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Conserved domains on  [gi|489294630|ref|WP_003202149|]
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alpha/beta fold hydrolase [Pseudomonas brassicacearum]

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, ...
 72-340 8.00e-38

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: 134.74  E-value: 8.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  72 NGRTVVLMHGKNFCAATWGDSIKVLSEaGYRVIAADQVGFCTSSKPEHyQYSFQQLASNTQALLKALGVQKAVLLGHSTG 151
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAG-GYTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 152 GMLATRYALQFADEVERLAMVNpigledwkalgvpyrtvdqwyarelkvnaEGIRNYERTTYYAGRWEPEFERWVDMLAG 231
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAPEALAALLRALAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 232 LNkgpghtqvawnsaliydmiftqpVYYEFKDLTVPTLLLIGTSDttaigsDIAPPAVkatlghyevlGKQAARLIPRST 311
Cdd:COG0596  151 TD-----------------------LRERLARITVPTLVIWGEKD------PIVPPAL----------ARRLAELLPNAE 191

                        250       260
                 ....*....|....*....|....*....
gi 489294630 312 LVEFPNLGHAPQMEEPDRFHKALLSWLDK 340
Cdd:COG0596  192 LVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 72-340 8.00e-38

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: 134.74  E-value: 8.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  72 NGRTVVLMHGKNFCAATWGDSIKVLSEaGYRVIAADQVGFCTSSKPEHyQYSFQQLASNTQALLKALGVQKAVLLGHSTG 151
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAG-GYTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 152 GMLATRYALQFADEVERLAMVNpigledwkalgvpyrtvdqwyarelkvnaEGIRNYERTTYYAGRWEPEFERWVDMLAG 231
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAPEALAALLRALAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 232 LNkgpghtqvawnsaliydmiftqpVYYEFKDLTVPTLLLIGTSDttaigsDIAPPAVkatlghyevlGKQAARLIPRST 311
Cdd:COG0596  151 TD-----------------------LRERLARITVPTLVIWGEKD------PIVPPAL----------ARRLAELLPNAE 191

                        250       260
                 ....*....|....*....|....*....
gi 489294630 312 LVEFPNLGHAPQMEEPDRFHKALLSWLDK 340
Cdd:COG0596  192 LVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 75-327 6.07e-22

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: 92.95  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   75 TVVLMHGKNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSKPEH-YQYSFQQLASNTQALLKALGVQKAVLLGHSTGGM 153
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  154 LATRYALQFADEVERLAMVNPIglEDWKALGVPYRTVDQWYARELKVNAEGIRNYERTTYYA-------GRWEPEFE--- 223
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAkllalllLRLRLLKAlpl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  224 ----RWVDMLAgLNKGPGHTQVAWNSALIYDmiftqPVYYEFKDLTVPTLLLIGTSDTtaigsdIAPPAVKATLghyevl 299
Cdd:pfam00561 160 lnkrFPSGDYA-LAKSLVTGALLFIETWSTE-----LRAKFLGRLDEPTLIIWGDQDP------LVPPQALEKL------ 221

                         250       260
                  ....*....|....*....|....*...
gi 489294630  300 gkqaARLIPRSTLVEFPNLGHAPQMEEP 327
Cdd:pfam00561 222 ----AQLFPNARLVVIPDAGHFAFLEGP 245
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 68-339 2.14e-15

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: 75.49  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   68 QGKVNGRTVVLMHGKNFCAATWGDSIKVLS-EAGYRVIAADQVGFCTSSKPEH-------YQYSFQQLAsntqALLKALG 139
Cdd:TIGR01250  20 GGEGEKIKLLLLHGGPGMSHEYLENLRELLkEEGREVIMYDQLGCGYSDQPDDsdeelwtIDYFVDELE----EVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  140 VQKAVLLGHSTGGMLATRYALQFADEVERLAMVNPIgledwkaLGVPYRTVDQWYARE-LKVNA-EGIRNYERTTYYAgr 217
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSML-------DSAPEYVKELNRLRKeLPPEVrAAIKRCEASGDYD-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  218 wEPEFERWVDMLAGLNKGPGHTQVAWNSALIYDMifTQPVY-----------------YEFKD----LTVPTLLLIGTSD 276
Cdd:TIGR01250 167 -NPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGG--NTNVYnimqgpneftitgnlkdWDITDklseIKVPTLLTVGEFD 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489294630  277 TtaigsdiAPPAVKATLGHyevlgkqaarLIPRSTLVEFPNLGHAPQMEEPDRFHKALLSWLD 339
Cdd:TIGR01250 244 T-------MTPEAAREMQE----------LIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 55-176 1.89e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 66.92  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  55 GQSLQMGYMDvpaQGKVNGRTVVLMHGKnfcaATWG----DSIKVLSEAGYRVIAADQVGFCTSSKP-EHYQYSFQQLAS 129
Cdd:PRK00870  31 GGPLRMHYVD---EGPADGPPVLLLHGE----PSWSylyrKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVE 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489294630 130 NTQALLKALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVN---PIG 176
Cdd:PRK00870 104 WMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANtglPTG 153
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 72-340 8.00e-38

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: 134.74  E-value: 8.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  72 NGRTVVLMHGKNFCAATWGDSIKVLSEaGYRVIAADQVGFCTSSKPEHyQYSFQQLASNTQALLKALGVQKAVLLGHSTG 151
Cdd:COG0596   22 DGPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAG-GYTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 152 GMLATRYALQFADEVERLAMVNpigledwkalgvpyrtvdqwyarelkvnaEGIRNYERTTYYAGRWEPEFERWVDMLAG 231
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVD-----------------------------EVLAALAEPLRRPGLAPEALAALLRALAR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 232 LNkgpghtqvawnsaliydmiftqpVYYEFKDLTVPTLLLIGTSDttaigsDIAPPAVkatlghyevlGKQAARLIPRST 311
Cdd:COG0596  151 TD-----------------------LRERLARITVPTLVIWGEKD------PIVPPAL----------ARRLAELLPNAE 191

                        250       260
                 ....*....|....*....|....*....
gi 489294630 312 LVEFPNLGHAPQMEEPDRFHKALLSWLDK 340
Cdd:COG0596  192 LVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 75-327 6.07e-22

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: 92.95  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   75 TVVLMHGKNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSKPEH-YQYSFQQLASNTQALLKALGVQKAVLLGHSTGGM 153
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  154 LATRYALQFADEVERLAMVNPIglEDWKALGVPYRTVDQWYARELKVNAEGIRNYERTTYYA-------GRWEPEFE--- 223
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAkllalllLRLRLLKAlpl 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  224 ----RWVDMLAgLNKGPGHTQVAWNSALIYDmiftqPVYYEFKDLTVPTLLLIGTSDTtaigsdIAPPAVKATLghyevl 299
Cdd:pfam00561 160 lnkrFPSGDYA-LAKSLVTGALLFIETWSTE-----LRAKFLGRLDEPTLIIWGDQDP------LVPPQALEKL------ 221

                         250       260
                  ....*....|....*....|....*...
gi 489294630  300 gkqaARLIPRSTLVEFPNLGHAPQMEEP 327
Cdd:pfam00561 222 ----AQLFPNARLVVIPDAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
73-340 2.64e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.45  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  73 GRTVVLMHGKNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSKPEHYQYSFQQLASNTQAL---LKALGVQKAVLLGHS 149
Cdd:COG2267   28 RGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAAldaLRARPGLPVVLLGHS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 150 TGGMLATRYALQFADEVERLAMVNPIGLEDwKALGVPYRTVDQWYARElkvnaegirnyerttyyagrwepeferwvdml 229
Cdd:COG2267  108 MGGLIALLYAARYPDRVAGLVLLAPAYRAD-PLLGPSARWLRALRLAE-------------------------------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 230 aglnkgpghtqvawnsaliydmiftqpvyyEFKDLTVPTLLLIGTSDTTaigsdIAPPAVKATlghyevlgkqAARLIPR 309
Cdd:COG2267  155 ------------------------------ALARIDVPVLVLHGGADRV-----VPPEAARRL----------AARLSPD 189

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489294630 310 STLVEFPNLGHAPQMEEP-DRFHKALLSWLDK 340
Cdd:COG2267  190 VELVLLPGARHELLNEPArEEVLAAILAWLER 221
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 68-339 2.14e-15

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: 75.49  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   68 QGKVNGRTVVLMHGKNFCAATWGDSIKVLS-EAGYRVIAADQVGFCTSSKPEH-------YQYSFQQLAsntqALLKALG 139
Cdd:TIGR01250  20 GGEGEKIKLLLLHGGPGMSHEYLENLRELLkEEGREVIMYDQLGCGYSDQPDDsdeelwtIDYFVDELE----EVREKLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  140 VQKAVLLGHSTGGMLATRYALQFADEVERLAMVNPIgledwkaLGVPYRTVDQWYARE-LKVNA-EGIRNYERTTYYAgr 217
Cdd:TIGR01250  96 LDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSML-------DSAPEYVKELNRLRKeLPPEVrAAIKRCEASGDYD-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  218 wEPEFERWVDMLAGLNKGPGHTQVAWNSALIYDMifTQPVY-----------------YEFKD----LTVPTLLLIGTSD 276
Cdd:TIGR01250 167 -NPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGG--NTNVYnimqgpneftitgnlkdWDITDklseIKVPTLLTVGEFD 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489294630  277 TtaigsdiAPPAVKATLGHyevlgkqaarLIPRSTLVEFPNLGHAPQMEEPDRFHKALLSWLD 339
Cdd:TIGR01250 244 T-------MTPEAAREMQE----------LIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFIR 289
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 75-325 1.40e-12

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: 66.47  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   75 TVVLMHGKNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSkPEH-YQYSFQQLASNTQALLKAL----GVQKAVLLGHS 149
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSD-GKRgHVPSFDDYVDDLDTFVDKIreehPGLPLFLLGHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  150 TGGMLATRYALQFADEVERLAMVNPigledwkALGVPYRTVDQWYARELKVNAEGIRNYERTTYYAGRWepeFERWVDML 229
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLILSAP-------ALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDS---LSRDPEVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  230 AGLNKGP---GHTQVAWNSALIYDMIFTQPvyyEFKDLTVPTLLLIGTSDTtaigsdIAPPAVkatlghyevlGKQAARL 306
Cdd:pfam12146 155 AAYAADPlvhGGISARTLYELLDAGERLLR---RAAAITVPLLLLHGGADR------VVDPAG----------SREFYER 215

                         250       260
                  ....*....|....*....|.
gi 489294630  307 IPRS--TLVEFPNLGHAPQME 325
Cdd:pfam12146 216 AGSTdkTLKLYPGLYHELLNE 236
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
72-340 1.59e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 66.50  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  72 NGRTVVLMHGknFCAAT-----WGDSikvLSEAGYRVIAADQVGFCTSskPEH-YQYSFQQLASNTQALLKAL--GVQKA 143
Cdd:COG1647   14 GRKGVLLLHG--FTGSPaemrpLAEA---LAKAGYTVYAPRLPGHGTS--PEDlLKTTWEDWLEDVEEAYEILkaGYDKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 144 VLLGHSTGGMLATRYALQFaDEVERLAMVNP-IGLEDWKALGVPYRtvdQWYARELKVNAEGIRNYERTTYYAGRWepef 222
Cdd:COG1647   87 IVIGLSMGGLLALLLAARY-PDVAGLVLLSPaLKIDDPSAPLLPLL---KYLARSLRGIGSDIEDPEVAEYAYDRT---- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 223 erWVDMLAGLNKgpghtqvawnsaliydmiFTQPVYYEFKDLTVPTLLLIGTSDttaigsDIAPPavkatlghyevlgkQ 302
Cdd:COG1647  159 --PLRALAELQR------------------LIREVRRDLPKITAPTLIIQSRKD------EVVPP--------------E 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489294630 303 AARLI------PRSTLVEFPNLGH-APQMEEPDRFHKALLSWLDK 340
Cdd:COG1647  199 SARYIyerlgsPDKELVWLEDSGHvITLDKDREEVAEEILDFLER 243
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 55-176 1.89e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 66.92  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  55 GQSLQMGYMDvpaQGKVNGRTVVLMHGKnfcaATWG----DSIKVLSEAGYRVIAADQVGFCTSSKP-EHYQYSFQQLAS 129
Cdd:PRK00870  31 GGPLRMHYVD---EGPADGPPVLLLHGE----PSWSylyrKMIPILAAAGHRVIAPDLIGFGRSDKPtRREDYTYARHVE 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489294630 130 NTQALLKALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVN---PIG 176
Cdd:PRK00870 104 WMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANtglPTG 153
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 76-174 5.50e-11

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 58.69  E-value: 5.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  76 VVLMHGkNFC-AATWGDSIKVLSEAGYRVIAADQvgfctSSKPEHYQYSFQQLASNTQALLKALGVQKAVLLGHSTGGML 154
Cdd:COG1075    8 VVLVHG-LGGsAASWAPLAPRLRAAGYPVYALNY-----PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLV 81

                         90       100
                 ....*....|....*....|...
gi 489294630 155 AtRYALQF---ADEVERLAMVNP 174
Cdd:COG1075   82 A-RYYLKRlggAAKVARVVTLGT 103
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 65-180 6.97e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 63.01  E-value: 6.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  65 VPAQGKVNGRTVVLMHG---------KNFCAATwgdsikvlseAGYRVIAADQVGFCTSSKPEHYQYSFQQLAS----NT 131
Cdd:PLN02894  97 VTFDSKEDAPTLVMVHGygasqgfffRNFDALA----------SRFRVIAIDQLGWGGSSRPDFTCKSTEETEAwfidSF 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489294630 132 QALLKALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVNPIGL----EDW 180
Cdd:PLN02894 167 EEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFssesDDK 219
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 69-177 3.15e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 57.65  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  69 GKVNGRTVVLMHGKNFCAATWGDSIKVLSeAGYRVIAADQVGFCTSSKpEHYQYSFQQLASNTQALLKALGVQKAVLLGH 148
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSK-AVGAGSLDELAAAVLAFLDALGIERAHLVGH 204

                         90       100
                 ....*....|....*....|....*....
gi 489294630 149 STGGMLATRYALQFADEVERLAMVNPIGL 177
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTLIAPAGL 233
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 59-180 1.54e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 55.00  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  59 QMGYMDvpaQGkvNGRTVVLMHGKNFCAATWGDSIKVLSEAGyRVIAADQVGFCTSSKPEhYQYSFQQLASNTQALLKAL 138
Cdd:PRK03592  18 RMAYIE---TG--EGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPD-IDYTFADHARYLDAWFDAL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489294630 139 GVQKAVLLGHSTGGMLATRYALQFADEVERLAM----VNPIGLEDW 180
Cdd:PRK03592  91 GLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFmeaiVRPMTWDDF 136
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 76-333 1.66e-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: 54.02  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   76 VVLMHGknfcAATWGDSIKVLSEAGYRVIAADQVGFCTSSKPEhyqYSFQQLASNTQALLKALGVQKAVLLGHSTGGMLA 155
Cdd:pfam12697   1 VVLVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPP---LDLADLADLAALLDELGAARPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  156 TRYAlqfADEVERLAMVNPIGLedwkALGVPYRTVDQWYARELKVNAEGIRNYERTTYYAGRWEPEFERWVDMLAGLNKg 235
Cdd:pfam12697  74 LAAA---AAALVVGVLVAPLAA----PPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  236 pghtqvawnsaliYDMIFTQPVYYEFKDLTVPTlLLIGTSDttaigsDIAPPAVkatlghyevlgKQAARLIPRSTLVEF 315
Cdd:pfam12697 146 -------------LLAALALLPLAAWRDLPVPV-LVLAEED------RLVPELA-----------QRLLAALAGARLVVL 194

                         250
                  ....*....|....*...
gi 489294630  316 PNLGHAPqMEEPDRFHKA 333
Cdd:pfam12697 195 PGAGHLP-LDDPEEVAEA 211
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 68-174 2.42e-07

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 51.81  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  68 QGKVNGRTVVLMHGknFC--AATWGDSIKVLSEaGYRVIAADQVGFCTSSKPEH---YQYSFQQLASNTQALLKALGVQK 142
Cdd:PLN03084 122 SGSNNNPPVLLIHG--FPsqAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQPgygFNYTLDEYVSSLESLIDELKSDK 198

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489294630 143 AVLLGHSTGGMLATRYALQFADEVERLAMVNP 174
Cdd:PLN03084 199 VSLVVQGYFSPPVVKYASAHPDKIKKLILLNP 230
PLN02578 PLN02578
hydrolase
 68-338 3.34e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 51.38  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  68 QGKvnGRTVVLMHGKNFCAATWGDSIKVLSEAgYRVIAADQVGFCTSSKPeHYQYSFQQLASNTQALLKALGVQKAVLLG 147
Cdd:PLN02578  83 QGE--GLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA-LIEYDAMVWRDQVADFVKEVVKEPAVLVG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 148 HSTGGMLATRYALQFADEVERLAMVNPIG-----LEDWKALGVPYRTVDQWYA-RELKvnaegirnyerttyyagRWepe 221
Cdd:PLN02578 159 NSLGGFTALSTAVGYPELVAGVALLNSAGqfgseSREKEEAIVVEETVLTRFVvKPLK-----------------EW--- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 222 FERWVDMLAGLN-KGPGHTQVAWNSALI---------YDMIfTQP--------VYYE-----------------FKDLTV 266
Cdd:PLN02578 219 FQRVVLGFLFWQaKQPSRIESVLKSVYKdksnvddylVESI-TEPaadpnageVYYRlmsrflfnqsrytldslLSKLSC 297

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489294630 267 PTLLLIGTSDTtaigsdIAPPAvKAtlghyevlgKQAARLIPRSTLVEFpNLGHAPQMEEPDRFHKALLSWL 338
Cdd:PLN02578 298 PLLLLWGDLDP------WVGPA-KA---------EKIKAFYPDTTLVNL-QAGHCPHDEVPEQVNKALLEWL 352
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 70-341 8.39e-07

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 51.01  E-value: 8.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   70 KVNGRTVVLMHGKNFCAATWGDSIKVLSEAGyRVIAAD-------QVGFCTSSKPEHYQYSFQQLASNTQALLKALGVQK 142
Cdd:PLN02980 1368 NAEGSVVLFLHGFLGTGEDWIPIMKAISGSA-RCISIDlpghggsKIQNHAKETQTEPTLSVELVADLLYKLIEHITPGK 1446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  143 AVLLGHSTGGMLATRYALQFADEVERLAMVN--PiGLEDWKALGVPYRTvDQWYARELKVNaeGIRNYERTTYYAGRWE- 219
Cdd:PLN02980 1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISgsP-GLKDEVARKIRSAK-DDSRARMLIDH--GLEIFLENWYSGELWKs 1522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  220 ----PEFERWVDMLAGlnkgpgHTQVAWNSALIYDM-IFTQ-PVYYEFKDLTVPTLLLIGTSDttAIGSDIAPPAVKATL 293
Cdd:PLN02980 1523 lrnhPHFNKIVASRLL------HKDVPSLAKLLSDLsIGRQpSLWEDLKQCDTPLLLVVGEKD--VKFKQIAQKMYREIG 1594

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 489294630  294 GHYEVLGKQAARLIprsTLVEFPNLGHAPQMEEPDRFHKALLSWLDKP 341
Cdd:PLN02980 1595 KSKESGNDKGKEII---EIVEIPNCGHAVHLENPLPVIRALRKFLTRL 1639
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 65-339 8.38e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 47.14  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  65 VPAQGKVNGRTVVLMHGKNFCAATWGDSIKVLSEAgYRVIAADQVGFCTSSKPEHYQYSFQQLASNTQALLKALGVQKAV 144
Cdd:PLN02679  80 GSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTV 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 145 LLGHSTGGmLATRYALQFA--DEVERLAMVNPIG-------LEDWK-ALGVPYRTVDQWYARELKV---------NAEGI 205
Cdd:PLN02679 159 LIGNSVGS-LACVIAASEStrDLVRGLVLLNCAGgmnnkavVDDWRiKLLLPLLWLIDFLLKQRGIasalfnrvkQRDNL 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 206 RNYERTTYyaGRWEPEFERWVDMLaglnKGPGHTQVAWNSaliYDMIFTQP----VYYEFKDLTVPTLLLIGTSDT-TAI 280
Cdd:PLN02679 238 KNILLSVY--GNKEAVDDELVEII----RGPADDEGALDA---FVSIVTGPpgpnPIKLIPRISLPILVLWGDQDPfTPL 308

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489294630 281 GSDIappavkatlghyevlGKQAARL---IPRSTLVEFPNLGHAPQMEEPDRFHKALLSWLD 339
Cdd:PLN02679 309 DGPV---------------GKYFSSLpsqLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLA 355
DUF1057 pfam06342
Alpha/beta hydrolase of unknown function (DUF1057); This family consists of several ...
 58-188 1.69e-05

Alpha/beta hydrolase of unknown function (DUF1057); This family consists of several Caenorhabditis elegans specific proteins of unknown function. Members of this family have an alpha/beta hydrolase fold.


Pssm-ID: 115027  Cd Length: 297  Bit Score: 45.90  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630   58 LQMGYMDVPAQGKVNGrTVVLMHGKnfcAATWGDsIKV----LSEAGYRVIAADQVGFCTSSKPEHYQYSFQQLASNTQA 133
Cdd:pfam06342  21 VQAVYEDSLTSGSPFG-TVVAFHGS---PGSHND-FKYirskFEDLNIRFIGVNYPGFEFTTGYPGQSHTNQERNSYSKA 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489294630  134 LLKALGVQ-KAVLLGHSTGGmlatRYALQFAD--EVERLAMVNPIGLEDWKALGVPYR 188
Cdd:pfam06342  96 LLEELELKgKLIIMGHSRGC----ENALQTATtrPAHGLVMINPTGFRIHKGIRPKSR 149
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
61-340 2.14e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.01  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  61 GYMDVPAQGKvNGRTVVLMHG-KNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSKpEHYQYSFQQLASNTQALLKALG 139
Cdd:COG1506   12 GWLYLPADGK-KYPVVVYVHGgPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAG-DWGGDEVDDVLAAIDYLAARPY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 140 V--QKAVLLGHSTGGMLATRYALQFADEVERLAMVNPIGleDWKALgvpYRTVDQWYARELKVNAEGIRNYERTTyyagr 217
Cdd:COG1506   90 VdpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS--DLRSY---YGTTREYTERLMGGPWEDPEAYAARS----- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630 218 wepeferwvdmlaglnkgpghtqvawnsaliydmiftqPVYYeFKDLTVPTLLLIGTSDttaigsDIAPPAvkatlgHYE 297
Cdd:COG1506  160 --------------------------------------PLAY-ADKLKTPLLLIHGEAD------DRVPPE------QAE 188

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489294630 298 VLGKQAARLIPRSTLVEFPNLGHAPQMEEPDRFHKALLSWLDK 340
Cdd:COG1506  189 RLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PRK05855 PRK05855
SDR family oxidoreductase;
68-151 5.96e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 44.59  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  68 QGKVNGRTVVLMHGKNFCAATWGDSIKVLSEAgYRVIAADQVGFCTSSKPEHY-QYSFQQLASNTQALLKALGVQKAV-L 145
Cdd:PRK05855  20 WGDPDRPTVVLVHGYPDNHEVWDGVAPLLADR-FRVVAYDVRGAGRSSAPKRTaAYTLARLADDFAAVIDAVSPDRPVhL 98


                 ....*.
gi 489294630 146 LGHSTG 151
Cdd:PRK05855  99 LAHDWG 104
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 42-173 6.44e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 41.00  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  42 YPYTLKHFAfQSQGQslqMGYMDvpaQGkvNGRTVVLMHGKNFCAATWGDSIKVLSEAgYRVIAADQVGFCTSSKPEHYQ 121
Cdd:PRK03204  12 YPFESRWFD-SSRGR---IHYID---EG--TGPPILLCHGNPTWSFLYRDIIVALRDR-FRCVAPDYLGFGLSERPSGFG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489294630 122 YSFQQLASNTQALLKALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVN 173
Cdd:PRK03204  82 YQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGN 133
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 66-174 1.86e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 39.88  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  66 PAQGKVNGrTVVLMHGKNFCAATWGDSIKVLSEAGYRVIAADQVGFCTSSKPEHYQYSFQQLASNTQALLKALGVQK--- 142
Cdd:PLN02652 130 PAAGEMRG-ILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDTEAFLEKIRSENpgv 208

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489294630 143 -AVLLGHSTGGMLATRYAL--QFADEVERLAMVNP 174
Cdd:PLN02652 209 pCFLFGHSTGGAVVLKAASypSIEDKLEGIVLTSP 243
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 117-338 2.65e-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: 38.87  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  117 PEHYQY-SFQQLASNTQALLKALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVNPIGledwKALGvpyrtVDQWYA 195
Cdd:pfam03096  74 PGGYPYpSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTP----KAAG-----WIEWFY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  196 RelKVNAEGIRNYERTT---------YYAG---RWEPEFERWVDMLAGLNKGPGHTQVAWNSaliY----DMIFTQPVyy 259
Cdd:pfam03096 145 N--KLSSKLLYYYGMTDsakdyllahYFGKeelSNNSDIVQEYRKFLKERLNPKNLQLYLEA---YnsrrDLTIERPG-- 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489294630  260 efKDLTVPTLLLIGTSDttaigsdiapPAVKATLGHYEVLGKQaarlipRSTLVEFPNLGHAPQMEEPDRFHKALLSWL 338
Cdd:pfam03096 218 --LETKCPVLLVVGDNS----------PHVDAVVECNTKLDPT------KTTLLKVADCGGLVQQEQPGKLTESFKLFL 278
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 65-174 3.12e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 39.41  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489294630  65 VPAQGKVNGRT---VVLMHGKNFCAATWGDSI-KVLSEAG---YRVIAADQVGFCTSSKPEHYQYSFQQ-LASNTQALLK 136
Cdd:PLN03087 190 VHVQQPKDNKAkedVLFIHGFISSSAFWTETLfPNFSDAAkstYRLFAVDLLGFGRSPKPADSLYTLREhLEMIERSVLE 269

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489294630 137 ALGVQKAVLLGHSTGGMLATRYALQFADEVERLAMVNP 174
Cdd:PLN03087 270 RYKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAP 307
 
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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