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Conserved domains on  [gi|18777795|ref|NP_055324|]
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serine hydrolase-like protein 2 isoform a [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427000)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

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 6.84e-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: 99.69  E-value: 6.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596  14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                        90       100       110
                ....*....|....*....|....*....|.
gi 18777795 102 FSILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:COG0596  91 VVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
33-293 6.96e-19

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


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 84.09  E-value: 6.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    33 PPVLCLHGWLDNASSFDRLIPLLPQD-FYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGG 111
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   112 VVGGMFFCTFPEMVDKLILLDTPLFLLESDEMEnlltykrRAIEHVLQVEASQEPSHVFSLKQLLQRLLKSNSHLSEECG 191
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEAD-------RFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   192 ELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHVLLIkavhgyfdsrqnYSEKESLS--FMIDTM 269
Cdd:pfam00561 154 LKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLII------------WGDQDPLVppQALEKL 221
                         250       260
                  ....*....|....*....|....
gi 18777795   270 KSTLKEQFQFVEVPGNHCVHMSEP 293
Cdd:pfam00561 222 AQLFPNARLVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
22-132 6.84e-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: 99.69  E-value: 6.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596  14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                        90       100       110
                ....*....|....*....|....*....|.
gi 18777795 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.
33-293 6.96e-19

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: 84.09  E-value: 6.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    33 PPVLCLHGWLDNASSFDRLIPLLPQD-FYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGG 111
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   112 VVGGMFFCTFPEMVDKLILLDTPLFLLESDEMEnlltykrRAIEHVLQVEASQEPSHVFSLKQLLQRLLKSNSHLSEECG 191
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEAD-------RFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   192 ELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHVLLIkavhgyfdsrqnYSEKESLS--FMIDTM 269
Cdd:pfam00561 154 LKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLII------------WGDQDPLVppQALEKL 221
                         250       260
                  ....*....|....*....|....
gi 18777795   270 KSTLKEQFQFVEVPGNHCVHMSEP 293
Cdd:pfam00561 222 AQLFPNARLVVIPDAGHFAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
32-130 1.32e-13

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: 69.17  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    32 GPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEI-RRVVAALKWNRFSILGHSFG 110
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81
                          90       100
                  ....*....|....*....|
gi 18777795   111 GVVGGMFFCTFPEMVDKLIL 130
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLIL 101
PRK05855 PRK05855
SDR family oxidoreductase;
22-112 3.01e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 63.85  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   22 IAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:PRK05855  15 LAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDR 94
                         90
                 ....*....|..
gi 18777795  102 -FSILGHSFGGV 112
Cdd:PRK05855  95 pVHLLAHDWGSI 106
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
35-114 1.18e-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: 48.62  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    35 VLCLHGWldnASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVpyylqTFVSEIRRVVAALK-WNRFSILGHSFGGVV 113
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDL-----ADLADLAALLDELGaARPVVLVGHSLGGAV 72

                  .
gi 18777795   114 G 114
Cdd:pfam12697  73 A 73
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
5-299 2.10e-06

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: 49.32  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   5 AAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQD--FYyvamdfgghGLSSHYSPGVPYY 82
Cdd:COG3319 574 AALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDrpVY---------GLQAPGLDGGEPP 644
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  83 LQTF-------VSEIRRVVAAlkwNRFSILGHSFGGVVGgmFfctfpEM----------VDKLILLDT--PLFLLESDE- 142
Cdd:COG3319 645 PASVeemaaryVEAIRAVQPE---GPYHLLGWSFGGLVA--Y-----EMarqleaqgeeVALLVLLDSyaPGALARLDEa 714
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795 143 --MENLLTYKRRAIEHVLQVEASQEPShvfslkqllqrllksnshlSEECGELLLQRG-TTKVATGLVLNRDQRLAWAEN 219
Cdd:COG3319 715 elLAALLRDLARGVDLPLDAEELRALD-------------------PEERLARLLERLrEAGLPAGLDAERLRRLLRVFR 775
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795 220 SidfISRELCAHSIRKLQAHVLLIKAVhgyfDSRQNYSEKESLSFmidtmKSTLKEQFQFVEVPGNHcVHMSEPQHVASI 299
Cdd:COG3319 776 A---NLRALRRYRPRPYDGPVLLFRAE----EDPPGRADDPALGW-----RPLVAGGLEVHDVPGDH-FSMLREPHVAEL 842
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
22-132 6.84e-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: 99.69  E-value: 6.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  22 IAAKAWGSlQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHysPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:COG0596  14 LHYREAGP-DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK--PAGGYTLDDLADDLAALLDALGLER 90
                        90       100       110
                ....*....|....*....|....*....|.
gi 18777795 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.
33-293 6.96e-19

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: 84.09  E-value: 6.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    33 PPVLCLHGWLDNASSFDRLIPLLPQD-FYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGG 111
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   112 VVGGMFFCTFPEMVDKLILLDTPLFLLESDEMEnlltykrRAIEHVLQVEASQEPSHVFSLKQLLQRLLKSNSHLSEECG 191
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEAD-------RFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   192 ELLLQRGTTKVATGLVLNRDQRLAWAENSIDFISRELCAHSIRKLQAHVLLIkavhgyfdsrqnYSEKESLS--FMIDTM 269
Cdd:pfam00561 154 LKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLII------------WGDQDPLVppQALEKL 221
                         250       260
                  ....*....|....*....|....
gi 18777795   270 KSTLKEQFQFVEVPGNHCVHMSEP 293
Cdd:pfam00561 222 AQLFPNARLVVIPDAGHFAFLEGP 245
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
32-130 1.32e-13

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: 69.17  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    32 GPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEI-RRVVAALKWNRFSILGHSFG 110
Cdd:TIGR03695   2 KPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAQLLlATLLDQLGIEPFFLVGYSMG 81
                          90       100
                  ....*....|....*....|
gi 18777795   111 GVVGGMFFCTFPEMVDKLIL 130
Cdd:TIGR03695  82 GRIALYYALQYPERVQGLIL 101
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-133 2.26e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 62.33  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  21 HIAAKAWGSLQGP--PVLCLHGWLDNASSFDRLIP-LLPQDFYYVAMDFGGHGLSSHySPGVPYYLQTFVSEIRRVVAAL 97
Cdd:COG2267  15 RLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEaLAAAGYAVLAFDLRGHGRSDG-PRGHVDSFDDYVDDLRAALDAL 93
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18777795  98 KWN---RFSILGHSFGGVVGGMFFCTFPEMVDKLILLDT 133
Cdd:COG2267  94 RARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
PRK05855 PRK05855
SDR family oxidoreductase;
22-112 3.01e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 63.85  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   22 IAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVPYYLQTFVSEIRRVVAALKWNR 101
Cdd:PRK05855  15 LAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDR 94
                         90
                 ....*....|..
gi 18777795  102 -FSILGHSFGGV 112
Cdd:PRK05855  95 pVHLLAHDWGSI 106
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
28-146 4.60e-11

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 62.98  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   28 GSLQGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSS--HYSPGVPYYLQTFVSEIRRVVAALKWNRFSIL 105
Cdd:PLN03084 123 GSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpQPGYGFNYTLDEYVSSLESLIDELKSDKVSLV 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18777795  106 GHSFGGVVGGMFFCTFPEMVDKLILLDTPLflleSDEMENL 146
Cdd:PLN03084 203 VQGYFSPPVVKYASAHPDKIKKLILLNPPL----TKEHAKL 239
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
34-134 6.13e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.83  E-value: 6.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  34 PVLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLSshyspgVPYYLQTFVSEIRRVVAALKWNRFSILGHSFGGV 112
Cdd:COG1075   7 PVVLVHGLGGSAASWAPLAPRLRAAGYPVyALNYPSTNGS------IEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80
                        90       100       110
                ....*....|....*....|....*....|
gi 18777795 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 1.18e-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: 48.62  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    35 VLCLHGWldnASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSPGVpyylqTFVSEIRRVVAALK-WNRFSILGHSFGGVV 113
Cdd:pfam12697   1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDL-----ADLADLAALLDELGaARPVVLVGHSLGGAV 72

                  .
gi 18777795   114 G 114
Cdd:pfam12697  73 A 73
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
5-299 2.10e-06

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: 49.32  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   5 AAPGLISELKLAVPWGHIAAKAWGSLQGPPVLCLHGWLDNASSFDRLIPLLPQD--FYyvamdfgghGLSSHYSPGVPYY 82
Cdd:COG3319 574 AALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDrpVY---------GLQAPGLDGGEPP 644
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  83 LQTF-------VSEIRRVVAAlkwNRFSILGHSFGGVVGgmFfctfpEM----------VDKLILLDT--PLFLLESDE- 142
Cdd:COG3319 645 PASVeemaaryVEAIRAVQPE---GPYHLLGWSFGGLVA--Y-----EMarqleaqgeeVALLVLLDSyaPGALARLDEa 714
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795 143 --MENLLTYKRRAIEHVLQVEASQEPShvfslkqllqrllksnshlSEECGELLLQRG-TTKVATGLVLNRDQRLAWAEN 219
Cdd:COG3319 715 elLAALLRDLARGVDLPLDAEELRALD-------------------PEERLARLLERLrEAGLPAGLDAERLRRLLRVFR 775
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795 220 SidfISRELCAHSIRKLQAHVLLIKAVhgyfDSRQNYSEKESLSFmidtmKSTLKEQFQFVEVPGNHcVHMSEPQHVASI 299
Cdd:COG3319 776 A---NLRALRRYRPRPYDGPVLLFRAE----EDPPGRADDPALGW-----RPLVAGGLEVHDVPGDH-FSMLREPHVAEL 842
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
33-148 3.26e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 48.37  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   33 PPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSH-------YSPGVPYYLQTFvSEIRRvvaALKWNRFSIL 105
Cdd:PLN02894 106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdftcksTEETEAWFIDSF-EEWRK---AKNLSNFILL 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18777795  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 8.02e-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: 46.35  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    31 QGPPVLCL-HGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGlsshYSPGV-PYYLqtfvSEIRRVVAALKWNRFSILGHS 108
Cdd:TIGR01738   2 QGNVHLVLiHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHG----RSRGFgPLSL----ADMAEAIAAQAPDPAIWLGWS 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18777795   109 FGGVVGGMFFCTFPEMVDKLILL-DTPLFLLESD 141
Cdd:TIGR01738  74 LGGLVALHIAATHPDRVRALVTVaSSPCFSARED 107
PRK10673 PRK10673
esterase;
27-132 4.60e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 40.87  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   27 WGSLQGP----PVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHySPGVPYylQTFVSEIRRVVAALKWNRF 102
Cdd:PRK10673   7 AQTAQNPhnnsPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPR-DPVMNY--PAMAQDLLDTLDALQIEKA 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 18777795  103 SILGHSFGGVVGGMFFCTFPEMVDKLILLD 132
Cdd:PRK10673  84 TFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
28-113 3.05e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.77  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   28 GSLQGPPVLCLHG-------WLDNASSFDRLIPLlpqdfyyVAMDFGGHGLSSH-YSPGVPYYLQTFVSEirrVVAALKW 99
Cdd:PRK14875 127 GEGDGTPVVLIHGfggdlnnWLFNHAALAAGRPV-------IALDLPGHGASSKaVGAGSLDELAAAVLA---FLDALGI 196
                         90
                 ....*....|....
gi 18777795  100 NRFSILGHSFGGVV 113
Cdd:PRK14875 197 ERAHLVGHSMGGAV 210
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
35-137 5.09e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 37.61  E-value: 5.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795  35 VLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLS----SHYSPgvpyylQTFVSEIRRVVAALK--WNRFSILGH 107
Cdd:COG1647  18 VLLLHGFTGSPAEMRPLAEALAKAGYTVyAPRLPGHGTSpedlLKTTW------EDWLEDVEEAYEILKagYDKVIVIGL 91
                        90       100       110
                ....*....|....*....|....*....|
gi 18777795 108 SFGGVVGGMFFCTFPEmVDKLILLDTPLFL 137
Cdd:COG1647  92 SMGGLLALLLAARYPD-VAGLVLLSPALKI 120
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
31-138 6.04e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 37.80  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795   31 QGPPVLCLHGWLDNASSFDRLIPLLPQDFYYVAMDFGGHGLSSHYSP-----GVPYYLQTFVSEIRRVVAALKWNRFSIL 105
Cdd:PLN02824  28 SGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPrsappNSFYTFETWGEQLNDFCSDVVGDPAFVI 107
                         90       100       110
                 ....*....|....*....|....*....|...
gi 18777795  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 8.85e-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: 37.19  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777795    35 VLCLHGWLDNASSFDRLIPLLPQDFYYV-AMDFGGHGLsshySPGVPYY----------LQTFVSEIRRVVAALKwnRFs 103
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVyAYDHRGHGR----SDGKRGHvpsfddyvddLDTFVDKIREEHPGLP--LF- 79
                          90       100
                  ....*....|....*....|....*..
gi 18777795   104 ILGHSFGGVVGGMFFCTFPEMVDKLIL 130
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLIL 106
 
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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