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Conserved domains on  [gi|2217339456|ref|XP_047297256|]
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serine hydrolase-like protein 2 isoform X8 [Homo sapiens]

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, ...
 22-132 2.04e-25

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: 98.53  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596    14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217339456 102 FSILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 22-132 2.04e-25

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: 98.53  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596    14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217339456 102 FSILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-143 9.38e-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: 78.70  E-value: 9.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  33 PPVLCLHGWLDNASSFDRLIPLLPQD-FYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGG 111
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217339456 112 VVGGMFFCTFPEMVDKLILLDTPLFLLESDEM 143
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEA 112
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 32-130 1.57e-14

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 69.94  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  32 GPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEI-RRVVAALKWNRFSILGHSFG 110
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81

                          90       100
                  ....*....|....*....|
gi 2217339456 111 GVVGGMFFCTFPEMVDKLIL 130
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLIL 101
PRK05855 PRK05855
SDR family oxidoreductase;
22-112 9.54e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 63.46  E-value: 9.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  22 IAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:PRK05855   15 LAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDR 94

                          90
                  ....*....|..
gi 2217339456 102 -FSILGHSFGGV 112
Cdd:PRK05855   95 pVHLLAHDWGSI 106
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 22-132 2.04e-25

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: 98.53  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596    14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217339456 102 FSILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 33-143 9.38e-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: 78.70  E-value: 9.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  33 PPVLCLHGWLDNASSFDRLIPLLPQD-FYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGG 111
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217339456 112 VVGGMFFCTFPEMVDKLILLDTPLFLLESDEM 143
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEA 112
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 32-130 1.57e-14

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 69.94  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  32 GPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEI-RRVVAALKWNRFSILGHSFG 110
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81

                          90       100
                  ....*....|....*....|
gi 2217339456 111 GVVGGMFFCTFPEMVDKLIL 130
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLIL 101
PRK05855 PRK05855
SDR family oxidoreductase;
22-112 9.54e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 63.46  E-value: 9.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  22 IAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:PRK05855   15 LAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDR 94

                          90
                  ....*....|..
gi 2217339456 102 -FSILGHSFGGV 112
Cdd:PRK05855   95 pVHLLAHDWGSI 106
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-133 1.30e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.56  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  21 HIAAKAWGSLQGP--PVLCLHGWLDNASSFDRLIP-LLPQDFYYVAMDFGGHGLSSHySPGVPYYLQTFVSEIRRVVAAL 97
Cdd:COG2267    15 RLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEaLAAAGYAVLAFDLRGHGRSDG-PRGHVDSFDDYVDDLRAALDAL 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217339456  98 KWN---RFSILGHSFGGVVGGMFFCTFPEMVDKLILLDT 133
Cdd:COG2267    94 RARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 28-146 1.70e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 62.59  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  28 GSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSS--HYSPGVPYYLQTFVSEIRRVVAALKWNRFSIL 105
Cdd:PLN03084  123 GSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpQPGYGFNYTLDEYVSSLESLIDELKSDKVSLV 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2217339456 106 GHSFGGVVGGMFFCTFPEMVDKLILLDTPLflleSDEMENL 146
Cdd:PLN03084  203 VQGYFSPPVVKYASAHPDKIKKLILLNPPL----TKEHAKL 239
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 34-134 4.10e-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: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  34 PVLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLSshyspgVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGGV 112
Cdd:COG1075     7 PVVLVHGLGGSAASWAPLAPRLRAAGYPVyALNYPSTNGS------IEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217339456 113 V--------GGmffctfPEMVDKLILLDTP 134
Cdd:COG1075    81 VaryylkrlGG------AAKVARVVTLGTP 104
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-114 1.53e-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: 47.08  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  35 VLCLHGWldnASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVpyylqTFVSEIRRVVAALK-WNRFSILGHSFGGVV 113
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDL-----ADLADLAALLDELGaARPVVLVGHSLGGAV 72


                  .
gi 2217339456 114 G 114
Cdd:pfam12697  73 A 73
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 33-148 2.72e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 47.21  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  33 PPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSH-------YSPGVPYYLQTFvSEIRRvvaALKWNRFSIL 105
Cdd:PLN02894  106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdftcksTEETEAWFIDSF-EEWRK---AKNLSNFILL 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217339456 106 GHSFGGVVGGMFFCTFPEMVDKLILLDTPLFLLESDEMENLLT 148
Cdd:PLN02894  182 GHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLT 224
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 31-141 4.75e-06

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 45.96  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  31 QGPPVLCL-HGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGlsshYSPGV-PYYLqtfvSEIRRVVAALKWNRFSILGHS 108
Cdd:TIGR01738   2 QGNVHLVLiHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHG----RSRGFgPLSL----ADMAEAIAAQAPDPAIWLGWS 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217339456 109 FGGVVGGMFFCTFPEMVDKLILL-DTPLFLLESD 141
Cdd:TIGR01738  74 LGGLVALHIAATHPDRVRALVTVaSSPCFSARED 107
PRK10673 PRK10673
esterase;
27-132 1.89e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 41.25  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  27 WGSLQGP----PVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHySPGVPYylQTFVSEIRRVVAALKWNRF 102
Cdd:PRK10673    7 AQTAQNPhnnsPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPR-DPVMNY--PAMAQDLLDTLDALQIEKA 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217339456 103 SILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:PRK10673   84 TFIGHSMGGKAVMALTALAPDRIDKLVAID 113
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
35-137 2.57e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.00  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  35 VLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLS----SHYSPgvpyylQTFVSEIRRVVAALK--WNRFSILGH 107
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAKAGYTVyAPRLPGHGTSpedlLKTTW------EDWLEDVEEAYEILKagYDKVIVIGL 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217339456 108 SFGGVVGGMFFCTFPEmVDKLILLDTPLFL 137
Cdd:COG1647    92 SMGGLLALLLAARYPD-VAGLVLLSPALKI 120
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 28-113 3.06e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.00  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  28 GSLQGPPVLCLHG-------WLDNASSFDRLIPLlpqdfyyVAMDFGGHGLSSH-YSPGVPYYLQTFVSEirrVVAALKW 99
Cdd:PRK14875  127 GEGDGTPVVLIHGfggdlnnWLFNHAALAAGRPV-------IALDLPGHGASSKaVGAGSLDELAAAVLA---FLDALGI 196

                          90
                  ....*....|....
gi 2217339456 100 NRFSILGHSFGGVV 113
Cdd:PRK14875  197 ERAHLVGHSMGGAV 210
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 31-138 4.93e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 37.03  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  31 QGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSP-----GVPYYLQTFVSEIRRVVAALKWNRFSIL 105
Cdd:PLN02824   28 SGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPrsappNSFYTFETWGEQLNDFCSDVVGDPAFVI 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217339456 106 GHSFGGVVGGMFFCTFPEMVDKLILLDTPLFLL 138
Cdd:PLN02824  108 CNSVGGVVGLQAAVDAPELVRGVMLINISLRGL 140
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 35-130 5.46e-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: 36.81  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  35 VLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLsshySPGVPYY----------LQTFVSEIRRVVAALKwnRFs 103
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVyAYDHRGHGR----SDGKRGHvpsfddyvddLDTFVDKIREEHPGLP--LF- 79

                          90       100
                  ....*....|....*....|....*..
gi 2217339456 104 ILGHSFGGVVGGMFFCTFPEMVDKLIL 130
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLIL 106
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 5-153 9.53e-03

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: 36.60  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456   5 AAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQD--FYyvamdfgghGLSSHYSPGVPYY 82
Cdd:COG3319   574 AALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDrpVY---------GLQAPGLDGGEPP 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217339456  83 LQTF-------VSEIRRVVAAlkwNRFSILGHSFGGVVGgmFfctfpEM----------VDKLILLDT--PLFLLESDEM 143
Cdd:COG3319   645 PASVeemaaryVEAIRAVQPE---GPYHLLGWSFGGLVA--Y-----EMarqleaqgeeVALLVLLDSyaPGALARLDEA 714

                         170
                  ....*....|
gi 2217339456 144 ENLLTYKRRA 153
Cdd:COG3319   715 ELLAALLRDL 724
 
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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