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Conserved domains on  [gi|652339381|ref|WP_026736591|]
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alpha/beta fold hydrolase [Fischerella sp. PCC 9605]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 17-270 1.98e-46

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: 154.77  E-value: 1.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  17 LFWREVG-EGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYL 95
Cdd:COG0596   14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLERVVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  96 VGHSLGGWIASTYALKYPEQIYGLVLlapegveveeldkvwknmqslvklplwvfkilrllrpltqilgldkkIEQAWQQ 175
Cdd:COG0596   94 VGHSMGGMVALELAARHPERVAGLVL-----------------------------------------------VDEVLAA 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 176 RQLMLQYPTASQLLFLRQLPEIRAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIPQAELKIIAHGEHNLPEIC 255
Cdd:COG0596  127 LAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQ 206

                        250
                 ....*....|....*
gi 652339381 256 AAIVAEDIRDFIKGV 270
Cdd:COG0596  207 PEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 17-270 1.98e-46

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: 154.77  E-value: 1.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  17 LFWREVG-EGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYL 95
Cdd:COG0596   14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLERVVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  96 VGHSLGGWIASTYALKYPEQIYGLVLlapegveveeldkvwknmqslvklplwvfkilrllrpltqilgldkkIEQAWQQ 175
Cdd:COG0596   94 VGHSMGGMVALELAARHPERVAGLVL-----------------------------------------------VDEVLAA 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 176 RQLMLQYPTASQLLFLRQLPEIRAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIPQAELKIIAHGEHNLPEIC 255
Cdd:COG0596  127 LAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQ 206

                        250
                 ....*....|....*
gi 652339381 256 AAIVAEDIRDFIKGV 270
Cdd:COG0596  207 PEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 27-251 1.70e-29

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: 111.44  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   27 PVILLHGAWNDSSQWVSVMESLSQN-FHCFAPDFFGFGESD-YPNIH-YSIDLQVESLAELIHALKLEKVYLVGHSLGGW 103
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSrPKAQDdYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  104 IASTYALKYPEQIYGLVLLAP--EGVEVEELDKVWKN-----MQSLV-------KLPLWVFKILRLLRPLTQILGLDKKI 169
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAldPPHELDEADRFILAlfpgfFDGFVadfapnpLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  170 EQAWQQRQLMLQYPTASQLLFLRQLPeirAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIPQAELKIIAHGEH 249
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLFIETWS---TELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ..
gi 652339381  250 NL 251
Cdd:pfam00561 239 FA 240
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 19-272 2.07e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 90.82  E-value: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  19 WREVGEGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYLVGH 98
Cdd:PRK03592  21 YIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLDDVVLVGH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  99 SLGGWIASTYALKYPEQIYGLVLlapegveveeldkvwknMQSLVKLPLW------VFKILRLLRplTQILG----LDKK 168
Cdd:PRK03592 101 DWGSALGFDWAARHPDRVRGIAF-----------------MEAIVRPMTWddfppaVRELFQALR--SPGEGeemvLEEN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 169 --IEQAWQ---QRQL----MLQY----PTASQ----LLFLRQLP------------EIRAELL----QDKLMFLTVPVLI 215
Cdd:PRK03592 162 vfIERVLPgsiLRPLsdeeMAVYrrpfPTPESrrptLSWPRELPidgepadvvalvEEYAQWLatsdVPKLLINAEPGAI 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 652339381 216 LqgGKDSLDALAKSNsyarvIPQAELKIIAHGEHNLPEICAAIVAEDIRDFIKGVSG 272
Cdd:PRK03592 242 L--TTGAIRDWCRSW-----PNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRRLRL 291
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 21-147 2.36e-16

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 77.04  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   21 EVGEGIPVILLHGAWNDSSQWVSVMESLSQ--NFHCFAPDFFGFGESDYPNIH----YSIDLQVESLAELIHALKLEKVY 94
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSdeelWTIDYFVDELEEVREKLGLDKFY 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 652339381   95 LVGHSLGGWIASTYALKYPEQIYGLVLLAPegveVEELDKVWKNMQSLVK-LPL 147
Cdd:TIGR01250 101 LLGHSWGGMLAQEYALKYGQHLKGLIISSM----LDSAPEYVKELNRLRKeLPP 150
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 28-119 1.10e-03

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 39.53  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGaWNDSSQ--WVSVMES--LSQ-NFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALK------LEKVYLV 96
Cdd:cd00707   39 RFIIHG-WTSSGEesWISDLRKayLSRgDYNVIVVDWGRGANPNYPQAVNNTRVVGAELAKFLDFLVdntglsLENVHLI 117

                         90       100
                 ....*....|....*....|....*..
gi 652339381  97 GHSLGGWIAStYALKY----PEQIYGL 119
Cdd:cd00707  118 GHSLGAHVAG-FAGKRlngkLGRITGL 143
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 17-270 1.98e-46

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: 154.77  E-value: 1.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  17 LFWREVG-EGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYL 95
Cdd:COG0596   14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLERVVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  96 VGHSLGGWIASTYALKYPEQIYGLVLlapegveveeldkvwknmqslvklplwvfkilrllrpltqilgldkkIEQAWQQ 175
Cdd:COG0596   94 VGHSMGGMVALELAARHPERVAGLVL-----------------------------------------------VDEVLAA 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 176 RQLMLQYPTASQLLFLRQLPEIRAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIPQAELKIIAHGEHNLPEIC 255
Cdd:COG0596  127 LAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQ 206

                        250
                 ....*....|....*
gi 652339381 256 AAIVAEDIRDFIKGV 270
Cdd:COG0596  207 PEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 27-251 1.70e-29

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: 111.44  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   27 PVILLHGAWNDSSQWVSVMESLSQN-FHCFAPDFFGFGESD-YPNIH-YSIDLQVESLAELIHALKLEKVYLVGHSLGGW 103
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSrPKAQDdYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  104 IASTYALKYPEQIYGLVLLAP--EGVEVEELDKVWKN-----MQSLV-------KLPLWVFKILRLLRPLTQILGLDKKI 169
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAldPPHELDEADRFILAlfpgfFDGFVadfapnpLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  170 EQAWQQRQLMLQYPTASQLLFLRQLPeirAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIPQAELKIIAHGEH 249
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLFIETWS---TELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ..
gi 652339381  250 NL 251
Cdd:pfam00561 239 FA 240
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
27-268 1.05e-28

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 108.94  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  27 PVILLHGAWNDSSQWVSVMESLSQN-FHCFAPDFFGFGESDYPNIHY-SIDLQVESLAELIHALKLE---KVYLVGHSLG 101
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRARpglPVVLLGHSMG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 102 GWIASTYALKYPEQIYGLVLLAPEgveveeldkvwknmqsLVKLPLWvfkilrllrpltqilgldkkieqawqqrqlmlq 181
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLLAPA----------------YRADPLL--------------------------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 182 YPTASQLLFLRqlpeiraelLQDKLMFLTVPVLILQGGKDSLDALAKSNS-YARVIPQAELKIIAHGEHNLP-EICAAIV 259
Cdd:COG2267  141 GPSARWLRALR---------LAEALARIDVPVLVLHGGADRVVPPEAARRlAARLSPDVELVLLPGARHELLnEPAREEV 211


                 ....*....
gi 652339381 260 AEDIRDFIK 268
Cdd:COG2267  212 LAAILAWLE 220
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 28-249 6.01e-23

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: 93.82  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   28 VILLHGAwNDSSQWVS-VMESLSQN-FHCFAPDFFGFGESDYPNIHY-SIDLQVESLAELIHALKLE----KVYLVGHSL 100
Cdd:pfam12146   7 VVLVHGL-GEHSGRYAhLADALAAQgFAVYAYDHRGHGRSDGKRGHVpSFDDYVDDLDTFVDKIREEhpglPLFLLGHSM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  101 GGWIASTYALKYPEQIYGLVLLAPegveveeldKVWKNMQSLVKLPLWVFKILRLLRPLTQILG-LDKKIEQAWQQRQ-- 177
Cdd:pfam12146  86 GGLIAALYALRYPDKVDGLILSAP---------ALKIKPYLAPPILKLLAKLLGKLFPRLRVPNnLLPDSLSRDPEVVaa 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 652339381  178 -----LMLQYPTASQLLFLRQLpeirAELLQDKLMFLTVPVLILQGGKDSLDALAKSNSYARVIP--QAELKIIAHGEH 249
Cdd:pfam12146 157 yaadpLVHGGISARTLYELLDA----GERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGstDKTLKLYPGLYH 231
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 19-272 2.07e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 90.82  E-value: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  19 WREVGEGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYLVGH 98
Cdd:PRK03592  21 YIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHARYLDAWFDALGLDDVVLVGH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  99 SLGGWIASTYALKYPEQIYGLVLlapegveveeldkvwknMQSLVKLPLW------VFKILRLLRplTQILG----LDKK 168
Cdd:PRK03592 101 DWGSALGFDWAARHPDRVRGIAF-----------------MEAIVRPMTWddfppaVRELFQALR--SPGEGeemvLEEN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 169 --IEQAWQ---QRQL----MLQY----PTASQ----LLFLRQLP------------EIRAELL----QDKLMFLTVPVLI 215
Cdd:PRK03592 162 vfIERVLPgsiLRPLsdeeMAVYrrpfPTPESrrptLSWPRELPidgepadvvalvEEYAQWLatsdVPKLLINAEPGAI 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 652339381 216 LqgGKDSLDALAKSNsyarvIPQAELKIIAHGEHNLPEICAAIVAEDIRDFIKGVSG 272
Cdd:PRK03592 242 L--TTGAIRDWCRSW-----PNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRRLRL 291
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
28-272 9.49e-19

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 82.68  E-value: 9.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWVSVMESL-SQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKL--EKVYLVGHSLGGWI 104
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLAEALaKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAgyDKVIVIGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 105 ASTYALKYPEqIYGLVLLAPegveveeldkvwknmqsLVKLPLWVFKILRLLRPLT-QILGLDKKIEQAWQQRQLMLQYP 183
Cdd:COG1647   98 ALLLAARYPD-VAGLVLLSP-----------------ALKIDDPSAPLLPLLKYLArSLRGIGSDIEDPEVAEYAYDRTP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 184 TAS--QLLFLRQlpEIRAELLQdklmfLTVPVLILQGGKDslDALAKSNS---YARVI-PQAELKIIAHGEHNLP-EICA 256
Cdd:COG1647  160 LRAlaELQRLIR--EVRRDLPK-----ITAPTLIIQSRKD--EVVPPESAryiYERLGsPDKELVWLEDSGHVITlDKDR 230

                        250
                 ....*....|....*.
gi 652339381 257 AIVAEDIRDFIKGVSG 272
Cdd:COG1647  231 EEVAEEILDFLERLAA 246
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 21-147 2.36e-16

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 77.04  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   21 EVGEGIPVILLHGAWNDSSQWVSVMESLSQ--NFHCFAPDFFGFGESDYPNIH----YSIDLQVESLAELIHALKLEKVY 94
Cdd:TIGR01250  21 GEGEKIKLLLLHGGPGMSHEYLENLRELLKeeGREVIMYDQLGCGYSDQPDDSdeelWTIDYFVDELEEVREKLGLDKFY 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 652339381   95 LVGHSLGGWIASTYALKYPEQIYGLVLLAPegveVEELDKVWKNMQSLVK-LPL 147
Cdd:TIGR01250 101 LLGHSWGGMLAQEYALKYGQHLKGLIISSM----LDSAPEYVKELNRLRKeLPP 150
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 28-258 4.84e-16

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 74.82  E-value: 4.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   28 VILLHGAWNDSSQWVsvmESLSQNFHCFAPDFFGFGESDYPNIHYSidlQVESLAELIHALK-LEKVYLVGHSLGGWIAS 106
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGaARPVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  107 TYALKYPEQiygLVLLAPEGVEVEELDKVWKNMQSLvkLPLWVFKILRLLRPLTQILGLDKKIEQAWQQRqlmlqyptas 186
Cdd:pfam12697  75 AAAAAALVV---GVLVAPLAAPPGLLAALLALLARL--GAALAAPAWLAAESLARGFLDDLPADAEWAAA---------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 652339381  187 qLLFLRQLPEIRAELLQDKLMFLTVPVLILQGGKDSLDALAKsnSYARVIPQAELKIIAHGEHNL---PEICAAI 258
Cdd:pfam12697 140 -LARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQ--RLLAALAGARLVVLPGAGHLPlddPEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 15-127 2.66e-15

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 74.60  E-value: 2.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  15 GLLFWREVGE--GIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEK 92
Cdd:PRK14875 119 RTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIER 198

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 652339381  93 VYLVGHSLGGWIASTYALKYPEQIYGLVLLAPEGV 127
Cdd:PRK14875 199 AHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGL 233
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 27-134 4.65e-14

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 71.48  E-value: 4.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  27 PVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYP-----NIHYSIDLQVESLAELIHALKLEKVYLVGHSLG 101
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPdftckSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFG 186

                         90       100       110
                 ....*....|....*....|....*....|...
gi 652339381 102 GWIASTYALKYPEQIYGLVLLAPEGVEVEELDK 134
Cdd:PLN02894 187 GYVAAKYALKHPEHVQHLILVGPAGFSSESDDK 219
PLN02578 PLN02578
hydrolase
 23-126 1.11e-13

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 69.87  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  23 GEGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALKLEKVYLVGHSLGG 102
Cdd:PLN02578  84 GEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGG 163

                         90       100
                 ....*....|....*....|....
gi 652339381 103 WIASTYALKYPEQIYGLVLLAPEG 126
Cdd:PLN02578 164 FTALSTAVGYPELVAGVALLNSAG 187
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 27-124 1.26e-12

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 62.54  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  27 PVILLHGAWNDSSQWVSVMESL-SQNFHCFAPDffgfgesdYPNIHYSIDLQVESLAELIHALK----LEKVYLVGHSLG 101
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLrAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAVLaatgAEKVDLVGHSMG 78

                         90       100
                 ....*....|....*....|....*
gi 652339381 102 GWIASTYA--LKYPEQIYGLVLLAP 124
Cdd:COG1075   79 GLVARYYLkrLGGAAKVARVVTLGT 103
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 13-121 4.76e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 64.49  E-value: 4.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  13 SQGLLFWREVGEGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPN-IHYSIDLQVESLAELIHALKLE 91
Cdd:PRK03204  22 SRGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSgFGYQIDEHARVIGEFVDHLGLD 101

                         90       100       110
                 ....*....|....*....|....*....|
gi 652339381  92 KVYLVGHSLGGWIASTYALKYPEQIYGLVL 121
Cdd:PRK03204 102 RYLSMGQDWGGPISMAVAVERADRVRGVVL 131
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 11-124 7.01e-12

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 64.90  E-value: 7.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  11 KLSQGLLFWREVGEGI----PVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYP----NIHYSIDLQVESLA 82
Cdd:PLN03084 109 QASSDLFRWFCVESGSnnnpPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPqpgyGFNYTLDEYVSSLE 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 652339381  83 ELIHALKLEKVYLVGHSLGGWIASTYALKYPEQIYGLVLLAP 124
Cdd:PLN03084 189 SLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLILLNP 230
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
14-268 6.01e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.80  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  14 QGLLFWREVGEGIPVILL-HGA-WNDSSQWVSVMESLSQN-FHCFAPDFFGFGESDYPNIHYSIDLQVESLAELI--HAL 88
Cdd:COG1506   11 PGWLYLPADGKKYPVVVYvHGGpGSRDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYLAarPYV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  89 KLEKVYLVGHSLGGWIASTYALKYPEQIYGLVLLAPegveveeldkVWkNMQSLVKLPLWVFKILrllrpltqilgldkk 168
Cdd:COG1506   91 DPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG----------VS-DLRSYYGTTREYTERL--------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 169 IEQAWQQRQLMLQYptaSQLLFLRQlpeiraellqdklmfLTVPVLILQGGKDSL----------DALAKSNsyarviPQ 238
Cdd:COG1506  145 MGGPWEDPEAYAAR---SPLAYADK---------------LKTPLLLIHGEADDRvppeqaerlyEALKKAG------KP 200

                        250       260       270
                 ....*....|....*....|....*....|
gi 652339381 239 AELKIIAHGEHNLPEICAAIVAEDIRDFIK 268
Cdd:COG1506  201 VELLVYPGEGHGFSGAGAPDYLERILDFLD 230
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 20-123 3.83e-10

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 60.26  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   20 REVGEGIP---VILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPN--------IHYSIDLQVESLAELIHAL 88
Cdd:PLN02980 1363 HEVGQNAEgsvVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNhaketqtePTLSVELVADLLYKLIEHI 1442

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 652339381   89 KLEKVYLVGHSLGGWIASTYALKYPEQIYGLVLLA 123
Cdd:PLN02980 1443 TPGKVTLVGYSMGARIALYMALRFSDKIEGAVIIS 1477
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 28-124 1.55e-08

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 54.81  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWV-----SVMESLSQNFHCFAPDFFGFGESDYPNIH-YSIDLQVESLAE-LIHALKLEKVYLVGHSL 100
Cdd:PLN03087 204 VLFIHGFISSSAFWTetlfpNFSDAAKSTYRLFAVDLLGFGRSPKPADSlYTLREHLEMIERsVLERYKVKSFHIVAHSL 283

                         90       100
                 ....*....|....*....|....
gi 652339381 101 GGWIASTYALKYPEQIYGLVLLAP 124
Cdd:PLN03087 284 GCILALALAVKHPGAVKSLTLLAP 307
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
17-123 3.05e-08

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 53.10  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  17 LFWREVGEG-IPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIhysidLQVESLAELIHALKLEKVYL 95
Cdd:PRK10349   4 IWWQTKGQGnVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGA-----LSLADMAEAVLQQAPDKAIW 78

                         90       100
                 ....*....|....*....|....*...
gi 652339381  96 VGHSLGGWIASTYALKYPEQIYGLVLLA 123
Cdd:PRK10349  79 LGWSLGGLVASQIALTHPERVQALVTVA 106
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 23-120 1.49e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 48.43  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  23 GEGIPVILLHG--AWndSSQWVSVMESLSQNFH-CFAPDFFGFGESDYP-NIH-YSIDLQVESLAELIHALKLEKVYLVG 97
Cdd:PRK00870  44 ADGPPVLLLHGepSW--SYLYRKMIPILAAAGHrVIAPDLIGFGRSDKPtRREdYTYARHVEWMRSWFEQLDLTDVTLVC 121

                         90       100
                 ....*....|....*....|...
gi 652339381  98 HSLGGWIASTYALKYPEQIYGLV 120
Cdd:PRK00870 122 QDWGGLIGLRLAAEHPDRFARLV 144
YpfH COG0400
Predicted esterase [General function prediction only];
28-124 1.52e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 47.59  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWVSVMESLSQ-NFHCFAPD-----------FFGFGESDYPNIHYSIDLQVESLAELIHALK------ 89
Cdd:COG0400    8 VVLLHGYGGDEEDLLPLAPELALpGAAVLAPRapvpegpggraWFDLSFLEGREDEEGLAAAAEALAAFIDELEarygid 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 652339381  90 LEKVYLVGHSLGGWIASTYALKYPEQIYGLVLLAP 124
Cdd:COG0400   88 PERIVLAGFSQGAAMALSLALRRPELLAGVVALSG 122
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 20-122 1.77e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 48.20  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  20 REVGEGIPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYPNIH-------YSIDLQVESLAELIHALKLEK 92
Cdd:PLN02824  24 RAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRsappnsfYTFETWGEQLNDFCSDVVGDP 103

                         90       100       110
                 ....*....|....*....|....*....|
gi 652339381  93 VYLVGHSLGGWIASTYALKYPEQIYGLVLL 122
Cdd:PLN02824 104 AFVICNSVGGVVGLQAAVDAPELVRGVMLI 133
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 19-124 4.43e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 47.08  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  19 WREVGEGIP---VILLHGAWNDSSqWV--SVMESLSQ-NFHCFAPDFFGFGESD-----YPNIhysiDLQVESLAELIHA 87
Cdd:PLN02298  50 WLPSSSSPPralIFMVHGYGNDIS-WTfqSTAIFLAQmGFACFALDLEGHGRSEglrayVPNV----DLVVEDCLSFFNS 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 652339381  88 LKLEKVY------LVGHSLGGWIASTYALKYPEQIYGLVLLAP 124
Cdd:PLN02298 125 VKQREEFqglprfLYGESMGGAICLLIHLANPEGFDGAVLVAP 167
COG4099 COG4099
Predicted peptidase [General function prediction only];
21-150 4.65e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.50  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  21 EVGEGIPVILLHGAWNdssqWVSVMESLSQNFHCFAPdffGFGESDYpnihYSIDLQVESLAELIHALKLE------KVY 94
Cdd:COG4099   60 ERGTDNEKQLTHGAPK----FINPENQAKFPAIVLAP---QCPEDDY----WSDTKALDAVLALLDDLIAEyridpdRIY 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 652339381  95 LVGHSLGGWIASTYALKYPEQIYGLVLLAPEGVEveeldkvwKNMQSLVKLPLWVF 150
Cdd:COG4099  129 LTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDP--------ANAANLKKVPVWIF 176
PRK10673 PRK10673
esterase;
26-136 6.65e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 46.26  E-value: 6.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  26 IPVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDY-PNIHYSIDLQveSLAELIHALKLEKVYLVGHSLGGWI 104
Cdd:PRK10673  17 SPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRdPVMNYPAMAQ--DLLDTLDALQIEKATFIGHSMGGKA 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 652339381 105 ASTYALKYPEQIYGLVLL--APEGVEVEELDKVW 136
Cdd:PRK10673  95 VMALTALAPDRIDKLVAIdiAPVDYHVRRHDEIF 128
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 27-122 6.09e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.68  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  27 PVILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFGESDYP-NIHYSIdlqvESLAELIHALkLEKVY-----LVGHSL 100
Cdd:PLN02679  90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPpGFSYTM----ETWAELILDF-LEEVVqkptvLIGNSV 164

                         90       100
                 ....*....|....*....|....*
gi 652339381 101 GGW---IASTYAlkYPEQIYGLVLL 122
Cdd:PLN02679 165 GSLacvIAASES--TRDLVRGLVLL 187
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
198-272 1.92e-04

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 41.40  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381 198 RAELLQDklmfLTVPVLILQGGKDSLDALAKSNSYArVIPQAELKIIAHGEHNL---------PEICAAIVAEDIRDFIK 268
Cdd:COG3571  124 RTEHLAD----LTVPTLIVQGERDPFGTPEEVAGYP-LPPAIELVWLPGGDHDLkprkrsgrtQEDHLAAAADAVAAWLA 198


                 ....
gi 652339381 269 GVSG 272
Cdd:COG3571  199 RLLR 202
YcfP COG3150
Predicted esterase YcpF, UPF0227 family [General function prediction only];
68-124 2.28e-04

Predicted esterase YcpF, UPF0227 family [General function prediction only];


Pssm-ID: 442384 [Multi-domain]  Cd Length: 190  Bit Score: 40.90  E-value: 2.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 652339381  68 PNIHYSIDLQVESLAELIHALKLEKVYLVGHSLGG----WIASTYALKypeqiygLVLLAP 124
Cdd:COG3150   37 PQLPPSPAAAIAQLEALIAGLPGEPLALIGSSLGGfyatWLAERYGLR-------AVLINP 90
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 28-126 4.05e-04

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 40.59  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWVSVMESLsQNFHCFAPDFFGFGESdyPNIH-YSIDLQVESLAELIHALKLEKVYLVGHSLGGWIAS 106
Cdd:PRK11126   5 LVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGS--AAISvDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAM 81

                         90       100
                 ....*....|....*....|.
gi 652339381 107 TYAL-KYPEQIYGLVLlapEG 126
Cdd:PRK11126  82 YYACqGLAGGLCGLIV---EG 99
YdeN COG3545
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
29-124 4.14e-04

Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];


Pssm-ID: 442766 [Multi-domain]  Cd Length: 170  Bit Score: 40.22  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  29 ILLHGaWNDSSQ--WVSVMESLSQNFHCFAPDffgfgESDYPNIhysiDLQVESLAELIHALKlEKVYLVGHSLGGWIAS 106
Cdd:COG3545    1 LIVPG-LGGSGPdhWQSWWERELPTVRRVEQP-----DWDRPDL----DDWLAALDAAVAAAD-GPVVLVAHSLGCLAVA 69

                         90
                 ....*....|....*...
gi 652339381 107 TYALKYPEQIYGLVLLAP 124
Cdd:COG3545   70 HWAARLPRKVAGALLVAP 87
PRK05855 PRK05855
SDR family oxidoreductase;
24-107 5.17e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 41.12  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  24 EGIPVILLHGaWNDSSQ-WVSVMESLSQNFHCFAPDFFGFGESDYPN--IHYSIDLQVESLAELIHAL-KLEKVYLVGH- 98
Cdd:PRK05855  24 DRPTVVLVHG-YPDNHEvWDGVAPLLADRFRVVAYDVRGAGRSSAPKrtAAYTLARLADDFAAVIDAVsPDRPVHLLAHd 102

                         90
                 ....*....|.
gi 652339381  99 --SLGGWIAST 107
Cdd:PRK05855 103 wgSIQGWEAVT 113
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 28-119 1.10e-03

Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 39.53  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGaWNDSSQ--WVSVMES--LSQ-NFHCFAPDFFGFGESDYPNIHYSIDLQVESLAELIHALK------LEKVYLV 96
Cdd:cd00707   39 RFIIHG-WTSSGEesWISDLRKayLSRgDYNVIVVDWGRGANPNYPQAVNNTRVVGAELAKFLDFLVdntglsLENVHLI 117

                         90       100
                 ....*....|....*....|....*..
gi 652339381  97 GHSLGGWIAStYALKY----PEQIYGL 119
Cdd:cd00707  118 GHSLGAHVAG-FAGKRlngkLGRITGL 143
Abhydrolase_5 pfam12695
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ...
 89-134 1.21e-03

Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase enzymes.


Pssm-ID: 315383 [Multi-domain]  Cd Length: 164  Bit Score: 38.59  E-value: 1.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 652339381   89 KLEKVYLVGHSLGGWIASTYALKYpEQIYGLVLLA--PEGVEVEELDK 134
Cdd:pfam12695  55 KIQKWVVGGHSLGGVMASRFAADN-ELIKGVVFLAsyPDKDSLSNLSF 101
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
28-132 2.11e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.41  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWVSVMESL-SQNFHCFAPDFFGFGESDYPN-------IHYSIDLQVESLAELIHALK------LEKV 93
Cdd:COG0412   32 VVVLHEIFGLNPHIRDVARRLaAAGYVVLAPDLYGRGGPGDDPdearalmGALDPELLAADLRAALDWLKaqpevdAGRV 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 652339381  94 YLVGHSLGGWIASTYALKYPEQ-----IYGLVLLAPEGVEVEEL 132
Cdd:COG0412  112 GVVGFCFGGGLALLAAARGPDLaaavsFYGGLPADDLLDLAARI 155
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
18-164 2.82e-03

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 38.33  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  18 FWREVGEGIPVILLHGA-------WNDSSQWVSvmeslSQNFHCFAPDFFGFGES---DYPNIHYSI-DLQVESLAELIH 86
Cdd:COG4757   24 LFPPAGPPRAVVLINPAtgvpqrfYRPFARYLA-----ERGFAVLTYDYRGIGLSrpgSLRGFDAGYrDWGELDLPAVLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  87 ALKLE----KVYLVGHSLGGWIASTYAlkYPEQIYGLVLLAPEGVeveeldkVWKNMQSLVKLPLWVFkiLRLLRPL-TQ 161
Cdd:COG4757   99 ALRARfpglPLLLVGHSLGGQLLGLAP--NAERVDRLVTVASGSG-------YWRDYPPRRRLKVLLF--WHLLGPLlTR 167


                 ...
gi 652339381 162 ILG 164
Cdd:COG4757  168 LLG 170
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 95-127 3.06e-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: 214007  Cd Length: 309  Bit Score: 38.38  E-value: 3.06e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 652339381  95 LVGHSLGGWIASTYALKYPEQIYGLVLLAPEGV 127
Cdd:cd12808  192 VVAHSQGGGFAFEAARARPDLVRAVVALEPSGA 224
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
 45-124 3.79e-03

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 38.04  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   45 MESLSQNFHCFAP----DFFGFGESDYPNIH-----YSIDLQVESLAELIHAL------KLEKVYLVGHSLGGWIASTYA 109
Cdd:pfam10230  22 LSLLYEKLNPTFDvlgiSHAGHSLEDRNDAKengrvFSLQDQIEHKIDFIRAFlpansdKDVKLILIGHSIGAYIALEVL 101

                          90
                  ....*....|....*.
gi 652339381  110 LKYPE-QIYGLVLLAP 124
Cdd:pfam10230 102 KRLSErGIIKCVLLFP 117
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 45-124 3.93e-03

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 38.10  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   45 MESLSQNFhCF-----------APDFFGfgesDYPniHYSIDLQVESLAELIHALKLEKVYLVGHSLGGWIASTYALKYP 113
Cdd:pfam03096  49 MQEILENF-CIyhvdapgqedgAASFPG----GYP--YPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHP 121

                          90
                  ....*....|.
gi 652339381  114 EQIYGLVLLAP 124
Cdd:pfam03096 122 ERVEGLVLINP 132
Lipase_3 pfam01764
Lipase (class 3);
36-106 5.68e-03

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 36.47  E-value: 5.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 652339381   36 NDSSQWVSVMESLSQNFHCFAPD----FFGFGESdYPNIHYSIdlqVESLAELIHALKLEKVYLVGHSLGGWIAS 106
Cdd:pfam01764   8 NSILDWLTDFDFSLTPFKDFFLGggkvHSGFLSA-YTSVREQV---LAELKRLLEKYPDYSIVVTGHSLGGALAS 78
DUF676 pfam05057
Putative serine esterase (DUF676); This family of proteins are probably serine esterase type ...
 28-128 9.07e-03

Putative serine esterase (DUF676); This family of proteins are probably serine esterase type enzymes with an alpha/beta hydrolase fold.


Pssm-ID: 309968  Cd Length: 212  Bit Score: 36.70  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381   28 VILLHGAWNDSSQWVSVMESLSQNFHCFAPDFFGFgESDYPNIHYSIDLQVESLAELI-----HALKLEKVYLVGHSLGG 102
Cdd:pfam05057   8 VVLVHGLWGNSADMEYVAEQLEKKLPDELIVFLMS-SNNVSKTFKGIDVMGERLANEVlefvqDGSDGKKISFVGHSLGG 86

                          90       100
                  ....*....|....*....|....*.
gi 652339381  103 WIAsTYALKYPEQIYGLVLLAPEGVE 128
Cdd:pfam05057  87 LIA-RYAIGKLYDKAMTFKGFFKGLE 111
PHA02857 PHA02857
monoglyceride lipase; Provisional
 28-124 9.36e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 36.79  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652339381  28 VILLHGAWNDSSQWVSVMESLSQ-NFHCFAPDFFGFGESDYPNIHY-SIDLQVESLAELIHALKLE----KVYLVGHSLG 101
Cdd:PHA02857  28 VFISHGAGEHSGRYEELAENISSlGILVFSHDHIGHGRSNGEKMMIdDFGVYVRDVVQHVVTIKSTypgvPVFLLGHSMG 107

                         90       100
                 ....*....|....*....|...
gi 652339381 102 GWIASTYALKYPEQIYGLVLLAP 124
Cdd:PHA02857 108 ATISILAAYKNPNLFTAMILMSP 130
 
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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