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Conserved domains on  [gi|695774597|ref|WP_032697454|]
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MULTISPECIES: alpha/beta fold hydrolase [Pseudomonas]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 6-269 8.16e-47

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: 155.93  E-value: 8.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   6 IDGKTLHYSDQG-TGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGfPEGTRNLDDLARHALALLDHLN 84
Cdd:COG0596    9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGKeteakkayyfsLLDKLEEVGSFPEPLLDIvvpiffrpgidp 164
Cdd:COG0596   88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA-----------LAEPLRRPGLAPEALAAL------------ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 165 hspvytsFRAALAGMNAEQLRQSVVPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMANLI-GCPYVLV 243
Cdd:COG0596  145 -------LRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 695774597 244 PEAGHIANLENPAFVSDALMTFLARV 269
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 6-269 8.16e-47

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: 155.93  E-value: 8.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   6 IDGKTLHYSDQG-TGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGfPEGTRNLDDLARHALALLDHLN 84
Cdd:COG0596    9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGKeteakkayyfsLLDKLEEVGSFPEPLLDIvvpiffrpgidp 164
Cdd:COG0596   88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA-----------LAEPLRRPGLAPEALAAL------------ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 165 hspvytsFRAALAGMNAEQLRQSVVPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMANLI-GCPYVLV 243
Cdd:COG0596  145 -------LRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 695774597 244 PEAGHIANLENPAFVSDALMTFLARV 269
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 10-267 4.34e-37

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 131.71  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   10 TLHYSDQGTG---PVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGdSSGFPEGTRNLDDLARHALALLDHLNIE 86
Cdd:TIGR02427   1 RLHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHG-LSDAPEGPYSIEDLADDVLALLDHLGIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   87 RCSIVGLSVGGMWGAIAALLAPERITGLVLMDT---YLGKETEAKKAyyfsllDKLEEVGSfpEPLLDIVVPIFFRPGI- 162
Cdd:TIGR02427  80 RAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTaakIGTPESWNARI------AAVRAEGL--AALADAVLERWFTPGFr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  163 DPHSPVYTSFRAalagMNAEQLRQSVVPLGRMIFGRD--DRLGLIeqlnADTTLVMCGDADIPRPPEETREMANLI-GCP 239
Cdd:TIGR02427 152 EAHPARLDLYRN----MLVRQPPDGYAGCCAAIRDADfrDRLGAI----AVPTLCIAGDQDGSTPPELVREIADLVpGAR 223

                         250       260
                  ....*....|....*....|....*...
gi 695774597  240 YVLVPEAGHIANLENPAFVSDALMTFLA 267
Cdd:TIGR02427 224 FAEIRGAGHIPCVEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 20-255 8.70e-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: 82.94  E-value: 8.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   20 PVVLLGHSYLWDKAMWSAQIDTLA-SQYRVIVPDLWGHGDSSGFPEGTR-NLDDLARHALALLDHLNIERCSIVGLSVGG 97
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   98 MWGAIAALLAPERITGLVLMDTyLGKETEAKKAYYFSLLDKLEEVGSFPEPllDIVVPIFFRPGIDP-HSPVYTSFRAAL 176
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFDGFVAD--FAPNPLGRLVAKLLaLLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  177 AGMNAEQLRQSVVPLGRMIFGrddRLGLIEQLNAD-----------TTLVMCGDADIPRPPEETREMANLIGCPYVLV-P 244
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVTG---ALLFIETWSTElrakflgrldePTLIIWGDQDPLVPPQALEKLAQLFPNARLVViP 234

                         250
                  ....*....|.
gi 695774597  245 EAGHIANLENP 255
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-116 4.01e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 83.07  E-value: 4.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   6 IDGKTLHYSDQGTG---PVVLLgHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSgfPE-GTRNLDDLARHALALLD 81
Cdd:PRK14875 116 IGGRTVRYLRLGEGdgtPVVLI-HGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS--KAvGAGSLDELAAAVLAFLD 192

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695774597  82 HLNIERCSIVGLSVGGMWGAIAALLAPERITGLVL 116
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL 227
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 6-269 8.16e-47

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: 155.93  E-value: 8.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   6 IDGKTLHYSDQG-TGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGfPEGTRNLDDLARHALALLDHLN 84
Cdd:COG0596    9 VDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLAALLDALG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  85 IERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGKeteakkayyfsLLDKLEEVGSFPEPLLDIvvpiffrpgidp 164
Cdd:COG0596   88 LERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAA-----------LAEPLRRPGLAPEALAAL------------ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 165 hspvytsFRAALAGMNAEQLRQSVVPlgrmifgrddrlglieqlnadtTLVMCGDADIPRPPEETREMANLI-GCPYVLV 243
Cdd:COG0596  145 -------LRALARTDLRERLARITVP----------------------TLVIWGEKDPIVPPALARRLAELLpNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 695774597 244 PEAGHIANLENPAFVSDALMTFLARV 269
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 10-267 4.34e-37

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 131.71  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   10 TLHYSDQGTG---PVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGdSSGFPEGTRNLDDLARHALALLDHLNIE 86
Cdd:TIGR02427   1 RLHYRLDGAAdgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHG-LSDAPEGPYSIEDLADDVLALLDHLGIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   87 RCSIVGLSVGGMWGAIAALLAPERITGLVLMDT---YLGKETEAKKAyyfsllDKLEEVGSfpEPLLDIVVPIFFRPGI- 162
Cdd:TIGR02427  80 RAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTaakIGTPESWNARI------AAVRAEGL--AALADAVLERWFTPGFr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  163 DPHSPVYTSFRAalagMNAEQLRQSVVPLGRMIFGRD--DRLGLIeqlnADTTLVMCGDADIPRPPEETREMANLI-GCP 239
Cdd:TIGR02427 152 EAHPARLDLYRN----MLVRQPPDGYAGCCAAIRDADfrDRLGAI----AVPTLCIAGDQDGSTPPELVREIADLVpGAR 223

                         250       260
                  ....*....|....*....|....*...
gi 695774597  240 YVLVPEAGHIANLENPAFVSDALMTFLA 267
Cdd:TIGR02427 224 FAEIRGAGHIPCVEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 20-255 8.70e-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: 82.94  E-value: 8.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   20 PVVLLGHSYLWDKAMWSAQIDTLA-SQYRVIVPDLWGHGDSSGFPEGTR-NLDDLARHALALLDHLNIERCSIVGLSVGG 97
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   98 MWGAIAALLAPERITGLVLMDTyLGKETEAKKAYYFSLLDKLEEVGSFPEPllDIVVPIFFRPGIDP-HSPVYTSFRAAL 176
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFPGFFDGFVAD--FAPNPLGRLVAKLLaLLLLRLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  177 AGMNAEQLRQSVVPLGRMIFGrddRLGLIEQLNAD-----------TTLVMCGDADIPRPPEETREMANLIGCPYVLV-P 244
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVTG---ALLFIETWSTElrakflgrldePTLIIWGDQDPLVPPQALEKLAQLFPNARLVViP 234

                         250
                  ....*....|.
gi 695774597  245 EAGHIANLENP 255
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 6-116 4.01e-18

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 83.07  E-value: 4.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   6 IDGKTLHYSDQGTG---PVVLLgHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSgfPE-GTRNLDDLARHALALLD 81
Cdd:PRK14875 116 IGGRTVRYLRLGEGdgtPVVLI-HGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS--KAvGAGSLDELAAAVLAFLD 192

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695774597  82 HLNIERCSIVGLSVGGMWGAIAALLAPERITGLVL 116
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL 227
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
7-121 3.82e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 69.65  E-value: 3.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   7 DGKTLHY----SDQGTGPVVLLGHSYLWDKAMWSAQIDTLASQ-YRVIVPDLWGHGDSSGFPEGTRNLDDLARHALALLD 81
Cdd:COG2267   12 DGLRLRGrrwrPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALD 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695774597  82 HLNIE---RCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:COG2267   92 ALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAY 134
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-121 1.04e-12

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 66.56  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   1 MPDLLIDGKTLHYSDQGTGPVVLLGH-----SYLWDKAMwsaqiDTLASQYRVIVPDLWGHGDsSGFPEGTRNLDDLARH 75
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHgnptsSYLWRNII-----PHLAGLGRCLAPDLIGMGA-SDKPDIDYTFADHARY 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 695774597  76 ALALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:PRK03592  83 LDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIV 128
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
7-268 3.96e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.27  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   7 DGKTLHY-----SDQGTGPVVLLGHSYLWDKA-MWSAQIDTLASQ-YRVIVPDLWGHGDSSGFPeGTRNLDDL--ARHAL 77
Cdd:COG1506    6 DGTTLPGwlylpADGKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGYGESAGDW-GGDEVDDVlaAIDYL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  78 ALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMdtylgketeakkAYYFSLLDKLEEVGSFPEPLLDivVPIF 157
Cdd:COG1506   85 AARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVAL------------AGVSDLRSYYGTTREYTERLMG--GPWE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 158 FRPGIDPHSPVYtsfraalagmNAEQLRqsvVPLgrmifgrddrlglieqlnadttLVMCGDADIPRPPEETREMAN--- 234
Cdd:COG1506  151 DPEAYAARSPLA----------YADKLK---TPL----------------------LLIHGEADDRVPPEQAERLYEalk 195

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 695774597 235 LIGCP--YVLVPEAGH-IANLENPAFVsDALMTFLAR 268
Cdd:COG1506  196 KAGKPveLLVYPGEGHgFSGAGAPDYL-ERILDFLDR 231
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 8-268 5.27e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 58.60  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   8 GKTLHYSDQGT-GPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHG-----DSSGFPEGT-RNLDDLARHALALL 80
Cdd:PLN02824  17 GYNIRYQRAGTsGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGysdkpNPRSAPPNSfYTFETWGEQLNDFC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  81 DHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLG----------------------KETEAKKAyYFSLLDK 138
Cdd:PLN02824  97 SDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRglhikkqpwlgrpfikafqnllRETAVGKA-FFKSVAT 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 139 LEEVGSF-------PEPLLDIVVPIFFRPGIDPHS-PVYTSFRAALAG-MNAEQLRQSVVPLgrmifgrddrlglieqln 209
Cdd:PLN02824 176 PETVKNIlcqcyhdDSAVTDELVEAILRPGLEPGAvDVFLDFISYSGGpLPEELLPAVKCPV------------------ 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 210 adttLVMCGDADIPRPPEETREMANLIGC-PYVLVPEAGHIANLENPAFVSDALMTFLAR 268
Cdd:PLN02824 238 ----LIAWGEKDPWEPVELGRAYANFDAVeDFIVLPGVGHCPQDEAPELVNPLIESFVAR 293
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
42-269 6.50e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 54.95  E-value: 6.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  42 LASQ-YRVIVPDLWGHGDSSGFPEGTRnLDDLARHALALLDHL--NIERCSIVGLSVGgmwGAIAALLAPER--ITGLVL 116
Cdd:COG1647   38 LAKAgYTVYAPRLPGHGTSPEDLLKTT-WEDWLEDVEEAYEILkaGYDKVIVIGLSMG---GLLALLLAARYpdVAGLVL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 117 MDTYLgketeakkayyfslldKLEEVGSFPEPLLDIVVPIFFRPGIDPHSPvyTSFRAALAGMNAEQLRQsvvpLGRMIf 196
Cdd:COG1647  114 LSPAL----------------KIDDPSAPLLPLLKYLARSLRGIGSDIEDP--EVAEYAYDRTPLRALAE----LQRLI- 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695774597 197 grDDRLGLIEQLNADtTLVMCGDADIPRPPEETREMANLIGCP---YVLVPEAGH-IANLENPAFVSDALMTFLARV 269
Cdd:COG1647  171 --REVRRDLPKITAP-TLIIQSRKDEVVPPESARYIYERLGSPdkeLVWLEDSGHvITLDKDREEVAEEILDFLERL 244
PRK10673 PRK10673
esterase;
42-118 7.99e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 55.12  E-value: 7.99e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695774597  42 LASQYRVIVPDLWGHGDSSGFPEgtRNLDDLARHALALLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMD 118
Cdd:PRK10673  39 LVNDHDIIQVDMRNHGLSPRDPV--MNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAID 113
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 11-131 8.53e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 55.25  E-value: 8.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  11 LHYSDQGTGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDS---SGFpegTRNLDDLARHALALLDHLNIER 87
Cdd:PRK03204  26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSerpSGF---GYQIDEHARVIGEFVDHLGLDR 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695774597  88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL-GKETEAKKAY 131
Cdd:PRK03204 103 YLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFwPADTLAMKAF 147
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 18-268 1.64e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 54.07  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  18 TGPVVLLGHSYLWDKAMWSAQIDTLaSQYRVIVPDLWGHGDSSGFPegTRNLDDLARHALALLDHLNIERCSIVGLSVGG 97
Cdd:PRK11126   1 GLPWLVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAIS--VDGFADVSRLLSQTLQSYNILPYWLVGYSLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  98 ---MWGAIAALlaPERITGLVLMDTYLGKETEAKK----------AYYFSlldkleevgsfPEPLLDiVVPIFFRpgidp 164
Cdd:PRK11126  78 riaMYYACQGL--AGGLCGLIVEGGNPGLQNAEERqarwqndrqwAQRFR-----------QEPLEQ-VLADWYQ----- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 165 hSPVYTSfraalagMNAEQlRQSVVPLgrmifgRDDRLG-----------------LIEQLNADTT--LVMCGDADiprp 225
Cdd:PRK11126 139 -QPVFAS-------LNAEQ-RQQLVAK------RSNNNGaavaamleatslakqpdLRPALQALTFpfYYLCGERD---- 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 695774597 226 pEETREMANLIGCPYVLVPEAGHIANLENPAFVSDALMTFLAR 268
Cdd:PRK11126 200 -SKFQALAQQLALPLHVIPNAGHNAHRENPAAFAASLAQILRL 241
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 7-268 8.00e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.84  E-value: 8.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   7 DGKTLH---Y---SDQGTGPVVLLGHSYLWDKAMWSAQIDTLASQ-YRVIVPDLWGHGDSSGFPegtRNLDDLARH-ALA 78
Cdd:COG1073   19 DGIKLAgdlYlpaGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEGEP---REEGSPERRdARA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  79 LLDHL----NIERCSIV--GLSvggMWGAIAALLAPE--RITGLVLMDTYLGKETEAKkayyfsllDKLEEVGSFPEPLL 150
Cdd:COG1073   96 AVDYLrtlpGVDPERIGllGIS---LGGGYALNAAATdpRVKAVILDSPFTSLEDLAA--------QRAKEARGAYLPGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597 151 DivvpifFRPGIdphspvyTSFRAALAGMNA-EQLRQSVVPLgRMIFGRDDRLGlieqlnadttlvmcgdadiprPPEET 229
Cdd:COG1073  165 P------YLPNV-------RLASLLNDEFDPlAKIEKISRPL-LFIHGEKDEAV---------------------PFYMS 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 695774597 230 REMANLIGCP--YVLVPEAGHI-ANLENPAFVSDALMTFLAR 268
Cdd:COG1073  210 EDLYEAAAEPkeLLIVPGAGHVdLYDRPEEEYFDKLAEFFKK 251
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 42-261 1.35e-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: 50.94  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   42 LASQYRVIVPDLWGHGDSSGFPEGTRNLDDLARHALALLDHLNIercSIVGLSVGGMwgaIAALLAPERITGLVLMDTyl 121
Cdd:pfam12697  18 LAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPV---VLVGHSLGGA---VALAAAAAALVVGVLVAP-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  122 gketeakkayyfslldkleevGSFPEPLLDIVVPIFFRPGIDPHSPVYTSFRAALAGM-----NAEQLRQSVVPLGRMIF 196
Cdd:pfam12697  90 ---------------------LAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFlddlpADAEWAAALARLAALLA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695774597  197 GRD-DRLGLIEQLNADTTLVMCGDADIPRPPEetREMANLIGCPYVLVPEAGHiANLENPAFVSDA 261
Cdd:pfam12697 149 ALAlLPLAAWRDLPVPVLVLAEEDRLVPELAQ--RLLAALAGARLVVLPGAGH-LPLDDPEEVAEA 211
PRK05855 PRK05855
SDR family oxidoreductase;
7-104 2.51e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 48.44  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   7 DGKTLHYSDQG--TGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGfPEGTRN--LDDLARHALALLDH 82
Cdd:PRK05855  11 DGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSA-PKRTAAytLARLADDFAAVIDA 89

                         90       100
                 ....*....|....*....|..
gi 695774597  83 LNIERcsIVGLsVGGMWGAIAA 104
Cdd:PRK05855  90 VSPDR--PVHL-LAHDWGSIQG 108
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 11-121 2.78e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 47.66  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  11 LHYSDQGT--GPVVLLGH-----SYLWDKaMwsaqIDTLASQ-YRVIVPDLWGHGDSSgfpEGTRNLD-DLARHA---LA 78
Cdd:PRK00870  36 MHYVDEGPadGPPVLLLHgepswSYLYRK-M----IPILAAAgHRVIAPDLIGFGRSD---KPTRREDyTYARHVewmRS 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695774597  79 LLDHLNIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYL 121
Cdd:PRK00870 108 WFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTGL 150
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 15-269 6.62e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 47.16  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   15 DQGTGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGFPEGTRN-------LDDLARHALALLDHLNIER 87
Cdd:PLN02980 1367 QNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAKETqteptlsVELVADLLYKLIEHITPGK 1446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   88 CSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLG-KETEAKKayYFSLLDKleevgSFPEPLLDIVVPIFFR------- 159
Cdd:PLN02980 1447 VTLVGYSMGARIALYMALRFSDKIEGAVIISGSPGlKDEVARK--IRSAKDD-----SRARMLIDHGLEIFLEnwysgel 1519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  160 -------PGIDP-------HSPVYtSFRAALAGMNA-------EQLRQSVVPLgRMIFG-RDDRLGLIEQlnadttlVMC 217
Cdd:PLN02980 1520 wkslrnhPHFNKivasrllHKDVP-SLAKLLSDLSIgrqpslwEDLKQCDTPL-LLVVGeKDVKFKQIAQ-------KMY 1590

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 695774597  218 gdADIPRPPEETREMANLIgCPYVLVPEAGHIANLENPAFVSDALMTFLARV 269
Cdd:PLN02980 1591 --REIGKSKESGNDKGKEI-IEIVEIPNCGHAVHLENPLPVIRALRKFLTRL 1639
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 52-248 1.13e-04

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: 42.59  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   52 DLWGHGDSSGFPEGTRNLDDLARHALALLDHL----NIERCSIVGLSVGGMWGAIAALLAPERITGLVLMDTYLGketea 127
Cdd:pfam12146  38 DHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIreehPGLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALK----- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  128 KKAYYFSLLDKLEevgsfpEPLLDIVVP-IFFRPGIDPHSPvyTSFRAALAGMNAEQLRQSVVPLGrmiFGRDDRLG--- 203
Cdd:pfam12146 113 IKPYLAPPILKLL------AKLLGKLFPrLRVPNNLLPDSL--SRDPEVVAAYAADPLVHGGISAR---TLYELLDAger 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 695774597  204 LIEQLNADT--TLVMCGDADIPRPPEETREMANLIGCP---YVLVPEAGH 248
Cdd:pfam12146 182 LLRRAAAITvpLLLLHGGADRVVDPAGSREFYERAGSTdktLKLYPGLYH 231
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
16-115 2.11e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 41.93  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  16 QGTGPVVLLgHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGFpeGTRNLDDLARHALALLDhlniERCSIVGLSV 95
Cdd:PRK10349  11 QGNVHLVLL-HGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGF--GALSLADMAEAVLQQAP----DKAIWLGWSL 83

                         90       100
                 ....*....|....*....|
gi 695774597  96 GGMWGAIAALLAPERITGLV 115
Cdd:PRK10349  84 GGLVASQIALTHPERVQALV 103
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 46-117 8.79e-04

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 40.03  E-value: 8.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695774597   46 YRVIVPdlwGHGD-SSGFPEGTR--NLDDLARHALALLDHLNIErcSIVGLSVGGmwGA-IAALLA---PERITGLVLM 117
Cdd:pfam03096  59 YHVDAP---GQEDgAASFPGGYPypSMDDLADMLPVVLDHFRLK--SVIGMGVGA--GAyILARFAlkhPERVEGLVLI 130
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 14-118 9.90e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 40.21  E-value: 9.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  14 SDQGTGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHGDSSGFPEGTRNLDDLARHALALLDHLNIERCSIVGL 93
Cdd:PLN02679  83 EVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPGFSYTMETWAELILDFLEEVVQKPTVLIGN 162

                         90       100
                 ....*....|....*....|....*.
gi 695774597  94 SVGGMWGAIAALLAPER-ITGLVLMD 118
Cdd:PLN02679 163 SVGSLACVIAASESTRDlVRGLVLLN 188
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
15-109 1.21e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.18  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  15 DQGTGPVVLLGH------SYLWDKAmwsaqiDTLASQ-YRVIVPDLWGHGDSSGFPE------GTRNLDDLARHALALLD 81
Cdd:COG0412   25 GGGPRPGVVVLHeifglnPHIRDVA------RRLAAAgYVVLAPDLYGRGGPGDDPDearalmGALDPELLAADLRAALD 98

                         90       100       110
                 ....*....|....*....|....*....|....
gi 695774597  82 HL------NIERCSIVGLSVGGMWGAIAALLAPE 109
Cdd:COG0412   99 WLkaqpevDAGRVGVVGFCFGGGLALLAAARGPD 132
PRK06489 PRK06489
hypothetical protein; Provisional
 1-100 1.53e-03

hypothetical protein; Provisional


Pssm-ID: 235815 [Multi-domain]  Cd Length: 360  Bit Score: 39.58  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597   1 MPDLlidgkTLHYSDQGT---------GPVVLLGH-SYLWDKAMWSAQI-DTL--------ASQYRVIVPDLWGHGDSSG 61
Cdd:PRK06489  47 LPEL-----RLHYTTLGTphrnadgeiDNAVLVLHgTGGSGKSFLSPTFaGELfgpgqpldASKYFIILPDGIGHGKSSK 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695774597  62 FPEGTR------NLDD--LARHALaLLDHLNIERCS-IVGLSVGGM----WG 100
Cdd:PRK06489 122 PSDGLRaafpryDYDDmvEAQYRL-VTEGLGVKHLRlILGTSMGGMhawmWG 172
PRK08775 PRK08775
homoserine O-succinyltransferase;
44-116 1.97e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 39.00  E-value: 1.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695774597  44 SQYRVIVPDLWGHGDSSGFPEGTRnldDLARHALALLDHLNIERCS-IVGLSVGGMWGAIAALLAPERITGLVL 116
Cdd:PRK08775  98 ARFRLLAFDFIGADGSLDVPIDTA---DQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVV 168
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
 15-116 8.90e-03

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 37.09  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695774597  15 DQGTGPVVLLGHSYLWDKAMWSAQIDTLASQYRVIVPDLWGHG-------DSSGFPEG------TRNLDDLARH------ 75
Cdd:COG3458   78 GEGPLPAVVEFHGYGGGRGLPHEDLDWAAAGYAVLVMDTRGQGsswgdtpDPGGYSGGalpgymTRGIDDPDTYyyrrvy 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 695774597  76 --------ALALLDHLNIERCSIVGLSVGGMWGAIAALLAPeRITGLVL 116
Cdd:COG3458  158 ldavravdALRSLPEVDGKRIGVTGGSQGGGLALAAAALDP-RVKAAAA 205
 
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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