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Conserved domains on  [gi|815880521|ref|XP_001245576|]
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alpha/beta hydrolase [Coccidioides immitis RS]

Protein Classification

alpha/beta hydrolase domain-containing protein( domain architecture ID 1005082)

alpha/beta hydrolase (abhydrolase) domain-containing protein

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02894 super family cl30398
hydrolase, alpha/beta fold family protein
112-544 6.96e-58

hydrolase, alpha/beta fold family protein


The actual alignment was detected with superfamily member PLN02894:

Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 198.60  E-value: 6.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 112 PYGPRRW-RSTmvelSGKNRELNEFSVErlGEKVENNLVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRP 190
Cdd:PLN02894  77 PGSKVRWfRSA----SNEPRFINTVTFD--SKEDAPTLVMVHGYGASQGFFFRNFDAL--ASRFRVIAIDQLGWGGSSRP 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 191 PFRiaAKEREkaikEAEDWFVDALEEWRVKRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPVGIPedpyavnad 270
Cdd:PLN02894 149 DFT--CKSTE----ETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFS--------- 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 271 vPEPTSSTlaNEFTQDQAggvqvgdnnnflnardkraaasvdnndiskppakTIPKWLV-YLWDANVSPFSLVRWSGPLG 349
Cdd:PLN02894 214 -SESDDKS--EWLTKFRA----------------------------------TWKGAVLnHLWESNFTPQKIIRGLGPWG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 350 PRLVSGWTSRRFSH------LPQDEARALHDYAYSLFRLRGSGEYALSYILAPGAYARSPVIRRIHgvgrqflppqvnpp 423
Cdd:PLN02894 257 PNLVRRYTTARFGAhstgdiLSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS-------------- 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 424 spkpdsasestslscsdlpppssapsapsasdssssfsvqtaprrEPGIPIVFMYGEHDWMDAQGGhaakekidqekqri 503
Cdd:PLN02894 323 ---------------------------------------------EWKVPTTFIYGRHDWMNYEGA-------------- 343
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 815880521 504 lkdasVEEQKADKGSAKVVVIKKAGHHLYLDGWEEFNEVML 544
Cdd:PLN02894 344 -----VEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVL 379
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
112-544 6.96e-58

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 198.60  E-value: 6.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 112 PYGPRRW-RSTmvelSGKNRELNEFSVErlGEKVENNLVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRP 190
Cdd:PLN02894  77 PGSKVRWfRSA----SNEPRFINTVTFD--SKEDAPTLVMVHGYGASQGFFFRNFDAL--ASRFRVIAIDQLGWGGSSRP 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 191 PFRiaAKEREkaikEAEDWFVDALEEWRVKRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPVGIPedpyavnad 270
Cdd:PLN02894 149 DFT--CKSTE----ETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFS--------- 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 271 vPEPTSSTlaNEFTQDQAggvqvgdnnnflnardkraaasvdnndiskppakTIPKWLV-YLWDANVSPFSLVRWSGPLG 349
Cdd:PLN02894 214 -SESDDKS--EWLTKFRA----------------------------------TWKGAVLnHLWESNFTPQKIIRGLGPWG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 350 PRLVSGWTSRRFSH------LPQDEARALHDYAYSLFRLRGSGEYALSYILAPGAYARSPVIRRIHgvgrqflppqvnpp 423
Cdd:PLN02894 257 PNLVRRYTTARFGAhstgdiLSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS-------------- 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 424 spkpdsasestslscsdlpppssapsapsasdssssfsvqtaprrEPGIPIVFMYGEHDWMDAQGGhaakekidqekqri 503
Cdd:PLN02894 323 ---------------------------------------------EWKVPTTFIYGRHDWMNYEGA-------------- 343
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 815880521 504 lkdasVEEQKADKGSAKVVVIKKAGHHLYLDGWEEFNEVML 544
Cdd:PLN02894 344 -----VEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVL 379
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
148-258 3.73e-19

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: 86.21  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRP--PFRIAAkerekaikEAEDW--FVDALEewrvkrrI 223
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPAL--AAGYRVIAPDLRGHGRSDKPagGYTLDD--------LADDLaaLLDALG-------L 88
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815880521 224 ERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPV 258
Cdd:COG0596   89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV 123
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
148-347 8.86e-19

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: 86.02  E-value: 8.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  148 LVVLHGYGAGLGFFYKNFEALSRaKGWQLYALDLLGMGRSTRPPFRiaAKEREKAIKEAEDWFVDALeewrvkrRIERFT 227
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALAR-DGFRVIALDLRGFGKSSRPKAQ--DDYRTDDLAEDLEYILEAL-------GLEKVN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  228 LLGHSLGGYLAVAYALKYPGRLNKLILASPVG----IPEDPYAVNADVPEpTSSTLANEFTQDQAgGVQVGDNNNFLNAR 303
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDppheLDEADRFILALFPG-FFDGFVADFAPNPL-GRLVAKLLALLLLR 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 815880521  304 DKR--------AAASVDNNDISKPPAKTIPKWLVYlWDANVSPFSLVRWSGP 347
Cdd:pfam00561 151 LRLlkalpllnKRFPSGDYALAKSLVTGALLFIET-WSTELRAKFLGRLDEP 201
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
141-262 7.29e-17

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: 81.27  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  141 GEKVEnnLVVLHGyGAGLGFFY-KNFEALSRAKGWQLYALDLLGMGRSTRPPFriaAKEREKAIkeaeDWFVDALEEWRV 219
Cdd:TIGR01250  23 GEKIK--LLLLHG-GPGMSHEYlENLRELLKEEGREVIMYDQLGCGYSDQPDD---SDEELWTI----DYFVDELEEVRE 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 815880521  220 KRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPV-GIPE 262
Cdd:TIGR01250  93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLdSAPE 136
 
Name Accession Description Interval E-value
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
112-544 6.96e-58

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 198.60  E-value: 6.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 112 PYGPRRW-RSTmvelSGKNRELNEFSVErlGEKVENNLVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRP 190
Cdd:PLN02894  77 PGSKVRWfRSA----SNEPRFINTVTFD--SKEDAPTLVMVHGYGASQGFFFRNFDAL--ASRFRVIAIDQLGWGGSSRP 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 191 PFRiaAKEREkaikEAEDWFVDALEEWRVKRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPVGIPedpyavnad 270
Cdd:PLN02894 149 DFT--CKSTE----ETEAWFIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFS--------- 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 271 vPEPTSSTlaNEFTQDQAggvqvgdnnnflnardkraaasvdnndiskppakTIPKWLV-YLWDANVSPFSLVRWSGPLG 349
Cdd:PLN02894 214 -SESDDKS--EWLTKFRA----------------------------------TWKGAVLnHLWESNFTPQKIIRGLGPWG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 350 PRLVSGWTSRRFSH------LPQDEARALHDYAYSLFRLRGSGEYALSYILAPGAYARSPVIRRIHgvgrqflppqvnpp 423
Cdd:PLN02894 257 PNLVRRYTTARFGAhstgdiLSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS-------------- 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 424 spkpdsasestslscsdlpppssapsapsasdssssfsvqtaprrEPGIPIVFMYGEHDWMDAQGGhaakekidqekqri 503
Cdd:PLN02894 323 ---------------------------------------------EWKVPTTFIYGRHDWMNYEGA-------------- 343
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 815880521 504 lkdasVEEQKADKGSAKVVVIKKAGHHLYLDGWEEFNEVML 544
Cdd:PLN02894 344 -----VEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVL 379
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
148-258 3.73e-19

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: 86.21  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRP--PFRIAAkerekaikEAEDW--FVDALEewrvkrrI 223
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPAL--AAGYRVIAPDLRGHGRSDKPagGYTLDD--------LADDLaaLLDALG-------L 88
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815880521 224 ERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPV 258
Cdd:COG0596   89 ERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV 123
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
148-347 8.86e-19

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: 86.02  E-value: 8.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  148 LVVLHGYGAGLGFFYKNFEALSRaKGWQLYALDLLGMGRSTRPPFRiaAKEREKAIKEAEDWFVDALeewrvkrRIERFT 227
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALAR-DGFRVIALDLRGFGKSSRPKAQ--DDYRTDDLAEDLEYILEAL-------GLEKVN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  228 LLGHSLGGYLAVAYALKYPGRLNKLILASPVG----IPEDPYAVNADVPEpTSSTLANEFTQDQAgGVQVGDNNNFLNAR 303
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDppheLDEADRFILALFPG-FFDGFVADFAPNPL-GRLVAKLLALLLLR 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 815880521  304 DKR--------AAASVDNNDISKPPAKTIPKWLVYlWDANVSPFSLVRWSGP 347
Cdd:pfam00561 151 LRLlkalpllnKRFPSGDYALAKSLVTGALLFIET-WSTELRAKFLGRLDEP 201
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
141-262 7.29e-17

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: 81.27  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  141 GEKVEnnLVVLHGyGAGLGFFY-KNFEALSRAKGWQLYALDLLGMGRSTRPPFriaAKEREKAIkeaeDWFVDALEEWRV 219
Cdd:TIGR01250  23 GEKIK--LLLLHG-GPGMSHEYlENLRELLKEEGREVIMYDQLGCGYSDQPDD---SDEELWTI----DYFVDELEEVRE 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 815880521  220 KRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPV-GIPE 262
Cdd:TIGR01250  93 KLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLdSAPE 136
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
148-257 7.09e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 76.96  E-value: 7.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALSRAkGWQLYALDLLGMGRSTRPPFRIAAKEREkaikeAEDwfVDALEEWRVKRRIERFT 227
Cdd:COG2267   31 VVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHVDSFDDY-----VDD--LRAALDALRARPGLPVV 102
                         90       100       110
                 ....*....|....*....|....*....|
gi 815880521 228 LLGHSLGGYLAVAYALKYPGRLNKLILASP 257
Cdd:COG2267  103 LLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
139-270 1.91e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 65.74  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 139 RLGEKVENNLVVLHGYGAGLGFFYKNFEALSRAKgwQLYALDLLGMGRSTrppfriaakereKAIKEAE-DWFVDALEEW 217
Cdd:PRK14875 125 RLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGR--PVIALDLPGHGASS------------KAVGAGSlDELAAAVLAF 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815880521 218 RVKRRIERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPVGIPEDpyaVNAD 270
Cdd:PRK14875 191 LDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPE---INGD 240
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
148-265 2.61e-11

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: 63.77  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  148 LVVLHGYGAGLGFFYKNFEALSRAkGWQLYALDLLGMGRStrPPFRIAAKEREKAIKEAEDwFVDAL-EEWRVKRRIerf 226
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQ-GFAVYAYDHRGHGRS--DGKRGHVPSFDDYVDDLDT-FVDKIrEEHPGLPLF--- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 815880521  227 tLLGHSLGGYLAVAYALKYPGRLNKLILASP-VGIPEDPY 265
Cdd:pfam12146  80 -LLGHSMGGLIAALYALRYPDKVDGLILSAPaLKIKPYLA 118
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
141-257 8.51e-10

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 60.98  E-value: 8.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 141 GEKVENNLVVLHGYGAGLGFF----YKNFEALSRAKgWQLYALDLLGMGRSTRPPFRI-AAKEREKAIKEAedwfvdALE 215
Cdd:PLN03087 197 DNKAKEDVLFIHGFISSSAFWtetlFPNFSDAAKST-YRLFAVDLLGFGRSPKPADSLyTLREHLEMIERS------VLE 269
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815880521 216 EWRVKRrierFTLLGHSLGGYLAVAYALKYPGRLNKLILASP 257
Cdd:PLN03087 270 RYKVKS----FHIVAHSLGCILALALAVKHPGAVKSLTLLAP 307
YpfH COG0400
Predicted esterase [General function prediction only];
148-264 5.43e-09

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 56.07  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGA-GLGFFYKnFEALSRAkGWQLYALD----LLGMGRSTRPPFRIAAKEREKAIKEAEDWFVDALEEWRVKRR 222
Cdd:COG0400    8 VVLLHGYGGdEEDLLPL-APELALP-GAAVLAPRapvpEGPGGRAWFDLSFLEGREDEEGLAAAAEALAAFIDELEARYG 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 815880521 223 I--ERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPvGIPEDP 264
Cdd:COG0400   86 IdpERIVLAGFSQGAAMALSLALRRPELLAGVVALSG-YLPGEE 128
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
148-374 1.20e-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: 55.56  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  148 LVVLHGYGAGLGFFyknfeALSRAKGWQLYALDLLGMGRSTRPPFRIAAKEREKAikeaedwFVDALEEWRvkrrieRFT 227
Cdd:pfam12697   1 VVLVHGAGLSAAPL-----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAA-------LLDELGAAR------PVV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  228 LLGHSLGGYLAVAYAlkyPGRLNKLILASPVGIPEDPYAVNADVPEPTSSTLANEFTQDQAGGVQV----GDNNNFLNAR 303
Cdd:pfam12697  63 LVGHSLGGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGflddLPADAEWAAA 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815880521  304 DKRAAASVDNNDISKPPA-KTIPKWLVYLWDANvspfslvRWSGPLGPRLVSGWTSRRF------SHLPQDEARALHD 374
Cdd:pfam12697 140 LARLAALLAALALLPLAAwRDLPVPVLVLAEED-------RLVPELAQRLLAALAGARLvvlpgaGHLPLDDPEEVAE 210
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
149-266 1.02e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 53.02  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 149 VVLHGYGAG------LGffyknfEALSRAkGWQLYALDLLGMGRSTRPPFRIAAkerekaikeaEDWFVDALEEWR-VKR 221
Cdd:COG1647   19 LLLHGFTGSpaemrpLA------EALAKA-GYTVYAPRLPGHGTSPEDLLKTTW----------EDWLEDVEEAYEiLKA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 815880521 222 RIERFTLLGHSLGGYLAVAYALKYPgRLNKLILASPVGIPEDPYA 266
Cdd:COG1647   82 GYDKVIVIGLSMGGLLALLLAARYP-DVAGLVLLSPALKIDDPSA 125
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
148-257 1.73e-07

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.44  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALsRAKGWQLYALDLlgmgRSTRPPFRIAAKErekaikeaedwFVDALEEWRVKRRIERFT 227
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRL-RAAGYPVYALNY----PSTNGSIEDSAEQ-----------LAAFVDAVLAATGAEKVD 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 815880521 228 LLGHSLGGYLAVAYA--LKYPGRLNKLI-LASP 257
Cdd:COG1075   72 LVGHSMGGLVARYYLkrLGGAAKVARVVtLGTP 104
PLN02578 PLN02578
hydrolase
148-279 1.08e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 50.99  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRStrppfriaakerEKAIKEAE-----DWFVDALEEwRVKrr 222
Cdd:PLN02578  89 IVLIHGFGASAFHWRYNIPEL--AKKYKVYALDLLGFGWS------------DKALIEYDamvwrDQVADFVKE-VVK-- 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815880521 223 iERFTLLGHSLGGYLAVAYALKYPGRLNKLILASPVGIPEDPYAVNADVPEPTSSTL 279
Cdd:PLN02578 152 -EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIVVEETVL 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
148-258 1.10e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.85  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAG-LGFFYKNFEALSRAkGWQLYALDLLGMGRSTRPPFRIAAKEREKAIKE-AEDWFVDAleewrvkrriER 225
Cdd:COG1506   26 VVYVHGGPGSrDDSFLPLAQALASR-GYAVLAPDYRGYGESAGDWGGDEVDDVLAAIDYlAARPYVDP----------DR 94
                         90       100       110
                 ....*....|....*....|....*....|...
gi 815880521 226 FTLLGHSLGGYLAVAYALKYPGRLNKLILASPV 258
Cdd:COG1506   95 IGIYGHSYGGYMALLAAARHPDRFKAAVALAGV 127
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
148-191 2.50e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.68  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALsrAKGWQLYALDLLGMGRSTRPP 191
Cdd:PLN02679  91 VLLVHGFGASIPHWRRNIGVL--AKNYTVYAIDLLGFGASDKPP 132
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
210-257 1.11e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 41.12  E-value: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 815880521 210 FVDAleEWRVKRriERFTLLGHSLGGYLAVAYALKYPGRLNKLILASP 257
Cdd:COG2819  120 YIDK--RYRTDP--ERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
152-263 1.29e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 41.28  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 152 HGYGAGLGFFyknFEALSR---AKGWQLYALDLLGMGRStrppfriaaKEREKAIKEAEDWFVDALEEW-RVKRRIE--- 224
Cdd:PLN02385  94 HGYGDTCTFF---FEGIARkiaSSGYGVFAMDYPGFGLS---------EGLHGYIPSFDDLVDDVIEHYsKIKGNPEfrg 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815880521 225 --RFtLLGHSLGGYLAVAYALKYPGRLNKLILASPV-GIPED 263
Cdd:PLN02385 162 lpSF-LFGQSMGGAVALKVHLKQPNAWDGAILVAPMcKIADD 202
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
132-273 2.03e-03

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 40.05  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521  132 LNEFSVERLGEKVENNLVVLHGYGA---GLGFFYKNFEALSRAKGWQLYA---LDLLGMGRSTRPPFRI-----AAKERE 200
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDsghGWADAAKTEAPLPNIKFIFPHGpeiPVTLNGGMRMPAWFDLvglspNAKEDE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815880521  201 KAIKEAEDWFVDALEEWRVK-RRIERFTLLGHSLGGYLAVAYALKYPGRLNKLI-----LASPVGIPEDPYAVNADVPE 273
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKgIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVafsgfLPLPTKFPSHPNLVTKKTPI 159
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
178-301 2.50e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.98  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 178 ALDLLGMGRSTRPP--FRIAAKEREKaikeaeDWFVDALEewrvkrrIERFTLLGHSLGGYLAVAYALKYPGRLNKLILA 255
Cdd:PRK03592  58 APDLIGMGASDKPDidYTFADHARYL------DAWFDALG-------LDDVVLVGHDWGSALGFDWAARHPDRVRGIAFM 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815880521 256 SPVGIPEDpyavNADVPEPtSSTLANEFTQDQAGGVQVGDNNNFLN 301
Cdd:PRK03592 125 EAIVRPMT----WDDFPPA-VRELFQALRSPGEGEEMVLEENVFIE 165
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
148-258 4.73e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.13  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815880521 148 LVVLHGYGAGLGFFYKNFEALSRAkGWQLYALDLLGMGRST-RPpfriaakeREKAIKEAEDW--FVDALEEWR-VKRri 223
Cdd:COG1073   40 VVVAHGNGGVKEQRALYAQRLAEL-GFNVLAFDYRGYGESEgEP--------REEGSPERRDAraAVDYLRTLPgVDP-- 108
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 815880521 224 ERFTLLGHSLGGYLAVAYALKYPgRLNKLILASPV 258
Cdd:COG1073  109 ERIGLLGISLGGGYALNAAATDP-RVKAVILDSPF 142
 
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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