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Conserved domains on  [gi|15230367|ref|NP_190669|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

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, ...
6-319 1.94e-41

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: 143.60  E-value: 1.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   6 REKKIKTNGIWLNVAEKGDEeGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDslPSHESYTVSHLVAD 85
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGPD-GPPVVLLHGLPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSD--KPAGGYTLDDLADD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  86 VIGLLDHYGTTQAFVAGHDWGAIIGWCLCLFRPDRVKGFISLsvpyfprdpklkpSDFFKifgdgLYITQFQKPGRAEAA 165
Cdd:COG0596  79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV-------------DEVLA-----ALAEPLRRPGLAPEA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367 166 FAKHdclsvmkkFLLITRTDYlvappdteiidhleipstipdwiteeeiqvyaekfqrsgftgplnyyrsmdmnWEILAP 245
Cdd:COG0596 141 LAAL--------LRALARTDL-----------------------------------------------------RERLAR 159
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230367 246 WQdskivVPTKFIAGDKDIGYegPNGTMEYVKGEvfkivVPNLEIVVIEGGHHFIQQEKSEQVSQEILSFLNKL 319
Cdd:COG0596 160 IT-----VPTLVIWGEKDPIV--PPALARRLAEL-----LPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
6-319 1.94e-41

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: 143.60  E-value: 1.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   6 REKKIKTNGIWLNVAEKGDEeGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDslPSHESYTVSHLVAD 85
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGPD-GPPVVLLHGLPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSD--KPAGGYTLDDLADD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  86 VIGLLDHYGTTQAFVAGHDWGAIIGWCLCLFRPDRVKGFISLsvpyfprdpklkpSDFFKifgdgLYITQFQKPGRAEAA 165
Cdd:COG0596  79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV-------------DEVLA-----ALAEPLRRPGLAPEA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367 166 FAKHdclsvmkkFLLITRTDYlvappdteiidhleipstipdwiteeeiqvyaekfqrsgftgplnyyrsmdmnWEILAP 245
Cdd:COG0596 141 LAAL--------LRALARTDL-----------------------------------------------------RERLAR 159
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230367 246 WQdskivVPTKFIAGDKDIGYegPNGTMEYVKGEvfkivVPNLEIVVIEGGHHFIQQEKSEQVSQEILSFLNKL 319
Cdd:COG0596 160 IT-----VPTLVIWGEKDPIV--PPALARRLAEL-----LPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
28-174 1.71e-26

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: 104.89  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    28 PLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHESYTVSHLVADVIGLLDHYGTTQAFVAGHDWGA 107
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230367   108 IIGWCLCLFRPDRVKGFISLSvpyfprdPKLKPSDFFKIFGDGLYITQFQKPGRAEAAFAKHDCLSV 174
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG-------ALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLV 140
PRK05855 PRK05855
SDR family oxidoreductase;
3-166 1.59e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 97.74  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    3 SSVREKKIKTNGIWLNVAEKGDEEGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDSLPSHESYTVSHL 82
Cdd:PRK05855   1 SQPRRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADR-FRVVAYDVRGAGRSSAPKRTAAYTLARL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   83 VADVIGLLDHYGTTQAF-VAGHDWGAIIGWCLcLFRP---DRVKGFISLSVP------YFPRD--PKLKPSDFFKIFGDG 150
Cdd:PRK05855  80 ADDFAAVIDAVSPDRPVhLLAHDWGSIQGWEA-VTRPraaGRIASFTSVSGPsldhvgFWLRSglRRPTPRRLARALGQL 158
                        170
                 ....*....|....*....
gi 15230367  151 L---YITQFQKPGRAEAAF 166
Cdd:PRK05855 159 LrswYIYLFHLPVLPELLW 177
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
6-319 1.94e-41

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: 143.60  E-value: 1.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   6 REKKIKTNGIWLNVAEKGDEeGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDslPSHESYTVSHLVAD 85
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGPD-GPPVVLLHGLPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSD--KPAGGYTLDDLADD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  86 VIGLLDHYGTTQAFVAGHDWGAIIGWCLCLFRPDRVKGFISLsvpyfprdpklkpSDFFKifgdgLYITQFQKPGRAEAA 165
Cdd:COG0596  79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV-------------DEVLA-----ALAEPLRRPGLAPEA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367 166 FAKHdclsvmkkFLLITRTDYlvappdteiidhleipstipdwiteeeiqvyaekfqrsgftgplnyyrsmdmnWEILAP 245
Cdd:COG0596 141 LAAL--------LRALARTDL-----------------------------------------------------RERLAR 159
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230367 246 WQdskivVPTKFIAGDKDIGYegPNGTMEYVKGEvfkivVPNLEIVVIEGGHHFIQQEKSEQVSQEILSFLNKL 319
Cdd:COG0596 160 IT-----VPTLVIWGEKDPIV--PPALARRLAEL-----LPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
28-174 1.71e-26

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: 104.89  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    28 PLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHESYTVSHLVADVIGLLDHYGTTQAFVAGHDWGA 107
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230367   108 IIGWCLCLFRPDRVKGFISLSvpyfprdPKLKPSDFFKIFGDGLYITQFQKPGRAEAAFAKHDCLSV 174
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLG-------ALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLV 140
PRK05855 PRK05855
SDR family oxidoreductase;
3-166 1.59e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 97.74  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    3 SSVREKKIKTNGIWLNVAEKGDEEGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDSLPSHESYTVSHL 82
Cdd:PRK05855   1 SQPRRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADR-FRVVAYDVRGAGRSSAPKRTAAYTLARL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   83 VADVIGLLDHYGTTQAF-VAGHDWGAIIGWCLcLFRP---DRVKGFISLSVP------YFPRD--PKLKPSDFFKIFGDG 150
Cdd:PRK05855  80 ADDFAAVIDAVSPDRPVhLLAHDWGSIQGWEA-VTRPraaGRIASFTSVSGPsldhvgFWLRSglRRPTPRRLARALGQL 158
                        170
                 ....*....|....*....
gi 15230367  151 L---YITQFQKPGRAEAAF 166
Cdd:PRK05855 159 LrswYIYLFHLPVLPELLW 177
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
24-141 2.06e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.45  E-value: 2.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  24 DEEGPLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHEsYTVSHLVADVIGLLDH---YGTTQAFV 100
Cdd:COG2267  25 GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHV-DSFDDYVDDLRAALDAlraRPGLPVVL 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15230367 101 AGHDWGAIIGWCLCLFRPDRVKGFISLSvPYFPRDPKLKPS 141
Cdd:COG2267 104 LGHSMGGLIALLYAARYPDRVAGLVLLA-PAYRADPLLGPS 143
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
26-320 1.69e-18

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 83.89  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   26 EGPLVLLLHGFPETWYSWRHQIDFLSSHGyHVVAPDLRGYGDSDSLPshESYTVSHLVADVIGLLDHYGTTQAFVAGHDW 105
Cdd:PRK03592  26 EGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPD--IDYTFADHARYLDAWFDALGLDDVVLVGHDW 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  106 GAIIGWCLCLFRPDRVKGfislsVPYFprDPKLKPSDFFKIFGDGLYITQ-FQKPGRAEAAfakhdclsVMKKFLLITRT 184
Cdd:PRK03592 103 GSALGFDWAARHPDRVRG-----IAFM--EAIVRPMTWDDFPPAVRELFQaLRSPGEGEEM--------VLEENVFIERV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  185 dylvappdteiidhleIPSTIPDWITEEEIQVYaekfqRSGFTGP------LNYYRSMDMNWEilaPWQDSKIV------ 252
Cdd:PRK03592 168 ----------------LPGSILRPLSDEEMAVY-----RRPFPTPesrrptLSWPRELPIDGE---PADVVALVeeyaqw 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230367  253 -----VPTKFIAGDkdigyEGPnGTMEyvkGEVFKIV---VPNLEIVVIEGGHHFIQQEKSEQVSQEILSFLNKLS 320
Cdd:PRK03592 224 latsdVPKLLINAE-----PGA-ILTT---GAIRDWCrswPNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRRLR 290
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
21-125 1.32e-16

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 78.86  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   21 EKGDEEGPLVLLLHGFPeTW-YSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHESYTVSHLVADVIGLLDHYGTTQAF 99
Cdd:PRK00870  40 DEGPADGPPVLLLHGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVT 118
                         90       100
                 ....*....|....*....|....*.
gi 15230367  100 VAGHDWGAIIGWCLCLFRPDRVKGFI 125
Cdd:PRK00870 119 LVCQDWGGLIGLRLAAEHPDRFARLV 144
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
29-140 3.92e-15

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: 73.40  E-value: 3.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    29 LVLLLHGFPEtwYSWR--HQIDFLSSHGYHVVAPDLRGYGDSDSLPSHESyTVSHLVADVIGLLDH----YGTTQAFVAG 102
Cdd:pfam12146   6 VVVLVHGLGE--HSGRyaHLADALAAQGFAVYAYDHRGHGRSDGKRGHVP-SFDDYVDDLDTFVDKireeHPGLPLFLLG 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15230367   103 HDWGAIIGWCLCLFRPDRVKGFIsLSVPYF-PRDPKLKP 140
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLI-LSAPALkIKPYLAPP 120
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
22-194 4.15e-15

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 73.51  E-value: 4.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  22 KGDEEGPLVLLLHGFPET-WYSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHEsytvshLVADVIGLLDH------YG 94
Cdd:COG1506  18 ADGKKYPVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGD------EVDDVLAAIDYlaarpyVD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  95 TTQAFVAGHDWGAIIGWCLCLFRPDRVKGFISLSVpyfprdpklkPSDFFKIFGDGLYITQ--FQKPGRAEAAFAKHDCL 172
Cdd:COG1506  92 PDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG----------VSDLRSYYGTTREYTErlMGGPWEDPEAYAARSPL 161
                       170       180
                ....*....|....*....|....*..
gi 15230367 173 SVMKK----FLLIT-RTDYLVAPPDTE 194
Cdd:COG1506 162 AYADKlktpLLLIHgEADDRVPPEQAE 188
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
8-128 5.22e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.90  E-value: 5.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    8 KKIKTNGIWLNVAEKGDEEGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDslPSHESYTVSHLVADVI 87
Cdd:PRK14875 112 RKARIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAG-RPVIALDLPGHGASS--KAVGAGSLDELAAAVL 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15230367   88 GLLDHYGTTQAFVAGHDWGAIIGWCLCLFRPDRVKgfiSLS 128
Cdd:PRK14875 189 AFLDALGIERAHLVGHSMGGAVALRLAARAPQRVA---SLT 226
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
24-135 2.37e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 66.42  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   24 DE-EGPLVLLLHGFPeTW-YSWRHQIDFLSSHgYHVVAPDLRGYGDSDSlPSHESYTVSHLVADVIGLLDHYGTTQAFVA 101
Cdd:PRK03204  30 DEgTGPPILLCHGNP-TWsFLYRDIIVALRDR-FRCVAPDYLGFGLSER-PSGFGYQIDEHARVIGEFVDHLGLDRYLSM 106
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15230367  102 GHDWGAIIGWCLCLFRPDRVKGFISLSVPYFPRD 135
Cdd:PRK03204 107 GQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
16-318 6.15e-12

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 65.67  E-value: 6.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   16 WLNVaEKGDEEGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDS-LPSHE-SYTVSHLVADVIGLLDHY 93
Cdd:PLN03084 117 WFCV-ESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKN-YHAIAFDWLGFGFSDKpQPGYGfNYTLDEYVSSLESLIDEL 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   94 GTTQA--FVAGHDWGAIIGWCLClfRPDRVKGFISLSVPYFPRDPKLkPSDffkifgdglyitqfqkpgraeaafakhdc 171
Cdd:PLN03084 195 KSDKVslVVQGYFSPPVVKYASA--HPDKIKKLILLNPPLTKEHAKL-PST----------------------------- 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  172 LSVMKKFLL--ITRTDYLVAPPDTeiidhleIPSTIPDWITEEEIQVYAEKFQRSGFTG-PLN------------YYRSM 236
Cdd:PLN03084 243 LSEFSNFLLgeIFSQDPLRASDKA-------LTSCGPYAMKEDDAMVYRRPYLTSGSSGfALNaisrsmkkelkkYIEEM 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  237 -----DMNWEilapwqdskivVPTKFIAGDKD--IGYEgpnGTMEYVKGEVFKIV-VPNleivvieGGHHfIQQEKSEQV 308
Cdd:PLN03084 316 rsiltDKNWK-----------TPITVCWGLRDrwLNYD---GVEDFCKSSQHKLIeLPM-------AGHH-VQEDCGEEL 373
                        330
                 ....*....|
gi 15230367  309 SQEILSFLNK 318
Cdd:PLN03084 374 GGIISGILSK 383
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
30-168 4.97e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 61.34  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367    30 VLLLHGFpetWYSWRHqIDFLSSHGYHVVAPDLRGYGDSDslPSHESYTVSHLVADVIGLLDhyGTTQAFVAGHDWGAII 109
Cdd:pfam12697   1 VVLVHGA---GLSAAP-LAALLAAGVAVLAPDLPGHGSSS--PPPLDLADLADLAALLDELG--AARPVVLVGHSLGGAV 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230367   110 GwcLCLFRPDRVKGFIsLSVPYFPRDPKLKPSDFFKIFGDGLYITQFQKPGRAEAAFAK 168
Cdd:pfam12697  73 A--LAAAAAALVVGVL-VAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD 128
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
30-183 1.67e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 57.26  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  30 VLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLRGYGDS-DSLpshESYTVSHLVADVIGLLDH--YGTTQAFVAGHDWG 106
Cdd:COG1647  18 VLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSpEDL---LKTTWEDWLEDVEEAYEIlkAGYDKVIVIGLSMG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367 107 AIIGWCLCLFRPDrVKGFISLSVPYFPRDPKLKPSDFFKIFGDGL--YITQFQKPGRAEAAFAKH--DCLSVMKKFLLIT 182
Cdd:COG1647  95 GLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYLARSLrgIGSDIEDPEVAEYAYDRTplRALAELQRLIREV 173

                .
gi 15230367 183 R 183
Cdd:COG1647 174 R 174
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
16-113 4.66e-07

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 50.30  E-value: 4.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  16 WLNVAEKGDEEGPLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHEsytVSHLVADVIGLLDhYGT 95
Cdd:COG1073  26 DLYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREE---GSPERRDARAAVD-YLR 101
                        90
                ....*....|....*...
gi 15230367  96 TQAFVAGHDWGaIIGWCL 113
Cdd:COG1073 102 TLPGVDPERIG-LLGISL 118
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
30-130 1.03e-06

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 46.75  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  30 VLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDLrgygDSDSLPSHESytVSHLVADVIGLLDHYGTTQAFVAGHDWGAII 109
Cdd:COG1075   8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNY----PSTNGSIEDS--AEQLAAFVDAVLAATGAEKVDLVGHSMGGLV 81
                        90       100
                ....*....|....*....|...
gi 15230367 110 G--WCLCLFRPDRVKGFISLSVP 130
Cdd:COG1075  82 AryYLKRLGGAAKVARVVTLGTP 104
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
22-113 2.02e-06

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 48.04  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  22 KGDEEGPLVLLLHGfpetWYSWRHQI----DFLSSHGYHVVAPDLRGYGDSDSLPS-----HESYTVSHLVADVIGLLDH 92
Cdd:COG0412  24 AGGGPRPGVVVLHE----IFGLNPHIrdvaRRLAAAGYVVLAPDLYGRGGPGDDPDearalMGALDPELLAADLRAALDW 99
                        90       100
                ....*....|....*....|....*.
gi 15230367  93 ygttqafVAGHDWG-----AIIGWCL 113
Cdd:COG0412 100 -------LKAQPEVdagrvGVVGFCF 118
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
27-154 1.49e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 45.88  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   27 GPLVLLLHGFPETWYSWRHQIDFLSSHGyHVVAPDLRGYGDSD-----SLPSHESYT-------VSHLVADVIGlldhyg 94
Cdd:PLN02824  29 GPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDkpnprSAPPNSFYTfetwgeqLNDFCSDVVG------ 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230367   95 tTQAFVAGHDWGAIIGWCLCLFRPDRVKGF----ISLSVPYFPRDPKL-KPsdFFKIFGDGLYIT 154
Cdd:PLN02824 102 -DPAFVICNSVGGVVGLQAAVDAPELVRGVmlinISLRGLHIKKQPWLgRP--FIKAFQNLLRET 163
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
27-79 4.83e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 44.45  E-value: 4.83e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15230367   27 GPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSDSlPSHESYTV 79
Cdd:PLN02679  88 GPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDK-PPGFSYTM 138
YpfH COG0400
Predicted esterase [General function prediction only];
23-140 7.36e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 7.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  23 GDEEGPLVLLLHGfpeTWYSWRHQIDF---LSSHGYHVVAP--------------DLRGYGDSDSLPSHESYTvsHLVAD 85
Cdd:COG0400   1 GGPAAPLVVLLHG---YGGDEEDLLPLapeLALPGAAVLAPrapvpegpggrawfDLSFLEGREDEEGLAAAA--EALAA 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230367  86 VI-GLLDHYG--TTQAFVAGHDWGAIIGWCLCLFRPDRVKGFISLSvPYFPRDPKLKP 140
Cdd:COG0400  76 FIdELEARYGidPERIVLAGFSQGAAMALSLALRRPELLAGVVALS-GYLPGEEALPA 132
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
30-125 7.66e-05

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 43.72  E-value: 7.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  30 VLLLH---GFPETWYswRHQIDFLSSHGYHVVAPDLRGYGDSDSLPSHES-YTVSHLVA-DVIGLLD----HYGTTQAFV 100
Cdd:COG4757  34 VVLINpatGVPQRFY--RPFARYLAERGFAVLTYDYRGIGLSRPGSLRGFdAGYRDWGElDLPAVLDalraRFPGLPLLL 111
                        90       100
                ....*....|....*....|....*.
gi 15230367 101 AGHDWGaiiGWCLCLFR-PDRVKGFI 125
Cdd:COG4757 112 VGHSLG---GQLLGLAPnAERVDRLV 134
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
23-107 1.57e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.79  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  23 GDEEGPLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPD----------LRGYGDSDSLPSHE--------SYTVSHL-- 82
Cdd:COG4188  58 AGGPFPLVVLSHGLGGSREGYAYLAEHLASHGYVVAAPDhpgsnaadlsAALDGLADALDPEElwerpldlSFVLDQLla 137
                        90       100
                ....*....|....*....|....*....
gi 15230367  83 ----VADVIGLLDhygTTQAFVAGHDWGA 107
Cdd:COG4188 138 lnksDPPLAGRLD---LDRIGVIGHSLGG 163
PLN00021 PLN00021
chlorophyllase
24-76 2.37e-04

chlorophyllase


Pssm-ID: 177659  Cd Length: 313  Bit Score: 42.34  E-value: 2.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230367   24 DEEG--PLVLLLHGF--PETWYSwrhQI-DFLSSHGYHVVAPDLRGYGDSDSLPSHES 76
Cdd:PLN00021  47 SEAGtyPVLLFLHGYllYNSFYS---QLlQHIASHGFIVVAPQLYTLAGPDGTDEIKD 101
Chlorophyllase2 pfam12740
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ...
25-62 3.68e-04

Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.


Pssm-ID: 432755  Cd Length: 254  Bit Score: 41.54  E-value: 3.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15230367    25 EEG--PLVLLLHGF--PETWYSwrHQIDFLSSHGYHVVAPDL 62
Cdd:pfam12740  13 EAGtyPVLLFLHGYllYNSFYS--QLLQHIASHGFIVVAPQL 52
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
21-150 7.56e-04

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 40.61  E-value: 7.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367  21 EKGDEEGPLVLLLHGFPETWYSWRHQ------IDFLSSHG----YHVVAPDLRGYGDSDS-LPSHESYTvSHLVADVIGL 89
Cdd:COG2382 106 DNPGKKYPVLYLLDGGGGDEQDWFDQgrlptiLDNLIAAGkippMIVVMPDGGDGGDRGTeGPGNDAFE-RFLAEELIPF 184
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230367  90 LD-HYGTTQA----FVAGHDWGAIIGWCLCLFRPDRVKGFISLSVPYFPRDPKLKPSDFFKIFGDG 150
Cdd:COG2382 185 VEkNYRVSADpehrAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDADRGGWAELLAAG 250
PLN02578 PLN02578
hydrolase
26-69 1.12e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 40.21  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15230367   26 EGPLVLLLHGFPETWYSWRHQIDFLSSHgYHVVAPDLRGYGDSD 69
Cdd:PLN02578  85 EGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSD 127
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
20-62 2.47e-03

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 39.05  E-value: 2.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15230367    20 AEKGdeEGPLVLLLHGFPETWYSWRHQIDFLSSHGYHVVAPDL 62
Cdd:pfam07224  41 KEAG--TYPVVLFLHGTMLSNEFYSLFFNHIASHGFIVVAPQL 81
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
30-133 5.54e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 38.25  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230367   30 VLLLHGFPETWYSWRHQI--DF--LSSHGYHVVAPDLRGYGDSDSlPSHESYTV-SHLvaDVI--GLLDHYGTTQAFVAG 102
Cdd:PLN03087 204 VLFIHGFISSSAFWTETLfpNFsdAAKSTYRLFAVDLLGFGRSPK-PADSLYTLrEHL--EMIerSVLERYKVKSFHIVA 280
                         90       100       110
                 ....*....|....*....|....*....|.
gi 15230367  103 HDWGAIIGWCLCLFRPDRVKGFISLSVPYFP 133
Cdd:PLN03087 281 HSLGCILALALAVKHPGAVKSLTLLAPPYYP 311
 
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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