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Conserved domains on  [gi|15230110|ref|NP_189085|]
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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, ...
14-272 2.88e-34

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: 123.57  E-value: 2.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  14 MNAKIIGSGERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWL---FSGaikdqtlyDPSKYNSLDVFSDDLIALMEE 90
Cdd:COG0596  14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRghgRSD--------KPAGGYTLDDLADDLAALLDA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  91 LKFGPVVFVGHSMSGVIGCAASIKRPDLFTNLLLIAaspryinsedykggfeskdidtiitsigsnyEAWAVDFSSFVVD 170
Cdd:COG0596  86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------------------------------EVLAALAEPLRRP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 171 SRDslsvqrfekslkkmkPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGkSTVEIIEDA 250
Cdd:COG0596 135 GLA---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPN-AELVVLPGA 198
                       250       260
                ....*....|....*....|..
gi 15230110 251 iGHFPQMTSHLELLGVMRRLLE 272
Cdd:COG0596 199 -GHFPPLEQPEAFAAALRDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
14-272 2.88e-34

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: 123.57  E-value: 2.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  14 MNAKIIGSGERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWL---FSGaikdqtlyDPSKYNSLDVFSDDLIALMEE 90
Cdd:COG0596  14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRghgRSD--------KPAGGYTLDDLADDLAALLDA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  91 LKFGPVVFVGHSMSGVIGCAASIKRPDLFTNLLLIAaspryinsedykggfeskdidtiitsigsnyEAWAVDFSSFVVD 170
Cdd:COG0596  86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------------------------------EVLAALAEPLRRP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 171 SRDslsvqrfekslkkmkPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGkSTVEIIEDA 250
Cdd:COG0596 135 GLA---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPN-AELVVLPGA 198
                       250       260
                ....*....|....*....|..
gi 15230110 251 iGHFPQMTSHLELLGVMRRLLE 272
Cdd:COG0596 199 -GHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
26-258 1.06e-17

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: 79.86  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110    26 MVLAHGFGGDQSVWDKIIPVLSQS-FKVLVFDWL---FSGAIKDQTLYdpskynSLDVFSDDLIALMEELKFGPVVFVGH 101
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRgfgKSSRPKAQDDY------RTDDLAEDLEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   102 SMSGVIGCAASIKRPDLFTNLLLIAASP--------RYINSEDYKGGFESKDIDTIITSIG---SNYEAWAVDFSSFVVD 170
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDppheldeaDRFILALFPGFFDGFVADFAPNPLGrlvAKLLALLLLRLRLLKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   171 SRD-SLSVQRFEKSLKKMKPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKgKSTVEIIED 249
Cdd:pfam00561 157 LPLlNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFP-NARLVVIPD 235

                  ....*....
gi 15230110   250 AiGHFPQMT 258
Cdd:pfam00561 236 A-GHFAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
22-257 3.47e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 62.65  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   22 GERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAiKDQTLYDPSkynsLDVFSDDLIALMEELKFGPVVFVGH 101
Cdd:PRK14875 130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGA-SSKAVGAGS----LDELAAAVLAFLDALGIERAHLVGH 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  102 SMSGVIGCAASIKRPDLFTNLLLIAAS--PRYINSeDYKGGF----ESKDIDTIITSIGSNYEawavdfssfvvdsrdSL 175
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTLIAPAglGPEING-DYIDGFvaaeSRRELKPVLELLFADPA---------------LV 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  176 SVQRFEKSLKKMKPE---TAL-ALAKIVFG-----SDEREILGQVSVPCHVIQPGNDVVVPVSVAyfmqEKIKGKSTVEI 246
Cdd:PRK14875 269 TRQMVEDLLKYKRLDgvdDALrALADALFAggrqrVDLRDRLASLAIPVLVIWGEQDRIIPAAHA----QGLPDGVAVHV 344
                        250
                 ....*....|.
gi 15230110  247 IEDAiGHFPQM 257
Cdd:PRK14875 345 LPGA-GHMPQM 354
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
14-272 2.88e-34

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: 123.57  E-value: 2.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  14 MNAKIIGSGERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWL---FSGaikdqtlyDPSKYNSLDVFSDDLIALMEE 90
Cdd:COG0596  14 LHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRghgRSD--------KPAGGYTLDDLADDLAALLDA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  91 LKFGPVVFVGHSMSGVIGCAASIKRPDLFTNLLLIAaspryinsedykggfeskdidtiitsigsnyEAWAVDFSSFVVD 170
Cdd:COG0596  86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD-------------------------------EVLAALAEPLRRP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 171 SRDslsvqrfekslkkmkPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGkSTVEIIEDA 250
Cdd:COG0596 135 GLA---------------PEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPN-AELVVLPGA 198
                       250       260
                ....*....|....*....|..
gi 15230110 251 iGHFPQMTSHLELLGVMRRLLE 272
Cdd:COG0596 199 -GHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
26-258 1.06e-17

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: 79.86  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110    26 MVLAHGFGGDQSVWDKIIPVLSQS-FKVLVFDWL---FSGAIKDQTLYdpskynSLDVFSDDLIALMEELKFGPVVFVGH 101
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRgfgKSSRPKAQDDY------RTDDLAEDLEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   102 SMSGVIGCAASIKRPDLFTNLLLIAASP--------RYINSEDYKGGFESKDIDTIITSIG---SNYEAWAVDFSSFVVD 170
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDppheldeaDRFILALFPGFFDGFVADFAPNPLGrlvAKLLALLLLRLRLLKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   171 SRD-SLSVQRFEKSLKKMKPETALALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKgKSTVEIIED 249
Cdd:pfam00561 157 LPLlNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFP-NARLVVIPD 235

                  ....*....
gi 15230110   250 AiGHFPQMT 258
Cdd:pfam00561 236 A-GHFAFLE 243
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
27-273 1.53e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.02  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  27 VLAHGFGGDQSVWDKIIPVLSQS-FKVLVFDWLFSGAikdqTLYDPSKYNSLDVFSDDLIALMEELK---FGPVVFVGHS 102
Cdd:COG2267  32 VLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGR----SDGPRGHVDSFDDYVDDLRAALDALRarpGLPVVLLGHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 103 MSGVIGCAASIKRPDLFTNLLLIAasPRYINSEDYkggfeskdidtiitsigsnyeawavdfssfvvdsrdslsvqrfek 182
Cdd:COG2267 108 MGGLIALLYAARYPDRVAGLVLLA--PAYRADPLL--------------------------------------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 183 slkkmkpetaLALAKIVFGSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGKSTVEIIEDAiGHFPQMTSHLE 262
Cdd:COG2267 141 ----------GPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGA-RHELLNEPARE 209
                       250
                ....*....|.
gi 15230110 263 LlgVMRRLLEF 273
Cdd:COG2267 210 E--VLAAILAW 218
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
22-257 3.47e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 62.65  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   22 GERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAiKDQTLYDPSkynsLDVFSDDLIALMEELKFGPVVFVGH 101
Cdd:PRK14875 130 DGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGA-SSKAVGAGS----LDELAAAVLAFLDALGIERAHLVGH 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  102 SMSGVIGCAASIKRPDLFTNLLLIAAS--PRYINSeDYKGGF----ESKDIDTIITSIGSNYEawavdfssfvvdsrdSL 175
Cdd:PRK14875 205 SMGGAVALRLAARAPQRVASLTLIAPAglGPEING-DYIDGFvaaeSRRELKPVLELLFADPA---------------LV 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  176 SVQRFEKSLKKMKPE---TAL-ALAKIVFG-----SDEREILGQVSVPCHVIQPGNDVVVPVSVAyfmqEKIKGKSTVEI 246
Cdd:PRK14875 269 TRQMVEDLLKYKRLDgvdDALrALADALFAggrqrVDLRDRLASLAIPVLVIWGEQDRIIPAAHA----QGLPDGVAVHV 344
                        250
                 ....*....|.
gi 15230110  247 IEDAiGHFPQM 257
Cdd:PRK14875 345 LPGA-GHMPQM 354
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
20-130 3.98e-09

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 56.29  E-value: 3.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   20 GSGErSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWL---FSGAIKDQTLYDPSKYNsLDVFSDDLIALMEELKFGPV 96
Cdd:PLN02824  27 TSGP-ALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLgygYSDKPNPRSAPPNSFYT-FETWGEQLNDFCSDVVGDPA 104
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15230110   97 VFVGHSMSGVIGCAASIKRPDLFTNLLLIAASPR 130
Cdd:PLN02824 105 FVICNSVGGVVGLQAAVDAPELVRGVMLINISLR 138
PLN02578 PLN02578
hydrolase
26-138 1.61e-08

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 54.46  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   26 MVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWL-FSGAIKDQTLYDPskynslDVFSDDLIALMEELKFGPVVFVGHSMS 104
Cdd:PLN02578  89 IVLIHGFGASAFHWRYNIPELAKKYKVYALDLLgFGWSDKALIEYDA------MVWRDQVADFVKEVVKEPAVLVGNSLG 162
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15230110  105 GVIGCAASIKRPDLFTNLLLIAASPRYINSEDYK 138
Cdd:PLN02578 163 GFTALSTAVGYPELVAGVALLNSAGQFGSESREK 196
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
27-107 6.78e-08

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: 6.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  27 VLAHGFGGDQSVWDKIIPVLSQS-FKVLVFDWlfsgaikdqtlydPSKYNSLDVFSDDLIALMEELK----FGPVVFVGH 101
Cdd:COG1075   9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALNY-------------PSTNGSIEDSAEQLAAFVDAVLaatgAEKVDLVGH 75

                ....*.
gi 15230110 102 SMSGVI 107
Cdd:COG1075  76 SMGGLV 81
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
18-273 1.74e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 51.10  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  18 IIGSGERSMVLAHGFGGDQSVWDKIIPVLSQS-FKVLVFdwLFSGAikDQTLYDPSKYNSLDVFsDDLIALMEELK--FG 94
Cdd:COG1647  10 FLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAP--RLPGH--GTSPEDLLKTTWEDWL-EDVEEAYEILKagYD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110  95 PVVFVGHSMSGVIGCAASIKRPDLfTNLLLIAASPRYINsedykggfESKDIDTIITSIGSNYEAWAVDFSSFvvdsrds 174
Cdd:COG1647  85 KVIVIGLSMGGLLALLLAARYPDV-AGLVLLSPALKIDD--------PSAPLLPLLKYLARSLRGIGSDIEDP------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110 175 lsvQRFEKSLKKMKPETALALAKIVfgSDEREILGQVSVPCHVIQPGNDVVVPVSVAYFMQEKIKGK-STVEIIEDAiGH 253
Cdd:COG1647 149 ---EVAEYAYDRTPLRALAELQRLI--REVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdKELVWLEDS-GH 222
                       250       260
                ....*....|....*....|
gi 15230110 254 FpqMTSHLELLGVMRRLLEF 273
Cdd:COG1647 223 V--ITLDKDREEVAEEILDF 240
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
26-256 7.29e-07

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.62  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110    26 MVLAHGFGgdqSVWDKIIPVLSQSFKVLVFDWLFSGAiKDQTLYDPSKYNSLDVFSDDLIALmeelkfGPVVFVGHSMSG 105
Cdd:pfam12697   1 VVLVHGAG---LSAAPLAALLAAGVAVLAPDLPGHGS-SSPPPLDLADLADLAALLDELGAA------RPVVLVGHSLGG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   106 VIGCAAsikRPDLFTNLLLIAASPRYINSEDYKGGFESKDIDTIITsigsnyEAWAVDFSSFVVDSRDSLSVQRFEKSLk 185
Cdd:pfam12697  71 AVALAA---AAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAA------PAWLAAESLARGFLDDLPADAEWAAAL- 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230110   186 kmkpeTALALAKIVFGSDEREILGQVSVPCHVIQpGNDVVVPVSVAYFMQEKIKGKstVEIIEDAiGHFPQ 256
Cdd:pfam12697 141 -----ARLAALLAALALLPLAAWRDLPVPVLVLA-EEDRLVPELAQRLLAALAGAR--LVVLPGA-GHLPL 202
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
75-250 2.30e-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: 47.59  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110    75 NSLDVFSDDLIALMEELKFG----PVVFVGHSMSGVIGCAASIKRPDLFTNLLLIAAsprYINSEDYKGGFESKDIDTII 150
Cdd:pfam12146  53 PSFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDKVDGLILSAP---ALKIKPYLAPPILKLLAKLL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   151 TSIG-SNYEAWAVDFSSFvvdSRDSLSVQRFEKS---LKKMKPETALALAKIvfGSDEREILGQVSVPCHVIQPGNDVVV 226
Cdd:pfam12146 130 GKLFpRLRVPNNLLPDSL---SRDPEVVAAYAADplvHGGISARTLYELLDA--GERLLRRAAAITVPLLLLHGGADRVV 204
                         170       180
                  ....*....|....*....|....*
gi 15230110   227 PVSVAYFMQEKIKGKS-TVEIIEDA 250
Cdd:pfam12146 205 DPAGSREFYERAGSTDkTLKLYPGL 229
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
25-125 2.88e-06

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 47.95  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   25 SMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGaIKDQTLYDPSKYNSLDVFSDDLIALMEELKFGPVVFV--GHS 102
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFG-FSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVvqGYF 207
                         90       100
                 ....*....|....*....|...
gi 15230110  103 MSGVIGCAAsiKRPDLFTNLLLI 125
Cdd:PLN03084 208 SPPVVKYAS--AHPDKIKKLILL 228
PRK05855 PRK05855
SDR family oxidoreductase;
27-118 1.71e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 45.74  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   27 VLAHGFGGDQSVWDKIIPVLSQSFKVLVFDwlFSGAIKDQTLYDPSKYnSLDVFSDDLIALMEEL-KFGPVVFVGHSMsG 105
Cdd:PRK05855  29 VLVHGYPDNHEVWDGVAPLLADRFRVVAYD--VRGAGRSSAPKRTAAY-TLARLADDFAAVIDAVsPDRPVHLLAHDW-G 104
                         90
                 ....*....|...
gi 15230110  106 VIGCAASIKRPDL 118
Cdd:PRK05855 105 SIQGWEAVTRPRA 117
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
14-125 2.53e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 44.83  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   14 MNAKIIGSGERS-----MVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAiKDQtlydPSKYN-SLDVFSDDLIAL 87
Cdd:PLN02679  74 INYLVKGSPEVTssgppVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGA-SDK----PPGFSyTMETWAELILDF 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15230110   88 MEELKFGPVVFVGHSMsGVIGC--AASIKRPDLFTNLLLI 125
Cdd:PLN02679 149 LEEVVQKPTVLIGNSV-GSLACviAASESTRDLVRGLVLL 187
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
25-125 2.25e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 39.12  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   25 SMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAIKDQTLYDPSKYNSLDVFSDDLIALMEELKFGPVVFVGHSMS 104
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEAWFIDSFEEWRKAKNLSNFILLGHSFG 186
                         90       100
                 ....*....|....*....|.
gi 15230110  105 GVIGCAASIKRPDLFTNLLLI 125
Cdd:PLN02894 187 GYVAAKYALKHPEHVQHLILV 207
PLN02965 PLN02965
Probable pheophorbidase
27-138 2.37e-03

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 38.75  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   27 VLAHGFGGDQSVWDKIIPVL-SQSFKVLVFDWLFSGAikdqTLYDPSKYNSLDVFSDDLIALMEEL-KFGPVVFVGHSMS 104
Cdd:PLN02965   7 VFVHGASHGAWCWYKLATLLdAAGFKSTCVDLTGAGI----SLTDSNTVSSSDQYNRPLFALLSDLpPDHKVILVGHSIG 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15230110  105 GVIGCAASIKRPDLFTNLLLIAAS---PRYINSEDYK 138
Cdd:PLN02965  83 GGSVTEALCKFTDKISMAIYVAAAmvkPGSIISPRLK 119
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
27-158 8.91e-03

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 36.79  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110   27 VLAHGFGGDQSVWDKIIPVLSQS-FKVLVFDwLFSGAIkDQTlyDPSKYNSLDVFSDDLIALMEELKFG-PVVFVGHSMS 104
Cdd:PLN02211  22 VLIHGISGGSWCWYKIRCLMENSgYKVTCID-LKSAGI-DQS--DADSVTTFDEYNKPLIDFLSSLPENeKVILVGHSAG 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230110  105 GVIGCAASIKRPDLFTNLLLIAASPryinsedYKGGFES----KDIDTIITSIGSNYE 158
Cdd:PLN02211  98 GLSVTQAIHRFPKKICLAVYVAATM-------LKLGFQTdedmKDGVPDLSEFGDVYE 148
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
23-129 8.96e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 37.53  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230110    23 ERSMVLAHGFGGDQSVWDKIIPVLSQSFKVLVFDWLFSGAIKDQTLYDPSKYN---SLDVFSDDLIALMEELKFGPVVFV 99
Cdd:PLN02980 1371 GSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAKETQTEptlSVELVADLLYKLIEHITPGKVTLV 1450
                          90       100       110
                  ....*....|....*....|....*....|
gi 15230110   100 GHSMSGVIGCAASIKRPDLFTNLLLIAASP 129
Cdd:PLN02980 1451 GYSMGARIALYMALRFSDKIEGAVIISGSP 1480
 
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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