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Conserved domains on  [gi|446371058|ref|WP_000448913|]
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MULTISPECIES: alpha/beta hydrolase [Staphylococcus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427000)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917|37582413

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, ...
 1-124 1.07e-27

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: 106.24  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   1 METLELQGAKLRYHQVG-QGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELteplpdsasnPDSDYRVK 79
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK----------PAGGYTLD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446371058  80 RDAQDIAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKIA 124
Cdd:COG0596   74 DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV 118
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 20-264 4.94e-18

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 81.01  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   20 PVLIFIPGANGTGDIFLPLAEQL-KDHFTVVAVDRRDYGESelteplpdSASNPDSDYRVKRDAQDIAELAKSLSDKPVY 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKS--------SRPKAQDDYRTDDLAEDLEYILEALGLEKVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   99 ILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDST---------YWKDKN---DDIVHQILTEGLEKGmkTFGET 166
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAdrfilalfpGFFDGFvadFAPNPLGRLVAKLLA--LLLLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  167 LNIAPIDAKMMSQPAdteEGRIEQYKRTMFWSKFEIRQYTHSDiTLDDFTKYSDKITLLNGTDSRGSFPQDVNFY---IN 243
Cdd:pfam00561 151 LRLLKALPLLNKRFP---SGDYALAKSLVTGALLFIETWSTEL-RAKFLGRLDEPTLIIWGDQDPLVPPQALEKLaqlFP 226

                         250       260
                  ....*....|....*....|.
gi 446371058  244 KETgiPIVDIPGGHLGYIQKP 264
Cdd:pfam00561 227 NAR--LVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-124 1.07e-27

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: 106.24  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   1 METLELQGAKLRYHQVG-QGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELteplpdsasnPDSDYRVK 79
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK----------PAGGYTLD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446371058  80 RDAQDIAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKIA 124
Cdd:COG0596   74 DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV 118
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 20-264 4.94e-18

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: 81.01  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   20 PVLIFIPGANGTGDIFLPLAEQL-KDHFTVVAVDRRDYGESelteplpdSASNPDSDYRVKRDAQDIAELAKSLSDKPVY 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKS--------SRPKAQDDYRTDDLAEDLEYILEALGLEKVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   99 ILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDST---------YWKDKN---DDIVHQILTEGLEKGmkTFGET 166
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAdrfilalfpGFFDGFvadFAPNPLGRLVAKLLA--LLLLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  167 LNIAPIDAKMMSQPAdteEGRIEQYKRTMFWSKFEIRQYTHSDiTLDDFTKYSDKITLLNGTDSRGSFPQDVNFY---IN 243
Cdd:pfam00561 151 LRLLKALPLLNKRFP---SGDYALAKSLVTGALLFIETWSTEL-RAKFLGRLDEPTLIIWGDQDPLVPPQALEKLaqlFP 226

                         250       260
                  ....*....|....*....|.
gi 446371058  244 KETgiPIVDIPGGHLGYIQKP 264
Cdd:pfam00561 227 NAR--LVVIPDAGHFAFLEGP 245
PRK05855 PRK05855
SDR family oxidoreductase;
8-124 5.16e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 56.53  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   8 GAKLRYHQVGQ--GPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESelteplpdSASNPDSDYRVKRDAQDI 85
Cdd:PRK05855  12 GVRLAVYEWGDpdRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRS--------SAPKRTAAYTLARLADDF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446371058  86 AELAKSLS-DKPVYILGSSSGSIVAMHVLKDyPEVVKKIA 124
Cdd:PRK05855  84 AAVIDAVSpDRPVHLLAHDWGSIQGWEAVTR-PRAAGRIA 122
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 22-119 1.16e-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: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   22 LIFIPGAngtGDIFLPLAEQLKDHFTVVAVDRRDYGESELteplpdsasnPDSDYrvkRDAQDIAELAKSL-SDKPVYIL 100
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSP----------PPLDL---ADLADLAALLDELgAARPVVLV 64

                          90
                  ....*....|....*....
gi 446371058  101 GSSSGSIVAMHVLKDYPEV 119
Cdd:pfam12697  65 GHSLGGAVALAAAAAALVV 83
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 17-271 5.38e-08

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 53.55  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  17 GQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRD-YGESELTEPLPDSAsnpdSDYrvkrdaqdIAELAKSLSDK 95
Cdd:COG3319  599 GSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGlDGGEPPPASVEEMA----ARY--------VEAIRAVQPEG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  96 PVYILGSSSGSIVAMHV---LKDYPEVVKKIAFheppINTFLPDstYWKDKNDDIVHQILTEGLEKGMKTFGETLNIAPI 172
Cdd:COG3319  667 PYHLLGWSFGGLVAYEMarqLEAQGEEVALLVL----LDSYAPG--ALARLDEAELLAALLRDLARGVDLPLDAEELRAL 740

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058 173 D-----------AKMMSQPADTEEGRIEQYKRTMFWSKFEIRQYTHsditlddfTKYSDKITLLNGTDSRGSFPQDVNF- 240
Cdd:COG3319  741 DpeerlarllerLREAGLPAGLDAERLRRLLRVFRANLRALRRYRP--------RPYDGPVLLFRAEEDPPGRADDPALg 812

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446371058 241 ---YINKetGIPIVDIPGGHLGYIQKP--EGFADVL 271
Cdd:COG3319  813 wrpLVAG--GLEVHDVPGDHFSMLREPhvAELAAAL 846
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-124 1.07e-27

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: 106.24  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   1 METLELQGAKLRYHQVG-QGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELteplpdsasnPDSDYRVK 79
Cdd:COG0596    4 PRFVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK----------PAGGYTLD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446371058  80 RDAQDIAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKIA 124
Cdd:COG0596   74 DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV 118
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 20-264 4.94e-18

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: 81.01  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   20 PVLIFIPGANGTGDIFLPLAEQL-KDHFTVVAVDRRDYGESelteplpdSASNPDSDYRVKRDAQDIAELAKSLSDKPVY 98
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKS--------SRPKAQDDYRTDDLAEDLEYILEALGLEKVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   99 ILGSSSGSIVAMHVLKDYPEVVKKIAFHEPPINTFLPDST---------YWKDKN---DDIVHQILTEGLEKGmkTFGET 166
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAdrfilalfpGFFDGFvadFAPNPLGRLVAKLLA--LLLLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  167 LNIAPIDAKMMSQPAdteEGRIEQYKRTMFWSKFEIRQYTHSDiTLDDFTKYSDKITLLNGTDSRGSFPQDVNFY---IN 243
Cdd:pfam00561 151 LRLLKALPLLNKRFP---SGDYALAKSLVTGALLFIETWSTEL-RAKFLGRLDEPTLIIWGDQDPLVPPQALEKLaqlFP 226

                         250       260
                  ....*....|....*....|.
gi 446371058  244 KETgiPIVDIPGGHLGYIQKP 264
Cdd:pfam00561 227 NAR--LVVIPDAGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
8-125 2.89e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.03  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   8 GAKLRYH----QVGQGPVLIFIPGANGTGDIFLPLAEQLKDH-FTVVAVDRRDYGESELTEPLPDSASnpdsDYRvkRDA 82
Cdd:COG2267   13 GLRLRGRrwrpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFD----DYV--DDL 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446371058  83 QDIAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKIAF 125
Cdd:COG2267   87 RAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVL 129
PRK05855 PRK05855
SDR family oxidoreductase;
8-124 5.16e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 56.53  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   8 GAKLRYHQVGQ--GPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESelteplpdSASNPDSDYRVKRDAQDI 85
Cdd:PRK05855  12 GVRLAVYEWGDpdRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRS--------SAPKRTAAYTLARLADDF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446371058  86 AELAKSLS-DKPVYILGSSSGSIVAMHVLKDyPEVVKKIA 124
Cdd:PRK05855  84 AAVIDAVSpDRPVHLLAHDWGSIQGWEAVTR-PRAAGRIA 122
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 22-119 1.16e-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: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   22 LIFIPGAngtGDIFLPLAEQLKDHFTVVAVDRRDYGESELteplpdsasnPDSDYrvkRDAQDIAELAKSL-SDKPVYIL 100
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSP----------PPLDL---ADLADLAALLDELgAARPVVLV 64

                          90
                  ....*....|....*....
gi 446371058  101 GSSSGSIVAMHVLKDYPEV 119
Cdd:pfam12697  65 GHSLGGAVALAAAAAALVV 83
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 17-271 5.38e-08

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 53.55  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  17 GQGPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRD-YGESELTEPLPDSAsnpdSDYrvkrdaqdIAELAKSLSDK 95
Cdd:COG3319  599 GSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGlDGGEPPPASVEEMA----ARY--------VEAIRAVQPEG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  96 PVYILGSSSGSIVAMHV---LKDYPEVVKKIAFheppINTFLPDstYWKDKNDDIVHQILTEGLEKGMKTFGETLNIAPI 172
Cdd:COG3319  667 PYHLLGWSFGGLVAYEMarqLEAQGEEVALLVL----LDSYAPG--ALARLDEAELLAALLRDLARGVDLPLDAEELRAL 740

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058 173 D-----------AKMMSQPADTEEGRIEQYKRTMFWSKFEIRQYTHsditlddfTKYSDKITLLNGTDSRGSFPQDVNF- 240
Cdd:COG3319  741 DpeerlarllerLREAGLPAGLDAERLRRLLRVFRANLRALRRYRP--------RPYDGPVLLFRAEEDPPGRADDPALg 812

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446371058 241 ---YINKetGIPIVDIPGGHLGYIQKP--EGFADVL 271
Cdd:COG3319  813 wrpLVAG--GLEVHDVPGDHFSMLREPhvAELAAAL 846
PRK10673 PRK10673
esterase;
10-123 2.41e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.80  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  10 KLRYH-QVGQGPV----LIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESelteplPDSasnPDSDYRVKrdAQD 84
Cdd:PRK10673   2 KLNIRaQTAQNPHnnspIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLS------PRD---PVMNYPAM--AQD 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446371058  85 IAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKI 123
Cdd:PRK10673  71 LLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKL 109
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 21-125 8.96e-06

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: 45.67  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   21 VLIFIPGANGTGDIFLPLAEQLKDH-FTVVAVDRRDYGESEltePLPdsaSNPDSDYRVKRDAQDIAELAKSLS-DKPVY 98
Cdd:pfam12146   6 VVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSD---GKR---GHVPSFDDYVDDLDTFVDKIREEHpGLPLF 79

                          90       100
                  ....*....|....*....|....*..
gi 446371058   99 ILGSSSGSIVAMHVLKDYPEVVKKIAF 125
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLIL 106
YpfH COG0400
Predicted esterase [General function prediction only];
20-146 5.81e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  20 PVLIFIPGANGTGDIFLPLAEQLK-DHFTVVAVDrrdyGESELTE------PLPDSASNPDSDyRVKRDAQDIAEL---- 88
Cdd:COG0400    6 PLVVLLHGYGGDEEDLLPLAPELAlPGAAVLAPR----APVPEGPggrawfDLSFLEGREDEE-GLAAAAEALAAFidel 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446371058  89 --AKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKK-IAFHeppinTFLPDSTYWKDKNDD 146
Cdd:COG0400   81 eaRYGIDPERIVLAGFSQGAAMALSLALRRPELLAGvVALS-----GYLPGEEALPAPEAA 136
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-131 5.86e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 43.39  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058  17 GQGPVLIFIPGANGTGDIFLPLAEQLKDH-FTVVAVDRRDYGeselTEPLPDSASNPDsDYRvkRDAQDIAELAKSLSDK 95
Cdd:COG1647   13 GGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHG----TSPEDLLKTTWE-DWL--EDVEEAYEILKAGYDK 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446371058  96 pVYILGSSSGSIVAMHVLKDYPEvVKKIAFHEPPIN 131
Cdd:COG1647   86 -VIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALK 119
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-128 1.02e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.98  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   1 METLELQGAKLRYHQVGQGPVLIFIPGaNGTG-----DIFLPLAeqlkDHFTVVAVDRRDYGESElteplpdsasNPDSD 75
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHG-NPTSsylwrNIIPHLA----GLGRCLAPDLIGMGASD----------KPDID 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446371058  76 YRVKRDAQDIAELAKSLSDKPVYILGSSSGSIVAMHVLKDYPEVVKKIAFHEP 128
Cdd:PRK03592  74 YTFADHARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEA 126
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-120 1.30e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.54  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   2 ETLELQGAKLRYHQVGQ--GPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESelteplpdsasnpdsdyrVK 79
Cdd:PRK14875 112 RKARIGGRTVRYLRLGEgdGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGAS------------------SK 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446371058  80 R-DAQDIAELAKSLSD-------KPVYILGSSSGSIVAMHVLKDYPEVV 120
Cdd:PRK14875 174 AvGAGSLDELAAAVLAfldalgiERAHLVGHSMGGAVALRLAARAPQRV 222
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 11-112 6.61e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 37.91  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446371058   11 LRYHQVGQ---GPVLIFIPGANGTGDIFLPLAEQLKDHFTVVAVDRRDYGESELTEplPDSASNPDSDYRVKRDAQDIAE 87
Cdd:PLN02980 1360 IKVHEVGQnaeGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQN--HAKETQTEPTLSVELVADLLYK 1437

                          90       100
                  ....*....|....*....|....*
gi 446371058   88 LAKSLSDKPVYILGSSSGSIVAMHV 112
Cdd:PLN02980 1438 LIEHITPGKVTLVGYSMGARIALYM 1462
 
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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