NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446583928|ref|WP_000661274|]
View 

MULTISPECIES: alpha/beta fold hydrolase [Bacillus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 6-233 2.27e-24

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: 96.61  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHF-KGYFVQCIDWR------------NVKEQSEFAGRIIDVAKDENVILVGWSLGALAAIQ 72
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALaAGYRVIAPDLRghgrsdkpaggyTLDDLADDLAALLDALGLERVVLVGHSMGGMVALE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  73 AYKKI--KAKGIVLIGGTakftnasdysngwnalhVERLKRNLARRkedtlkrfyenmftkdelkenksfedivkhfkGD 150
Cdd:COG0596  106 LAARHpeRVAGLVLVDEV-----------------LAALAEPLRRP--------------------------------GL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 151 SIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-NETATLKVVNEAGHALCVTNFEYCVNEIIQ 229
Cdd:COG0596  137 APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAElLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216


                 ....
gi 446583928 230 FVEG 233
Cdd:COG0596  217 FLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 6-233 2.27e-24

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: 96.61  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHF-KGYFVQCIDWR------------NVKEQSEFAGRIIDVAKDENVILVGWSLGALAAIQ 72
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALaAGYRVIAPDLRghgrsdkpaggyTLDDLADDLAALLDALGLERVVLVGHSMGGMVALE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  73 AYKKI--KAKGIVLIGGTakftnasdysngwnalhVERLKRNLARRkedtlkrfyenmftkdelkenksfedivkhfkGD 150
Cdd:COG0596  106 LAARHpeRVAGLVLVDEV-----------------LAALAEPLRRP--------------------------------GL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 151 SIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-NETATLKVVNEAGHALCVTNFEYCVNEIIQ 229
Cdd:COG0596  137 APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAElLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216


                 ....
gi 446583928 230 FVEG 233
Cdd:COG0596  217 FLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 6-220 6.28e-16

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: 74.46  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928    6 IIFIPGWGMEENIWDLVLPHF--KGYFVQCIDWRNV------KEQSEFagRIIDVAKD----------ENVILVGWSLG- 66
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALarDGFRVIALDLRGFgkssrpKAQDDY--RTDDLAEDleyilealglEKVNLVGHSMGg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   67 ---ALAAIQAYKKIKAkgIVLIGGTAKFTNASDYSNGWNALHVERLKRNLARRKEDTLKRFYENMFTKDELKEN--KSFE 141
Cdd:pfam00561  81 liaLAYAAKYPDRVKA--LVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRllKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  142 DIVKHFKGDSIQS-------LQFGLDYLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-NETATLKVVNEAGH 213
Cdd:pfam00561 159 LLNKRFPSGDYALakslvtgALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQlFPNARLVVIPDAGH 238


                  ....*..
gi 446583928  214 ALCVTNF 220
Cdd:pfam00561 239 FAFLEGP 245
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
6-190 1.88e-08

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 53.48  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHFKGYF-VQCIDWRNVKEQSEFAGRIID-----VAKD--ENVILVGWSLGALAAIQA--YK 75
Cdd:PRK10349  16 LVLLHGWGLNAEVWRCIDEELSSHFtLHLVDLPGFGRSRGFGALSLAdmaeaVLQQapDKAIWLGWSLGGLVASQIalTH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  76 KIKAKGIVLIGGTAKFTnASDysnGWNALHVERL---KRNLARRKEDTLKRFY--ENMFTKDELKENKSFEDIVKHFKGD 150
Cdd:PRK10349  96 PERVQALVTVASSPCFS-ARD---EWPGIKPDVLagfQQQLSDDFQRTVERFLalQTMGTETARQDARALKKTVLALPMP 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446583928 151 SIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDVICP 190
Cdd:PRK10349 172 EVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVP 211
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 6-233 2.27e-24

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: 96.61  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHF-KGYFVQCIDWR------------NVKEQSEFAGRIIDVAKDENVILVGWSLGALAAIQ 72
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALaAGYRVIAPDLRghgrsdkpaggyTLDDLADDLAALLDALGLERVVLVGHSMGGMVALE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  73 AYKKI--KAKGIVLIGGTakftnasdysngwnalhVERLKRNLARRkedtlkrfyenmftkdelkenksfedivkhfkGD 150
Cdd:COG0596  106 LAARHpeRVAGLVLVDEV-----------------LAALAEPLRRP--------------------------------GL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 151 SIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-NETATLKVVNEAGHALCVTNFEYCVNEIIQ 229
Cdd:COG0596  137 APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAElLPNAELVVLPGAGHFPPLEQPEAFAAALRD 216


                 ....
gi 446583928 230 FVEG 233
Cdd:COG0596  217 FLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 6-220 6.28e-16

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: 74.46  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928    6 IIFIPGWGMEENIWDLVLPHF--KGYFVQCIDWRNV------KEQSEFagRIIDVAKD----------ENVILVGWSLG- 66
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALarDGFRVIALDLRGFgkssrpKAQDDY--RTDDLAEDleyilealglEKVNLVGHSMGg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   67 ---ALAAIQAYKKIKAkgIVLIGGTAKFTNASDYSNGWNALHVERLKRNLARRKEDTLKRFYENMFTKDELKEN--KSFE 141
Cdd:pfam00561  81 liaLAYAAKYPDRVKA--LVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRllKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  142 DIVKHFKGDSIQS-------LQFGLDYLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-NETATLKVVNEAGH 213
Cdd:pfam00561 159 LLNKRFPSGDYALakslvtgALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQlFPNARLVVIPDAGH 238


                  ....*..
gi 446583928  214 ALCVTNF 220
Cdd:pfam00561 239 FAFLEGP 245
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
56-234 8.43e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 68.43  E-value: 8.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  56 ENVILVGWSLGALAAIQAYKKIKA-KGIVLIGGTAKFTNASDYSNGWnALHVERLKRNLAR--RKEDTLKRFYENMFTKd 132
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAARYPDvAGLVLLSPALKIDDPSAPLLPL-LKYLARSLRGIGSdiEDPEVAEYAYDRTPLR- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 133 elkenksfedivkhfkgdSIQSLQfgldYLIEtDMREELKEIKVPILLIHGEQDVICPLSAARSMAEN---ETATLKVVN 209
Cdd:COG1647  162 ------------------ALAELQ----RLIR-EVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERlgsPDKELVWLE 218

                        170       180
                 ....*....|....*....|....*.
gi 446583928 210 EAGHALCVTNF-EYCVNEIIQFVEGI 234
Cdd:COG1647  219 DSGHVITLDKDrEEVAEEILDFLERL 244
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 6-215 1.25e-12

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 64.80  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928    6 IIFIPGWGMEENIWDLVLPHfkGYFVQCIDWRN----------VKEQSEFAGRIIDVAKDENVILVGWSLGALAAIQAYK 75
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA--GVAVLAPDLPGhgssspppldLADLADLAALLDELGAARPVVLVGHSLGGAVALAAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   76 KIKAKGIVLiggtakftNASDYSNGWNALHVERLKRNLARRkedTLKRFYENMFTKDELKEnksfEDIVKHFKGDSIQSL 155
Cdd:pfam12697  79 AALVVGVLV--------APLAAPPGLLAALLALLARLGAAL---AAPAWLAAESLARGFLD----DLPADAEWAAALARL 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  156 QFGLDYLiETDMREELKEIKVPILLIHgEQDVICPLSAARSMAENETATLKVVNEAGHAL 215
Cdd:pfam12697 144 AALLAAL-ALLPLAAWRDLPVPVLVLA-EEDRLVPELAQRLLAALAGARLVVLPGAGHLP 201
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
6-215 3.10e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 55.39  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHF--KGYFVQCIDWR-------------NVKEQSEFAGRIIDVAK---DENVILVGWSLGA 67
Cdd:COG2267   31 VVLVHGLGEHSGRYAELAEALaaAGYAVLAFDLRghgrsdgprghvdSFDDYVDDLRAALDALRarpGLPVVLLGHSMGG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  68 LAAIQ--AYKKIKAKGIVLIGGTAKFTNASDYSNGWnalhverlkrnlarrkedtlkrfyenmftkdelkenksfedivk 145
Cdd:COG2267  111 LIALLyaARYPDRVAGLVLLAPAYRADPLLGPSARW-------------------------------------------- 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446583928 146 hfkgdsiqslqfgldyLIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE--NETATLKVVNEAGHAL 215
Cdd:COG2267  147 ----------------LRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAArlSPDVELVLLPGARHEL 202
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
6-232 1.54e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGW-GMEENIWDLVLPHF--KGYFVQCIDWRNV-KEQSEFAGRIIDVAKD-------------ENVILVGWSLGAL 68
Cdd:COG1506   26 VVYVHGGpGSRDDSFLPLAQALasRGYAVLAPDYRGYgESAGDWGGDEVDDVLAaidylaarpyvdpDRIGIYGHSYGGY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  69 AAIQA--YKKIKAKGIVLIGGtakFTNASDYSNGWNALhVERLKRNLARRKEDtlkrfYENMftkdelkenksfeDIVKH 146
Cdd:COG1506  106 MALLAaaRHPDRFKAAVALAG---VSDLRSYYGTTREY-TERLMGGPWEDPEA-----YAAR-------------SPLAY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 147 fkgdsiqslqfgldylietdmreeLKEIKVPILLIHGEQDVICPLSAARSMAE-----NETATLKVVNEAGHALCVTNFE 221
Cdd:COG1506  164 ------------------------ADKLKTPLLLIHGEADDRVPPEQAERLYEalkkaGKPVELLVYPGEGHGFSGAGAP 219

                        250
                 ....*....|.
gi 446583928 222 YCVNEIIQFVE 232
Cdd:COG1506  220 DYLERILDFLD 230
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
6-190 1.88e-08

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 53.48  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   6 IIFIPGWGMEENIWDLVLPHFKGYF-VQCIDWRNVKEQSEFAGRIID-----VAKD--ENVILVGWSLGALAAIQA--YK 75
Cdd:PRK10349  16 LVLLHGWGLNAEVWRCIDEELSSHFtLHLVDLPGFGRSRGFGALSLAdmaeaVLQQapDKAIWLGWSLGGLVASQIalTH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  76 KIKAKGIVLIGGTAKFTnASDysnGWNALHVERL---KRNLARRKEDTLKRFY--ENMFTKDELKENKSFEDIVKHFKGD 150
Cdd:PRK10349  96 PERVQALVTVASSPCFS-ARD---EWPGIKPDVLagfQQQLSDDFQRTVERFLalQTMGTETARQDARALKKTVLALPMP 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446583928 151 SIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDVICP 190
Cdd:PRK10349 172 EVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVP 211
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 55-232 2.76e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.91  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  55 DENVILVGWSLGALAAIQA---YKKIKAkgIVLIGGtakFTNASDysngwnalhverlkrnLARRKedtLKRFYENMFTK 131
Cdd:COG1073  108 PERIGLLGISLGGGYALNAaatDPRVKA--VILDSP---FTSLED----------------LAAQR---AKEARGAYLPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928 132 DELKENKSFEDIV-KHFkgdsiqslqfgldylietDMREELKEIKVPILLIHGEQDVICPLSAARSMAE--NETATLKVV 208
Cdd:COG1073  164 VPYLPNVRLASLLnDEF------------------DPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEaaAEPKELLIV 225

                        170       180
                 ....*....|....*....|....*
gi 446583928 209 NEAGHALC-VTNFEYCVNEIIQFVE 232
Cdd:COG1073  226 PGAGHVDLyDRPEEEYFDKLAEFFK 250
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
169-232 7.48e-06

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 45.15  E-value: 7.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446583928 169 EELKEIKVPILLIHGEQDVICPLSAARSMAE--NETATLKVVNEAGHalcvtNFEYCVNEIIQFVE 232
Cdd:COG2945  136 SFLAPCPAPTLVIHGEQDEVVPPAEVLDWARplSPPLPVVVVPGADH-----FFHGKLDELKELVA 196
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
162-214 9.70e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.34  E-value: 9.70e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446583928 162 LIETDMREELKEIKVPILLIHGEQDVICPLSAARSMAE-----NETATLKVVNEAGHA 214
Cdd:COG0412  143 LPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAalaaaGVDVELHVYPGAGHG 200
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 154-215 2.81e-05

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: 44.13  E-value: 2.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446583928  154 SLQFGLDyLIET--DMREELKEIKVPILLIHGEQDVICPLSAARSMAEN---ETATLKVVNEAGHAL 215
Cdd:pfam12146 168 SARTLYE-LLDAgeRLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERagsTDKTLKLYPGLYHEL 233
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 6-70 9.44e-04

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 37.89  E-value: 9.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446583928   6 IIFIPGWGMEENIWDLVLPHFK--GYFVQCID--------WRNVKEQSEFAGRIIDVAKDENVILVGWSLGALAA 70
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRaaGYPVYALNypstngsiEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82
YpfH COG0400
Predicted esterase [General function prediction only];
175-216 1.62e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 1.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446583928 175 KVPILLIHGEQDVICPLSAARSMAEN-ETATLKV---VNEAGHALC 216
Cdd:COG0400  139 GTPVFLAHGTQDPVIPVERAREAAEAlEAAGADVtyrEYPGGHEIS 184
PRK11460 PRK11460
putative hydrolase; Provisional
 180-224 8.85e-03

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 36.55  E-value: 8.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446583928 180 LIHGEQDVICPLSAARS-----MAENETATLKVVNEAGHAL-------CVTNFEYCV 224
Cdd:PRK11460 153 LIHGGEDPVIDVAHAVAaqealISLGGDVTLDIVEDLGHAIdprlmqfALDRLRYTV 209
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 58-235 9.92e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 37.14  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928   58 VILVGWSLGALAAIQAYKKI--KAKGIVLIGGtakftnasdySNGwnalhverLKRNLARR----KEDT---------LK 122
Cdd:PLN02980 1447 VTLVGYSMGARIALYMALRFsdKIEGAVIISG----------SPG--------LKDEVARKirsaKDDSrarmlidhgLE 1508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583928  123 RFYENMFTKD---ELKENKSFEDIV----KHFKGDSIQSLQFGLDYLIETDMREELKEIKVPILLIHGEQDV-------- 187
Cdd:PLN02980 1509 IFLENWYSGElwkSLRNHPHFNKIVasrlLHKDVPSLAKLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDVkfkqiaqk 1588

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446583928  188 ----ICPLSAARSMAENETATLKVVNEAGHALCVTNFEYCVNEIIQFVEGIR 235
Cdd:PLN02980 1589 myreIGKSKESGNDKGKEIIEIVEIPNCGHAVHLENPLPVIRALRKFLTRLH 1640
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH