLVFlHGLLGSGQDWqpvGEALPDY----PRLYIDLPGHG---GSAAISVDgfADVSRlLSQTLQSYNILPYWLVGY 73

                          90       100
                  ....*....|....*....|....
gi 1243381661  88 SLGGKVVMQYAI-TNPEKVEKLIV 110
Cdd:PRK11126   74 SLGGRIAMYYACqGLAGGLCGLIV 97
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
18-115 1.84e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 50.79  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  18 LLVFHGLFGMLDNWGSFGREFGELMPVHLIDLRNHGKSFHSEEMTIDAMVNDVQvymdYYGLEKVYLLGHSLGGKVVMQY 97
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVL----QQAPDKAIWLGWSLGGLVASQI 91

                          90
                  ....*....|....*...
gi 1243381661  98 AITNPEKVEKLIVADMAP 115
Cdd:PRK10349   92 ALTHPERVQALVTVASSP 109
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 12-122 1.13e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 45.98  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  12 DKTGTPLLVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKSFHSEEMTIDAMVNDVqvyMDYYGLEKVYLLGHSLG 90
Cdd:COG1075     2 AATRYPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLAAFVDAV---LAATGAEKVDLVGHSMG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1243381661  91 GkVVMQYAITN---PEKVEKLI-VAdmapkayPPHH 122
Cdd:COG1075    79 G-LVARYYLKRlggAAKVARVVtLG-------TPHH 106
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 18-258 3.39e-06

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 46.83  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  18 LLVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKS--FHSEEMTIDAmvNDVQVYMDYYGL------EKVYLLGHS 88
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESegEPREEGSPER--RDARAAVDYLRTlpgvdpERIGLLGIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  89 LGGKVVMQYAITNPEkveklivadmaPKAYpphhqgifkALNS--VDLNQVtSRQEVEEELKKYIPEIGviqfLLKNLYW 166
Cdd:COG1073   118 LGGGYALNAAATDPR-----------VKAV---------ILDSpfTSLEDL-AAQRAKEARGAYLPGVP----YLPNVRL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 167 TEdkklswrfnlhVLTDKYTTFvtNAVKYgvYNGPVLFLAGANSNYILPQDGLLIRQQFP-NSEVKKIANAGHwVQA--E 243
Cdd:COG1073   173 AS-----------LLNDEFDPL--AKIEK--ISRPLLFIHGEKDEAVPFYMSEDLYEAAAePKELLIVPGAGH-VDLydR 236

                         250
                  ....*....|....*
gi 1243381661 244 NPKDFNAAVKEFLTQ 258
Cdd:COG1073   237 PEEEYFDKLAEFFKK 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
17-258 1.80e-04

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.54  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  17 PLLVF-HGLFGmlDNWGSFGREFGEL----MPVHLIDLRNHGKSfhsEEMTIDAMVNDVQ------VYMDYYGLEKVYLL 85
Cdd:COG1506    24 PVVVYvHGGPG--SRDDSFLPLAQALasrgYAVLAPDYRGYGES---AGDWGGDEVDDVLaaidylAARPYVDPDRIGIY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  86 GHSLGGKVVMqYAITnpekveklivadmapkayppHHQGIFKALnsVDLNQVTSrqeveeeLKKYIPEIGVIQFLLKNLY 165
Cdd:COG1506    99 GHSYGGYMAL-LAAA--------------------RHPDRFKAA--VALAGVSD-------LRSYYGTTREYTERLMGGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 166 WtEDKKLSWRFNLHVLTDKYTTfvtnavkygvyngPVLFLAGANSNYILPQDGLLIRQQF----PNSEVKKIANAGHWVQ 241
Cdd:COG1506   149 W-EDPEAYAARSPLAYADKLKT-------------PLLLIHGEADDRVPPEQAERLYEALkkagKPVELLVYPGEGHGFS 214

                         250
                  ....*....|....*..
gi 1243381661 242 AENPKDFNAAVKEFLTQ 258
Cdd:COG1506   215 GAGAPDYLERILDFLDR 231
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 78-110 3.35e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 41.43  E-value: 3.35e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1243381661  78 GLEKVYLLGHSLGGKVVMQYAITNPEKVEKLIV 110
Cdd:PLN02894  174 NLSNFILLGHSFGGYVAAKYALKHPEHVQHLIL 206
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
19-258 7.73e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.92  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  19 LVFHGLFGMLDNWGSFGREFGEL-MPVHLIDLRNHGKSfhSEEM---TIDAMVNDVQVYMDY--YGLEKVYLLGHSLGGK 92
Cdd:COG1647    19 LLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTS--PEDLlktTWEDWLEDVEEAYEIlkAGYDKVIVIGLSMGGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  93 VVMQYAITNPEkVEKLIVadMAPKAYPPHHQGIFKALnsvdLNQvtsrqeveeeLKKYIPEIG-VIQFLLKNLYWTEdkk 171
Cdd:COG1647    97 LALLLAARYPD-VAGLVL--LSPALKIDDPSAPLLPL----LKY----------LARSLRGIGsDIEDPEVAEYAYD--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 172 lswRFNLHVLTDkYTTFVTNAVK-YGVYNGPVLFLAGANSNYILPQDGLLIRQQFPNSEVKKIA--NAGHWVQAENPKD- 247
Cdd:COG1647   157 ---RTPLRALAE-LQRLIREVRRdLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWleDSGHVITLDKDREe 232

                         250
                  ....*....|.
gi 1243381661 248 FNAAVKEFLTQ 258
Cdd:COG1647   233 VAEEILDFLER 243
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 58-258 8.31e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.98  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  58 SEEMTIDAMVNDVQVYMDYY----GLEKVYLLGHSLGGKVVMQYAITNPEKVEKL-----IVADMAPKAYPPHHQGIFKA 128
Cdd:PRK03592   67 SDKPDIDYTFADHARYLDAWfdalGLDDVVLVGHDWGSALGFDWAARHPDRVRGIafmeaIVRPMTWDDFPPAVRELFQA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661 129 L------------NSVDLNQV----TSRQEVEEELKKY-IPeigviqFLLKnlywtEDKKLSWRF-----------NLHV 180
Cdd:PRK03592  147 LrspgegeemvleENVFIERVlpgsILRPLSDEEMAVYrRP------FPTP-----ESRRPTLSWprelpidgepaDVVA 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243381661 181 LTDKYTTFVTNAvkygvyNGPVLFLAGANSNYILPQDGLLI-RQQFPNSEVKKIANAGHWVQAENPKDFNAAVKEFLTQ 258
Cdd:PRK03592  216 LVEEYAQWLATS------DVPKLLINAEPGAILTTGAIRDWcRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRR 288
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 18-121 1.75e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 39.11  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243381661  18 LLVFHGL---------FGMLDNWGSFGrefgelmpVHLIDLRNHGKS--FHSEEMTIDAMVNDVQVYMDYYGLEK----V 82
Cdd:PLN02652  139 LIIIHGLnehsgrylhFAKQLTSCGFG--------VYAMDWIGHGGSdgLHGYVPSLDYVVEDTEAFLEKIRSENpgvpC 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1243381661  83 YLLGHSLGGKVVMQyAITNPE---KVEKLIVADMAPKAYPPH 121
Cdd:PLN02652  211 FLFGHSTGGAVVLK-AASYPSiedKLEGIVLTSPALRVKPAH 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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