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Conserved domains on  [gi|515630477|ref|WP_017063077|]
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MULTISPECIES: pimeloyl-ACP methyl ester esterase BioH [Vibrio]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 11-256 4.95e-117

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 TIGR01738:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 334.86  E-value: 4.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   11 GQG-PDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAPKQAIWVGWSLGGLVAT 89
Cdd:TIGR01738   1 GQGnVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   90 HMALHHSDYVSKLVTVASSPKFAAAKEpvlWR-GIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQLKQAV 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED---WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  169 LSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQSSHAPFMTEADAF 248
Cdd:TIGR01738 158 LARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAF 237


                  ....*...
gi 515630477  249 CSELVSFA 256
Cdd:TIGR01738 238 CALLVAFK 245
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 11-256 4.95e-117

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: 334.86  E-value: 4.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   11 GQG-PDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAPKQAIWVGWSLGGLVAT 89
Cdd:TIGR01738   1 GQGnVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   90 HMALHHSDYVSKLVTVASSPKFAAAKEpvlWR-GIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQLKQAV 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED---WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  169 LSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQSSHAPFMTEADAF 248
Cdd:TIGR01738 158 LARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAF 237


                  ....*...
gi 515630477  249 CSELVSFA 256
Cdd:TIGR01738 238 CALLVAFK 245
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
5-258 1.97e-95

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 280.75  E-value: 1.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   5 LYWHVSGQGP-DLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAPKQAIWVGWSL 83
Cdd:PRK10349   4 IWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  84 GGLVATHMALHHSDYVSKLVTVASSPKFAAAKEpvlWRGIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQ 163
Cdd:PRK10349  84 GGLVASQIALTHPERVQALVTVASSPCFSARDE---WPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 164 LKQAVLSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQSSHAPFMT 243
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                        250
                 ....*....|....*
gi 515630477 244 EADAFCSELVSFAQK 258
Cdd:PRK10349 241 HPAEFCHLLVALKQR 255
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 5-258 7.74e-41

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: 139.75  E-value: 7.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   5 LYWHVSG-QGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHC--------HAQDLEEIAQQLLAEapkQ 75
Cdd:COG0596   14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaggytlddLADDLAALLDALGLE---R 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  76 AIWVGWSLGGLVATHMALHHSDYVSKLVTVAsspkfaaakepvlwrgiqpnvlsafteqlvedfqttierfmalqamgsp 155
Cdd:COG0596   91 VVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 156 sarqDVKQLKQAVLSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQ 235
Cdd:COG0596  122 ----EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                        250       260
                 ....*....|....*....|...
gi 515630477 236 SSHAPFMTEADAFCSELVSFAQK 258
Cdd:COG0596  198 AGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-245 1.70e-27

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: 106.05  E-value: 1.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   16 LVLVHGWGMNGAVWQQTVNALQ-ADFRVHVVDLPGYGHS----------AHCHAQDLEEIAQQLLaeaPKQAIWVGWSLG 84
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSsrpkaqddyrTDDLAEDLEYILEALG---LEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   85 GLVATHMALHHSDYVSKLVTVASSPKFAaakEPVLWRGIQPNVLSAFTEQLVEDF-QTTIERFMALQAMGSPSARQDVKQ 163
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPH---ELDEADRFILALFPGFFDGFVADFaPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  164 LKQAVLSRP---LPNPDSLLAGLKM----LSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQS 236
Cdd:pfam00561 157 LPLLNKRFPsgdYALAKSLVTGALLfietWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDA 236


                  ....*....
gi 515630477  237 SHAPFMTEA 245
Cdd:pfam00561 237 GHFAFLEGP 245
 
Name Accession Description Interval E-value
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 11-256 4.95e-117

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: 334.86  E-value: 4.95e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   11 GQG-PDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAPKQAIWVGWSLGGLVAT 89
Cdd:TIGR01738   1 GQGnVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   90 HMALHHSDYVSKLVTVASSPKFAAAKEpvlWR-GIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQLKQAV 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSARED---WPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  169 LSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQSSHAPFMTEADAF 248
Cdd:TIGR01738 158 LARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAF 237


                  ....*...
gi 515630477  249 CSELVSFA 256
Cdd:TIGR01738 238 CALLVAFK 245
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
5-258 1.97e-95

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 280.75  E-value: 1.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   5 LYWHVSGQGP-DLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAPKQAIWVGWSL 83
Cdd:PRK10349   4 IWWQTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  84 GGLVATHMALHHSDYVSKLVTVASSPKFAAAKEpvlWRGIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQ 163
Cdd:PRK10349  84 GGLVASQIALTHPERVQALVTVASSPCFSARDE---WPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 164 LKQAVLSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQSSHAPFMT 243
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                        250
                 ....*....|....*
gi 515630477 244 EADAFCSELVSFAQK 258
Cdd:PRK10349 241 HPAEFCHLLVALKQR 255
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 5-258 7.74e-41

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: 139.75  E-value: 7.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   5 LYWHVSG-QGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHC--------HAQDLEEIAQQLLAEapkQ 75
Cdd:COG0596   14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaggytlddLADDLAALLDALGLE---R 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  76 AIWVGWSLGGLVATHMALHHSDYVSKLVTVAsspkfaaakepvlwrgiqpnvlsafteqlvedfqttierfmalqamgsp 155
Cdd:COG0596   91 VVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 156 sarqDVKQLKQAVLSRPLPNPDSLLAGLKMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQ 235
Cdd:COG0596  122 ----EVLAALAEPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                        250       260
                 ....*....|....*....|...
gi 515630477 236 SSHAPFMTEADAFCSELVSFAQK 258
Cdd:COG0596  198 AGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-245 1.70e-27

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: 106.05  E-value: 1.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   16 LVLVHGWGMNGAVWQQTVNALQ-ADFRVHVVDLPGYGHS----------AHCHAQDLEEIAQQLLaeaPKQAIWVGWSLG 84
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRGFGKSsrpkaqddyrTDDLAEDLEYILEALG---LEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   85 GLVATHMALHHSDYVSKLVTVASSPKFAaakEPVLWRGIQPNVLSAFTEQLVEDF-QTTIERFMALQAMGSPSARQDVKQ 163
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGALDPPH---ELDEADRFILALFPGFFDGFVADFaPNPLGRLVAKLLALLLLRLRLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  164 LKQAVLSRP---LPNPDSLLAGLKM----LSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHTEQYIFTQS 236
Cdd:pfam00561 157 LPLLNKRFPsgdYALAKSLVTGALLfietWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDA 236


                  ....*....
gi 515630477  237 SHAPFMTEA 245
Cdd:pfam00561 237 GHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
13-258 2.00e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.81  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  13 GPDLVLVHGWGMNGAVWQQTVNAL-QADFRVHVVDLPGYGHSAHCH---------AQDLEEIAQQLLAEAPKQAIWVGWS 82
Cdd:COG2267   28 RGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRghvdsfddyVDDLRAALDALRARPGLPVVLLGHS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  83 LGGLVATHMALHHSDYVSKLvtVASSPKFAAakepvlwrgiqpnvlsafteqlvedfqttierfmalQAMGSPSARqdvk 162
Cdd:COG2267  108 MGGLIALLYAARYPDRVAGL--VLLAPAYRA------------------------------------DPLLGPSAR---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 163 qlkqavlsrplpnpdsllaglkMLSDVDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTAL-PHTEQYIFTQSSHAPF 241
Cdd:COG2267  146 ----------------------WLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELL 203

                        250
                 ....*....|....*...
gi 515630477 242 M-TEADAFCSELVSFAQK 258
Cdd:COG2267  204 NePAREEVLAAILAWLER 221
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-258 1.44e-14

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 71.13  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  17 VLVHGWGMNGAVWQQTVNAL-QADFRVHVVDLPGYGHS----AHCHAQD----LEEIAQQLLAEAPKQAIwVGWSLGGLV 87
Cdd:COG1647   19 LLLHGFTGSPAEMRPLAEALaKAGYTVYAPRLPGHGTSpedlLKTTWEDwledVEEAYEILKAGYDKVIV-IGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  88 ATHMALHHSDyVSKLVTVASSPKFAAakepvlWRGIQPNVLSAFTEQLvedfqttierfmalqaMGSPSARQDVKQLKQA 167
Cdd:COG1647   98 ALLLAARYPD-VAGLVLLSPALKIDD------PSAPLLPLLKYLARSL----------------RGIGSDIEDPEVAEYA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 168 VLSRPLPnpdSLLAGLKMLSDVdlREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHT--EQYIFTQSSHapFMT-- 243
Cdd:COG1647  155 YDRTPLR---ALAELQRLIREV--RRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGH--VITld 227

                        250
                 ....*....|....*.
gi 515630477 244 -EADAFCSELVSFAQK 258
Cdd:COG1647  228 kDREEVAEEILDFLER 243
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 13-95 2.28e-14

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 70.25  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  13 GPDLVLVHGWGMNGAVWQQTVNALQaDFRVHVVDLPGYGHSAHCHAQDLEEIAQQL---LAEAPKQAIW-VGWSLGGLVA 88
Cdd:PRK11126   2 LPWLVFLHGLLGSGQDWQPVGEALP-DYPRLYIDLPGHGGSAAISVDGFADVSRLLsqtLQSYNILPYWlVGYSLGGRIA 80


                 ....*..
gi 515630477  89 THMALHH 95
Cdd:PRK11126  81 MYYACQG 87
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 11-258 2.64e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.51  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  11 GQGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAH-CHAQDLEEIAQQLLA----EAPKQAIWVGWSLGG 85
Cdd:PRK14875 129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKaVGAGSLDELAAAVLAfldaLGIERAHLVGHSMGG 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  86 LVATHMALHHSDYVSKLVTVASSpkfaaakepvlwrGIQPNVLSAFTEQLVE-----DFQTTIERFMALQAMGSPSARQD 160
Cdd:PRK14875 209 AVALRLAARAPQRVASLTLIAPA-------------GLGPEINGDYIDGFVAaesrrELKPVLELLFADPALVTRQMVED 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 161 VKQLKQAvlsrplpnpDSLLAGLKMLSD---------VDLREQLPEISVPMLRLYGRLDGLVPIKVAKDLGtalPHTEQY 231
Cdd:PRK14875 276 LLKYKRL---------DGVDDALRALADalfaggrqrVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP---DGVAVH 343

                        250       260
                 ....*....|....*....|....*..
gi 515630477 232 IFTQSSHAPFMTEADAFCSELVSFAQK 258
Cdd:PRK14875 344 VLPGAGHMPQMEAAADVNRLLAEFLGK 370
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 16-107 3.22e-14

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 66.78  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  16 LVLVHGWGMNGAVWQQTVNALQAD-FRVHVVDLPGYGHSAHCHAQDLEEIAQQLLAEAP-KQAIWVGWSLGGLVATHMAL 93
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGaEKVDLVGHSMGGLVARYYLK 87

                         90
                 ....*....|....*.
gi 515630477  94 HHS--DYVSKLVTVAS 107
Cdd:COG1075   88 RLGgaAKVARVVTLGT 103
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 16-228 3.70e-11

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: 61.46  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   16 LVLVHGWGMNGAVWQQTVNAL-QADFRVHVVDLPGYGHS--AHCHA-------QDLEEIAQQLLAEAPKQAIWV-GWSLG 84
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALaAQGFAVYAYDHRGHGRSdgKRGHVpsfddyvDDLDTFVDKIREEHPGLPLFLlGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   85 GLVATHMALHHSDYVSKLVTVAsspkfaaakePVLWrgIQPNVLSAFTEQLVEDFQTTIERfMALQAMGSPSARQD---- 160
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILSA----------PALK--IKPYLAPPILKLLAKLLGKLFPR-LRVPNNLLPDSLSRdpev 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515630477  161 VKQLKQAVLSRPLPNPDSLLAGLKMLSDVdlREQLPEISVPMLRLYGRLDGLVPIKVAKDLGTALPHT 228
Cdd:pfam12146 154 VAAYAADPLVHGGISARTLYELLDAGERL--LRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGST 219
PLN02578 PLN02578
hydrolase
 9-214 5.31e-11

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 61.78  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   9 VSGQGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHS--------AHCHAQDLEEIAQQLLAEapkQAIWVG 80
Cdd:PLN02578  82 VQGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSdkalieydAMVWRDQVADFVKEVVKE---PAVLVG 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  81 WSLGGLVATHMALHHSDYVSKLVTVASSPKFAAAKEP-------------------------------VLWRGIQPNVLS 129
Cdd:PLN02578 159 NSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREkeeaivveetvltrfvvkplkewfqrvvlgfLFWQAKQPSRIE 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 130 AFTEQLVEDfQTTIERFMaLQAMGSPSARQDVKQLKQAVLSRPLPNPdsllaglkmlSDVDLREQLPEISVPMLRLYGRL 209
Cdd:PLN02578 239 SVLKSVYKD-KSNVDDYL-VESITEPAADPNAGEVYYRLMSRFLFNQ----------SRYTLDSLLSKLSCPLLLLWGDL 306


                 ....*
gi 515630477 210 DGLVP 214
Cdd:PLN02578 307 DPWVG 311
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 17-109 4.11e-10

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 59.87  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   17 VLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHS---AHCHAQDLE-EIAQQLLAEA---------PKQAIWVGWSL 83
Cdd:PLN02980 1375 LFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqNHAKETQTEpTLSVELVADLlykliehitPGKVTLVGYSM 1454

                          90       100
                  ....*....|....*....|....*.
gi 515630477   84 GGLVATHMALHHSDYVSKLVTVASSP 109
Cdd:PLN02980 1455 GARIALYMALRFSDKIEGAVIISGSP 1480
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 14-252 5.31e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 59.15  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  14 PDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAH----CHAQD------LEEIAQQLLAEAPKQAIWVGWSL 83
Cdd:PLN02894 106 PTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdftCKSTEeteawfIDSFEEWRKAKNLSNFILLGHSF 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  84 GGLVATHMALHHSDYVSKLVTVASS--PKFAAAKEPVL------WRGIQPNVL--SAFTEQ------------LVedFQT 141
Cdd:PLN02894 186 GGYVAAKYALKHPEHVQHLILVGPAgfSSESDDKSEWLtkfratWKGAVLNHLweSNFTPQkiirglgpwgpnLV--RRY 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 142 TIERFMAlQAMGSPSARQDVKQLKQAVLSrPLPNPDSLLAGLKML------SDVDLREQLPEISVPMLRLYGRLDGLVP- 214
Cdd:PLN02894 264 TTARFGA-HSTGDILSEEESKLLTDYVYH-TLAAKASGELCLKYIfsfgafARKPLLESASEWKVPTTFIYGRHDWMNYe 341

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 515630477 215 --IKVAKDLgtALPhTEQYIFTQSSHAPFMTEADAFCSEL 252
Cdd:PLN02894 342 gaVEARKRM--KVP-CEIIRVPQGGHFVFLDNPSGFHSAV 378
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 16-177 1.05e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 56.71  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   16 LVLVHGWGMNGAVWQQtvnALQADFRVHVVDLPGYGHSAHCH-----AQDLEEIAQQLLAEAPkqAIWVGWSLGGLVATH 90
Cdd:pfam12697   1 VVLVHGAGLSAAPLAA---LLAAGVAVLAPDLPGHGSSSPPPldladLADLAALLDELGAARP--VVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   91 MALHhsdyvSKLVTVASSPKFAAAKEPVLWRGIQPNVLSAFTEQLVEDFQTTIERFMALQAMGSPSARQDVKQLKQAVLS 170
Cdd:pfam12697  76 AAAA-----ALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAAL 150


                  ....*..
gi 515630477  171 RPLPNPD 177
Cdd:pfam12697 151 ALLPLAA 157
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 6-53 6.04e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 52.43  E-value: 6.04e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515630477   6 YWHVSGQGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHS 53
Cdd:PLN02824  22 YQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYS 69
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
14-169 7.46e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.86  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  14 PDLVLVHGWGMNGAV-WQQTVNAL-QADFRVHVVDLPGYGHSAHCH----AQDLEEIAQQLLAEA---PKQAIWVGWSLG 84
Cdd:COG1506   24 PVVVYVHGGPGSRDDsFLPLAQALaSRGYAVLAPDYRGYGESAGDWggdeVDDVLAAIDYLAARPyvdPDRIGIYGHSYG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  85 GLVATHMALHHSDYVSKLVTVASSPKFAAAKEPVLWrgiqpnvlsaFTEQLVEDFQTTIERFMALqamgSPSARqdVKQL 164
Cdd:COG1506  104 GYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTRE----------YTERLMGGPWEDPEAYAAR----SPLAY--ADKL 167


                 ....*
gi 515630477 165 KQAVL 169
Cdd:COG1506  168 KTPLL 172
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 9-240 6.77e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 43.29  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   9 VSGQGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHS--AHCHAQDLEEIAQQLL----AEAPKQAIWVGWS 82
Cdd:PLN02679  84 VTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASdkPPGFSYTMETWAELILdfleEVVQKPTVLIGNS 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  83 LGGLVATHMALHHS-DYVSKLVTVASSP-------------KFAAakePVLW--------RGIQP-------------NV 127
Cdd:PLN02679 164 VGSLACVIAASESTrDLVRGLVLLNCAGgmnnkavvddwriKLLL---PLLWlidfllkqRGIASalfnrvkqrdnlkNI 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477 128 LS-------AFTEQLVEDFQTTIERFMALQAMGSpsarqdvkqlkqAVLSRPLPNPDSLlaglkmlsdvdlreqLPEISV 200
Cdd:PLN02679 241 LLsvygnkeAVDDELVEIIRGPADDEGALDAFVS------------IVTGPPGPNPIKL---------------IPRISL 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 515630477 201 PMLRLYGRLDGLVPI-----KVAKDLGTALPHTEQYIFTQSSHAP 240
Cdd:PLN02679 294 PILVLWGDQDPFTPLdgpvgKYFSSLPSQLPNVTLYVLEGVGHCP 338
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-85 2.82e-04

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 41.28  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   4 ALYWHVSGQGPD--LVLVHGWG-------MNGAVWQqtvnALQADFRVHVVDLPGYGHSAH--------CHAQDLEEIAQ 66
Cdd:COG0429   50 DLDWSDPPAPSKplVVLLHGLEgssdshyARGLARA----LYARGWDVVRLNFRGCGGEPNllprlyhsGDTEDLVWVLA 125

                         90       100
                 ....*....|....*....|
gi 515630477  67 QLLAEAPKQAIW-VGWSLGG 85
Cdd:COG0429  126 HLRARYPYAPLYaVGFSLGG 145
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 10-92 3.72e-04

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: 41.61  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  10 SGQGPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAHCHAqDLEEIA----QQLLAEAPKQAIW-VGWSLG 84
Cdd:COG3319  598 GGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPA-SVEEMAaryvEAIRAVQPEGPYHlLGWSFG 676


                 ....*...
gi 515630477  85 GLVATHMA 92
Cdd:COG3319  677 GLVAYEMA 684
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
37-125 1.55e-03

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.10  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  37 QADFRVHVVDLPGYGHSA-----HCHA-------QDLEEIAQQLLAEAPKQAI-WVGWSLGGLVAthMALHHSDYVSKLV 103
Cdd:COG4757   57 ERGFAVLTYDYRGIGLSRpgslrGFDAgyrdwgeLDLPAVLDALRARFPGLPLlLVGHSLGGQLL--GLAPNAERVDRLV 134

                         90       100
                 ....*....|....*....|....*....
gi 515630477 104 TVASS-------PKFAAAKEPVLWRGIQP 125
Cdd:COG4757  135 TVASGsgywrdyPPRRRLKVLLFWHLLGP 163
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 14-93 1.58e-03

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 38.91  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   14 PDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGY--GHSAHCHAQDL-EEIAQQLLAEAPKQAIWV-GWSLGGLVAT 89
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRgrGEPPLNSIEALaDEYAEALRQIQPEGPYALfGHSMGGMLAF 80


                  ....
gi 515630477   90 HMAL 93
Cdd:pfam00975  81 EVAR 84
PRK05855 PRK05855
SDR family oxidoreductase;
13-55 3.38e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 38.42  E-value: 3.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515630477  13 GPDLVLVHGWGMNGAVWQQTVNALQADFRVHVVDLPGYGHSAH 55
Cdd:PRK05855  25 RPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSA 67
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 3-119 3.81e-03

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 38.25  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477   3 DALYWHVsgQGP-------DLVLVHGWGMNGAVWQQTV-----NALQADFRVHVVDLPGYGHSA------HCHAQDLEEI 64
Cdd:PLN03087 186 ESLFVHV--QQPkdnkakeDVLFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPkpadslYTLREHLEMI 263

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630477  65 AQQLLAE-APKQAIWVGWSLGGLVATHMALHHSDYVSKLVTVA----SSPKFAAAKEPVL 119
Cdd:PLN03087 264 ERSVLERyKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAppyyPVPKGVQATQYVM 323
 
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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