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Conserved domains on  [gi|30687414|ref|NP_568379|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta hydrolase 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
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 11-219 2.02e-20

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 86.51  E-value: 2.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  11 SVDSEEGVKLHTRIFKPRNEGEEVSddenlVIVLVHPFsllGGC--QALLkgIASELASKGFKSVTFDTRGAGKSTGRAT 88
Cdd:COG1073  14 TFKSRDGIKLAGDLYLPAGASKKYP-----AVVVAHGN---GGVkeQRAL--YAQRLAELGFNVLAFDYRGYGESEGEPR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  89 LTGFAEVKDVVAVCRWLCQ--NVDAHRILLVGSSAGAPIAGSAVEQVEQV------VGYVSL-----------------G 143
Cdd:COG1073  84 EEGSPERRDARAAVDYLRTlpGVDPERIGLLGISLGGGYALNAAATDPRVkavildSPFTSLedlaaqrakeargaylpG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 144 YPFGLMASIL-FGRHH----KAILSSPKPKLFVMGTQDGFTSVSQLKKKLKSAVGRTETHLIEGVSHFQM---EGPEYDS 215
Cdd:COG1073 164 VPYLPNVRLAsLLNDEfdplAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydrPEEEYFD 243


                ....
gi 30687414 216 QVTD 219
Cdd:COG1073 244 KLAE 247
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 11-219 2.02e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 86.51  E-value: 2.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  11 SVDSEEGVKLHTRIFKPRNEGEEVSddenlVIVLVHPFsllGGC--QALLkgIASELASKGFKSVTFDTRGAGKSTGRAT 88
Cdd:COG1073  14 TFKSRDGIKLAGDLYLPAGASKKYP-----AVVVAHGN---GGVkeQRAL--YAQRLAELGFNVLAFDYRGYGESEGEPR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  89 LTGFAEVKDVVAVCRWLCQ--NVDAHRILLVGSSAGAPIAGSAVEQVEQV------VGYVSL-----------------G 143
Cdd:COG1073  84 EEGSPERRDARAAVDYLRTlpGVDPERIGLLGISLGGGYALNAAATDPRVkavildSPFTSLedlaaqrakeargaylpG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 144 YPFGLMASIL-FGRHH----KAILSSPKPKLFVMGTQDGFTSVSQLKKKLKSAVGRTETHLIEGVSHFQM---EGPEYDS 215
Cdd:COG1073 164 VPYLPNVRLAsLLNDEfdplAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydrPEEEYFD 243


                ....
gi 30687414 216 QVTD 219
Cdd:COG1073 244 KLAE 247
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 41-143 3.41e-08

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: 52.51  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    41 VIVLVHpfsllGGCQALLK--GIASELASKGFKSVTFDTRGAGKSTGRATLTGFaEVKDVVAVCRWLCQNVDAHRILLVG 118
Cdd:pfam00561   2 PVLLLH-----GLPGSSDLwrKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY-RTDDLAEDLEYILEALGLEKVNLVG 75

                          90       100
                  ....*....|....*....|....*.
gi 30687414   119 SSAGAPIAGSAVEQVEQVV-GYVSLG 143
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVkALVLLG 101
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
 12-105 2.84e-04

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 41.33  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    12 VDSEEGVKLHTRIFKPrNEGEEVSddenlVIVLVHP---FSLLGGCQALLKGiaSELASKGFKSVTFDTRGAGKSTGRAT 88
Cdd:TIGR00976   1 VPMRDGTRLAIDVYRP-AGGGPVP-----VILSRTPygkDAGLRWGLDKTEP--AWFVAQGYAVVIQDTRGRGASEGEFD 72

                          90
                  ....*....|....*..
gi 30687414    89 LTGFAEVKDVVAVCRWL 105
Cdd:TIGR00976  73 LLGSDEAADGYDLVDWI 89
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 24-123 9.60e-04

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 39.62  E-value: 9.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  24 IFKPRNegeeVSDDENL-VIVLVHpfsllGGcqALLKGIASELASKGFKS-------VTFDTR-GAGK--STGRATLTGF 92
Cdd:cd00312  83 VYTPKN----TKPGNSLpVMVWIH-----GG--GFMFGSGSLYPGDGLARegdnvivVSINYRlGVLGflSTGDIELPGN 151

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30687414  93 AEVKDVVAVCRWLCQNV-----DAHRILLVGSSAGA 123
Cdd:cd00312 152 YGLKDQRLALKWVQDNIaafggDPDSVTIFGESAGG 187
PRK05855 PRK05855
SDR family oxidoreductase;
11-101 6.32e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 37.27  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414   11 SVDSEEGVKLHTRifkprnegeEVSDDENLVIVLVH--PFSllggcQALLKGIASELASKgFKSVTFDTRGAGKST---G 85
Cdd:PRK05855   6 TVVSSDGVRLAVY---------EWGDPDRPTVVLVHgyPDN-----HEVWDGVAPLLADR-FRVVAYDVRGAGRSSapkR 70

                         90
                 ....*....|....*...
gi 30687414   86 RA--TLTGFAEvkDVVAV 101
Cdd:PRK05855  71 TAayTLARLAD--DFAAV 86
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 11-219 2.02e-20

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 86.51  E-value: 2.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  11 SVDSEEGVKLHTRIFKPRNEGEEVSddenlVIVLVHPFsllGGC--QALLkgIASELASKGFKSVTFDTRGAGKSTGRAT 88
Cdd:COG1073  14 TFKSRDGIKLAGDLYLPAGASKKYP-----AVVVAHGN---GGVkeQRAL--YAQRLAELGFNVLAFDYRGYGESEGEPR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  89 LTGFAEVKDVVAVCRWLCQ--NVDAHRILLVGSSAGAPIAGSAVEQVEQV------VGYVSL-----------------G 143
Cdd:COG1073  84 EEGSPERRDARAAVDYLRTlpGVDPERIGLLGISLGGGYALNAAATDPRVkavildSPFTSLedlaaqrakeargaylpG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 144 YPFGLMASIL-FGRHH----KAILSSPKPKLFVMGTQDGFTSVSQLKKKLKSAVGRTETHLIEGVSHFQM---EGPEYDS 215
Cdd:COG1073 164 VPYLPNVRLAsLLNDEfdplAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLydrPEEEYFD 243


                ....
gi 30687414 216 QVTD 219
Cdd:COG1073 244 KLAE 247
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
11-225 2.32e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 77.35  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  11 SVDSEEGVKLHTRIFKPRNEGEEVsddenlvIVLVHPFsllGGCQALLKGIASELASKGFKSVTFDTRGAGKSTG-RATL 89
Cdd:COG2267   7 TLPTRDGLRLRGRRWRPAGSPRGT-------VVLVHGL---GEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGpRGHV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  90 TGFAE-VKDVVAVCRWLCQNVDAhRILLVGSSAGAPIAGSAVEQVEQVV-GYVSLG----------YPFGLMASILFGRH 157
Cdd:COG2267  77 DSFDDyVDDLRAALDALRARPGL-PVVLLGHSMGGLIALLYAARYPDRVaGLVLLApayradpllgPSARWLRALRLAEA 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30687414 158 HKAIlssPKPKLFVMGTQDGFTSVSQLKKKLKSAVGRTETHLIEGVSHFQMEGPEYDsQVTDIICKFI 225
Cdd:COG2267 156 LARI---DVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPARE-EVLAAILAWL 219
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
11-205 6.04e-17

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 76.59  E-value: 6.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  11 SVDSEEGVKLHTRIFKPRnegeevsDDENL-VIVLVHpfsllGGCQALLKG---IASELASKGFKSVTFDTRGAGKSTGR 86
Cdd:COG1506   1 TFKSADGTTLPGWLYLPA-------DGKKYpVVVYVH-----GGPGSRDDSflpLAQALASRGYAVLAPDYRGYGESAGD 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  87 AtltGFAEVKDVVAVCRWLCQN--VDAHRILLVGSSAGAPIAGSAVEQVEQVV-GYVSLGYPFGLMASILFGRHHKAIL- 162
Cdd:COG1506  69 W---GGDEVDDVLAAIDYLAARpyVDPDRIGIYGHSYGGYMALLAAARHPDRFkAAVALAGVSDLRSYYGTTREYTERLm 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30687414 163 ------------SSP--------KPKLFVMGTQDGFTSVSQ---LKKKLKSAVGRTETHLIEGVSH 205
Cdd:COG1506 146 ggpwedpeayaaRSPlayadklkTPLLLIHGEADDRVPPEQaerLYEALKKAGKPVELLVYPGEGH 211
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
30-206 1.31e-15

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 72.50  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  30 EGE-EVSDDENLVIVLV-HPFSLLGGC--QALLKGIASELASKGFKSVTFDTRGAGKSTGRATlTGFAEVKDVVAVCRWL 105
Cdd:COG2945  12 EGRlDLPEGPPRGVALIlHPHPLFGGTmdNKVVYTLARALVAAGFAVLRFNFRGVGRSEGEFD-EGRGELDDAAAALDWL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 106 cQNVDAHRILLVGSSAGAPIAGSAVEQVEQVVGYVSLGYPFGLMAsilFGrhhkAILSSPKPKLFVMGTQDGFTSVSQLK 185
Cdd:COG2945  91 -RAQNPLPLWLAGFSFGAYVALQLAMRLPEVEGLILVAPPVNRYD---FS----FLAPCPAPTLVIHGEQDEVVPPAEVL 162

                       170       180
                ....*....|....*....|.
gi 30687414 186 KKLKSAVGRTETHLIEGVSHF 206
Cdd:COG2945 163 DWARPLSPPLPVVVVPGADHF 183
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 33-228 4.75e-14

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: 68.49  E-value: 4.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  33 EVSDDENLVIVLVHPFsllGGCQALLKGIASELAsKGFKSVTFDTRGAGKSTGRATLTGFAE-VKDVVAVCRWLcqnvDA 111
Cdd:COG0596  17 REAGPDGPPVVLLHGL---PGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDlADDLAALLDAL----GL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 112 HRILLVGSSAGAPIA-----------------GSAVEQVEQVVGYVSLGYP--FGLMASILFGRHHKAILSSPKPKLFVM 172
Cdd:COG0596  89 ERVVLVGHSMGGMVAlelaarhpervaglvlvDEVLAALAEPLRRPGLAPEalAALLRALARTDLRERLARITVPTLVIW 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30687414 173 GTQDGFTSVSQLkKKLKSAVGRTETHLIEGVSHF-QMEGPEydsQVTDIICKFISSL 228
Cdd:COG0596 169 GEKDPIVPPALA-RRLAELLPNAELVVLPGAGHFpPLEQPE---AFAAALRDFLARL 221
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
93-228 2.37e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 55.26  E-value: 2.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  93 AEVKDVVAVCRWLCQN-----VDAHRILLVGSSAGAPIAGSAV-----EQVEQVVGYVSLgYP-FGLMASILFgrhhkAI 161
Cdd:COG0657  62 AALEDAYAALRWLRANaaelgIDPDRIAVAGDSAGGHLAAALAlrardRGGPRPAAQVLI-YPvLDLTASPLR-----AD 135

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 162 LSSPKPKLFVMGTQDGFTSVSQ-LKKKLKSAVGRTETHLIEGVSHF--QMEGPEYDSQVTDIICKFISSL 228
Cdd:COG0657 136 LAGLPPTLIVTGEADPLVDESEaLAAALRAAGVPVELHVYPGGGHGfgLLAGLPEARAALAEIAAFLRRA 205
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 41-143 3.41e-08

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: 52.51  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    41 VIVLVHpfsllGGCQALLK--GIASELASKGFKSVTFDTRGAGKSTGRATLTGFaEVKDVVAVCRWLCQNVDAHRILLVG 118
Cdd:pfam00561   2 PVLLLH-----GLPGSSDLwrKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY-RTDDLAEDLEYILEALGLEKVNLVG 75

                          90       100
                  ....*....|....*....|....*.
gi 30687414   119 SSAGAPIAGSAVEQVEQVV-GYVSLG 143
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVkALVLLG 101
Peptidase_S15 pfam02129
X-Pro dipeptidyl-peptidase (S15 family);
17-108 8.04e-07

X-Pro dipeptidyl-peptidase (S15 family);


Pssm-ID: 396621 [Multi-domain]  Cd Length: 264  Bit Score: 48.49  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    17 GVKLHTRIFKPRNEGEEVSddenlVIVLVHPFSLLGGCQALLKGI--ASELASKGFKSVTFDTRGAGKSTGRATLTGFAE 94
Cdd:pfam02129   2 GVRLAADIYRPTKTGGPVP-----ALLTRSPYGARRDGASDLALAhpEWEFAARGYAVVYQDVRGTGGSEGVFTVGGPQE 76

                          90
                  ....*....|....
gi 30687414    95 VKDVVAVCRWLCQN 108
Cdd:pfam02129  77 AADGKDVIDWLAGQ 90
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 42-170 3.16e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.31  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    42 IVLVHPFsllGGCQALLkgiaSELASKGFKSVTFDTRGAGKSTGRATltGFAEVKDVVAVCRWLcqnVDAHRILLVGSSA 121
Cdd:pfam12697   1 VVLVHGA---GLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPL--DLADLADLAALLDEL---GAARPVVLVGHSL 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 30687414   122 GAPIAgSAVEQVEQVVG-YVSLGYPFGLMASILFGRHHKAILSSPKPKLF 170
Cdd:pfam12697  69 GGAVA-LAAAAAALVVGvLVAPLAAPPGLLAALLALLARLGAALAAPAWL 117
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
46-205 1.07e-05

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


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 44.87  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  46 HPFsllggcqalLKGIASELASKGFKSVTFD--TRGAGKS--TGRATLtgFAEVKDVVAVCRwlcQNVDAHRILLVGSSA 121
Cdd:COG3571  24 SPF---------MVALAEALAAAGIAVARFEfpYMVAGRRppDRAPVL--DAAWRAVIAALR---ARLAGLPLVIGGKSM 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414 122 GAPIAGSAVEQVEQVVGYVSLGYPFglmasilfgrH-----------HKAILSspKPKLFVMGTQDGFTSVSQLKKKLKS 190
Cdd:COG3571  90 GGRVASMLAAEGGGAAGLVCLGYPF----------HppgkpeklrteHLADLT--VPTLIVQGERDPFGTPEEVAGYPLP 157

                       170
                ....*....|....*
gi 30687414 191 AvgRTETHLIEGVSH 205
Cdd:COG3571 158 P--AIELVWLPGGDH 170
COG2936 COG2936
Predicted acyl esterase [General function prediction only];
17-105 1.89e-05

Predicted acyl esterase [General function prediction only];


Pssm-ID: 442179 [Multi-domain]  Cd Length: 555  Bit Score: 44.92  E-value: 1.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  17 GVKLHTRIFKPRNEGEEVSddenlVIVLVHPFSLLGGCQALLKGIASELASKGFKSVTFDTRGAGKSTGRATLTGFAEVK 96
Cdd:COG2936  22 GVRLAADIYRPKDAEGPVP-----VILERTPYGKRDGTAGRDLGPHPYFAERGYAVVVQDVRGTGGSEGEFDPYRVDEQT 96


                ....*....
gi 30687414  97 DVVAVCRWL 105
Cdd:COG2936  97 DGYDTIDWL 105
/NonD TIGR00976
putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes ...
 12-105 2.84e-04

putative hydrolase, CocE/NonD family; This model represents a protein subfamily that includes the cocaine esterase CocE, several glutaryl-7-ACA acylases, and the putative diester hydrolase NonD of Streptomyces griseus (all hydrolases). This family shows extensive, low-level similarity to a family of xaa-pro dipeptidyl-peptidases, and local similarity by PSI-BLAST to many other hydrolases. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273375 [Multi-domain]  Cd Length: 550  Bit Score: 41.33  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    12 VDSEEGVKLHTRIFKPrNEGEEVSddenlVIVLVHP---FSLLGGCQALLKGiaSELASKGFKSVTFDTRGAGKSTGRAT 88
Cdd:TIGR00976   1 VPMRDGTRLAIDVYRP-AGGGPVP-----VILSRTPygkDAGLRWGLDKTEP--AWFVAQGYAVVIQDTRGRGASEGEFD 72

                          90
                  ....*....|....*..
gi 30687414    89 LTGFAEVKDVVAVCRWL 105
Cdd:TIGR00976  73 LLGSDEAADGYDLVDWI 89
Abhydrolase_11 pfam20408
Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta ...
 46-205 9.16e-04

Alpha/beta hydrolase domain; This entry represents a protein that belongs to the alpha/beta hydrolase superfamily. Although proteins in this family are uncharacterized they are likely to have an enzymatic activity.


Pssm-ID: 466557 [Multi-domain]  Cd Length: 193  Bit Score: 39.11  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    46 HPFsllggcqalLKGIASELASKGFKSVTFD------TRGAGKST--GRATLTgfaeVKDVVAVCRWLCQnvDAHRILLV 117
Cdd:pfam20408  17 SPF---------MQAMAAALAARGIAVVRFNfpymqrRRRTGKRRppDRAPKL----LEAFRAVIAALRG--PDLPLFIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414   118 GSSAGAPIAGSAVEQVeQVVGYVSLGYPF---GlMASILFGRHHKAIlssPKPKLFVMGTQDGFTSVSQLKK-KLKSAVg 193
Cdd:pfam20408  82 GKSMGGRVASLLADDS-GVKGVIALGYPFhppG-KPEKLRLEHLPDL---TCPTLILQGERDPFGNREEVAAyPLPDNV- 155

                         170
                  ....*....|..
gi 30687414   194 rtETHLIEGVSH 205
Cdd:pfam20408 156 --SLHWLEDGDH 165
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 24-123 9.60e-04

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 39.62  E-value: 9.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414  24 IFKPRNegeeVSDDENL-VIVLVHpfsllGGcqALLKGIASELASKGFKS-------VTFDTR-GAGK--STGRATLTGF 92
Cdd:cd00312  83 VYTPKN----TKPGNSLpVMVWIH-----GG--GFMFGSGSLYPGDGLARegdnvivVSINYRlGVLGflSTGDIELPGN 151

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30687414  93 AEVKDVVAVCRWLCQNV-----DAHRILLVGSSAGA 123
Cdd:cd00312 152 YGLKDQRLALKWVQDNIaafggDPDSVTIFGESAGG 187
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-165 3.80e-03

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: 37.58  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    41 VIVLVHpfsllGGC------QALlkgiASELASKGFKSVTFDTRGAGKSTG-RATLTGFAE-VKDVVAVCRWLCQNVDAH 112
Cdd:pfam12146   6 VVVLVH-----GLGehsgryAHL----ADALAAQGFAVYAYDHRGHGRSDGkRGHVPSFDDyVDDLDTFVDKIREEHPGL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 30687414   113 RILLVGSSAGAPIAGSAVeqveqvvgyvsLGYPfglmasilfGRHHKAILSSP 165
Cdd:pfam12146  77 PLFLLGHSMGGLIAALYA-----------LRYP---------DKVDGLILSAP 109
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 59-123 5.41e-03

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 36.77  E-value: 5.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414    59 KGIASELASKGFKSVTFDTRgagkSTGRATLTgfAEVKDVVAVCRWLCQN-----VDAHRILLVGSSAGA 123
Cdd:pfam20434  37 TNTVKALLKAGYAVASINYR----LSTDAKFP--AQIQDVKAAIRFLRANaakygIDTNKIALMGFSAGG 100
PRK05855 PRK05855
SDR family oxidoreductase;
11-101 6.32e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 37.27  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687414   11 SVDSEEGVKLHTRifkprnegeEVSDDENLVIVLVH--PFSllggcQALLKGIASELASKgFKSVTFDTRGAGKST---G 85
Cdd:PRK05855   6 TVVSSDGVRLAVY---------EWGDPDRPTVVLVHgyPDN-----HEVWDGVAPLLADR-FRVVAYDVRGAGRSSapkR 70

                         90
                 ....*....|....*...
gi 30687414   86 RA--TLTGFAEvkDVVAV 101
Cdd:PRK05855  71 TAayTLARLAD--DFAAV 86
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 93-145 7.76e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 36.42  E-value: 7.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30687414    93 AEVKDVVAVCRWLCQN-----VDAHRILLVGSSAGAPIAGSAV-----EQVEQVVGYVsLGYP 145
Cdd:pfam07859  47 AAYDDAYAALRWLAEQaaelgADPSRIAVAGDSAGGNLAAAVAlrardEGLPKPAGQV-LIYP 108
 
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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