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Conserved domains on  [gi|1006541049|ref|WP_061792356|]
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alpha/beta fold hydrolase [Cytobacillus firmus]

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, ...
 2-255 1.33e-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: 142.06  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   2 LYYRTYvkDESLPWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGTweEGDHFSEVSQDIVEVLDHLQIT 81
Cdd:COG0596    14 LHYREA--GPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  82 DSHFIGISLGTIVIQTIAQNHPERVASMILGGAitelnwrtrfliaianltkymlpymllykLFAWIIMPKRNHLESRHA 161
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------------------------VLAALAEPLRRPGLAPEA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 162 FVRQAAKMCQKEFINWLsltksvnpylGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITGAGHVCNID 240
Cdd:COG0596   141 LAALLRALARTDLRERL----------ARIT-----VPTLVIWGEKDPIVpPALARRLAELLPNAELVVLPGAGHFPPLE 205

                         250
                  ....*....|....*
gi 1006541049 241 KPDAFNRITIDFINR 255
Cdd:COG0596   206 QPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-255 1.33e-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: 142.06  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   2 LYYRTYvkDESLPWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGTweEGDHFSEVSQDIVEVLDHLQIT 81
Cdd:COG0596    14 LHYREA--GPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  82 DSHFIGISLGTIVIQTIAQNHPERVASMILGGAitelnwrtrfliaianltkymlpymllykLFAWIIMPKRNHLESRHA 161
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------------------------VLAALAEPLRRPGLAPEA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 162 FVRQAAKMCQKEFINWLsltksvnpylGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITGAGHVCNID 240
Cdd:COG0596   141 LAALLRALARTDLRERL----------ARIT-----VPTLVIWGEKDPIVpPALARRLAELLPNAELVVLPGAGHFPPLE 205

                         250
                  ....*....|....*
gi 1006541049 241 KPDAFNRITIDFINR 255
Cdd:COG0596   206 QPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 14-242 1.49e-26

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: 103.35  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  14 PWVTFVHGAGGSSAIWYKQMRE-YKKHFNVLLVDLRGHGQSGRGTWEEGDHFSEVSQDIVEVLDHLQITDSHFIGISLGT 92
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  93 IVIQTIAQNHPERVASMILGGAITE---------------LNWRTRFLIAIANLTKYMLPYMLLYKLFAWI-IMPKRNHL 156
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPpheldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLLLRLrLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 157 ESRHAFVRQA-AKMCQKEFINWLSL--TKSVNPYLGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITG 232
Cdd:pfam00561 161 NKRFPSGDYAlAKSLVTGALLFIETwsTELRAKFLGRLD-----EPTLIIWGDQDPLVpPQALEKLAQLFPNARLVVIPD 235

                         250
                  ....*....|
gi 1006541049 233 AGHVCNIDKP 242
Cdd:pfam00561 236 AGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 16-253 5.39e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 70.74  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  16 VTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRgTWEEGDhFSEVSQDIVEVLDHLQITDSHFIGISLGTIVI 95
Cdd:PRK14875  134 VVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSK-AVGAGS-LDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  96 QTIAQNHPERVASMIL---GGAITELNwrTRFL--IAIANLTKYMLPymLLYKLFA-----------WIIMPKRnhLESR 159
Cdd:PRK14875  212 LRLAARAPQRVASLTLiapAGLGPEIN--GDYIdgFVAAESRRELKP--VLELLFAdpalvtrqmveDLLKYKR--LDGV 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 160 HAFVRQAAKMCQKEFINwlslTKSVNPYLGKIQssishIPTLFIMGQEDHlfIKSVKSIAQKAKTATVKIITGAGHVCNI 239
Cdd:PRK14875  286 DDALRALADALFAGGRQ----RVDLRDRLASLA-----IPVLVIWGEQDR--IIPAAHAQGLPDGVAVHVLPGAGHMPQM 354

                         250
                  ....*....|....
gi 1006541049 240 DKPDAFNRITIDFI 253
Cdd:PRK14875  355 EAAADVNRLLAEFL 368
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 14-253 2.92e-08

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: 52.90  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  14 PWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSgrgTWEEGDHFSEVSQDIVEVLDHLQItdshFIGISLGTI 93
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS---RGFGPLSLADMAEAIAAQAPDPAI----WLGWSLGGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  94 VIQTIAQNHPERVASMILGGAITEL----NWR--------TRFLIAI-ANLTKYMLPYMLLYKLFA----WIIMPKRNHL 156
Cdd:TIGR01738  78 VALHIAATHPDRVRALVTVASSPCFsareDWPegikpdvlTGFQQQLsDDYQRTIERFLALQTLGTptarQDARALKQTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 157 ESRHAFVRQAakmcqkeFINWLSLTKSVNpylgkIQSSISHI--PTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITGA 233
Cdd:TIGR01738 158 LARPTPNVQV-------LQAGLEILATVD-----LRQPLQNIsvPFLRLYGYLDGLVpAKVVPMLDKLAPHSELYIFAKA 225

                         250       260
                  ....*....|....*....|
gi 1006541049 234 GHVCNIDKPDAFNRITIDFI 253
Cdd:TIGR01738 226 AHAPFLSHAEAFCALLVAFK 245
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-255 1.33e-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: 142.06  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   2 LYYRTYvkDESLPWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGTweEGDHFSEVSQDIVEVLDHLQIT 81
Cdd:COG0596    14 LHYREA--GPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLDALGLE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  82 DSHFIGISLGTIVIQTIAQNHPERVASMILGGAitelnwrtrfliaianltkymlpymllykLFAWIIMPKRNHLESRHA 161
Cdd:COG0596    90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDE-----------------------------VLAALAEPLRRPGLAPEA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 162 FVRQAAKMCQKEFINWLsltksvnpylGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITGAGHVCNID 240
Cdd:COG0596   141 LAALLRALARTDLRERL----------ARIT-----VPTLVIWGEKDPIVpPALARRLAELLPNAELVVLPGAGHFPPLE 205

                         250
                  ....*....|....*
gi 1006541049 241 KPDAFNRITIDFINR 255
Cdd:COG0596   206 QPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 14-242 1.49e-26

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: 103.35  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  14 PWVTFVHGAGGSSAIWYKQMRE-YKKHFNVLLVDLRGHGQSGRGTWEEGDHFSEVSQDIVEVLDHLQITDSHFIGISLGT 92
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  93 IVIQTIAQNHPERVASMILGGAITE---------------LNWRTRFLIAIANLTKYMLPYMLLYKLFAWI-IMPKRNHL 156
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPpheldeadrfilalfPGFFDGFVADFAPNPLGRLVAKLLALLLLRLrLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 157 ESRHAFVRQA-AKMCQKEFINWLSL--TKSVNPYLGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITG 232
Cdd:pfam00561 161 NKRFPSGDYAlAKSLVTGALLFIETwsTELRAKFLGRLD-----EPTLIIWGDQDPLVpPQALEKLAQLFPNARLVVIPD 235

                         250
                  ....*....|
gi 1006541049 233 AGHVCNIDKP 242
Cdd:pfam00561 236 AGHFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2-255 5.57e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 77.35  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   2 LYYRTYV-KDESLPWVTFVHGAGGSSAIWYKQMREY-KKHFNVLLVDLRGHGQSGR--GTWeegDHFSEVSQDIVEVLDH 77
Cdd:COG2267    16 LRGRRWRpAGSPRGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGprGHV---DSFDDYVDDLRAALDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  78 LQITDS---HFIGISLGTIVIQTIAQNHPERVASMILGGaitelnwrtrfliaianltkymlPYMLLYKLFAWiimpkrn 154
Cdd:COG2267    93 LRARPGlpvVLLGHSMGGLIALLYAARYPDRVAGLVLLA-----------------------PAYRADPLLGP------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 155 hlesRHAFVRQAAkmcqkefinwlsltksVNPYLGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQK-AKTATVKIITG 232
Cdd:COG2267   143 ----SARWLRALR----------------LAEALARID-----VPVLVLHGGADRVVpPEAARRLAARlSPDVELVLLPG 197

                         250       260
                  ....*....|....*....|....*
gi 1006541049 233 AGHVCNID--KPDAFNRItIDFINR 255
Cdd:COG2267   198 ARHELLNEpaREEVLAAI-LAWLER 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 16-253 5.39e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 70.74  E-value: 5.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  16 VTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRgTWEEGDhFSEVSQDIVEVLDHLQITDSHFIGISLGTIVI 95
Cdd:PRK14875  134 VVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSK-AVGAGS-LDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  96 QTIAQNHPERVASMIL---GGAITELNwrTRFL--IAIANLTKYMLPymLLYKLFA-----------WIIMPKRnhLESR 159
Cdd:PRK14875  212 LRLAARAPQRVASLTLiapAGLGPEIN--GDYIdgFVAAESRRELKP--VLELLFAdpalvtrqmveDLLKYKR--LDGV 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 160 HAFVRQAAKMCQKEFINwlslTKSVNPYLGKIQssishIPTLFIMGQEDHlfIKSVKSIAQKAKTATVKIITGAGHVCNI 239
Cdd:PRK14875  286 DDALRALADALFAGGRQ----RVDLRDRLASLA-----IPVLVIWGEQDR--IIPAAHAQGLPDGVAVHVLPGAGHMPQM 354

                         250
                  ....*....|....
gi 1006541049 240 DKPDAFNRITIDFI 253
Cdd:PRK14875  355 EAAADVNRLLAEFL 368
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 18-248 1.94e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 67.50  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  18 FVHGAGGSSAIWykqMREYKKHFNVLLVDLRGHGQSGRGTweegDHFSEVsQDIVEVLDHL-QITDSHFIGISLGTIVIQ 96
Cdd:pfam12697   3 LVHGAGLSAAPL---AALLAAGVAVLAPDLPGHGSSSPPP----LDLADL-ADLAALLDELgAARPVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  97 TIAqnHPERVASMILGGAITELNWRTRFLIAIANLTKYMLPYMLLYKLFAwiimpkrnhlesRHAFVRQAAkMCQKEFIN 176
Cdd:pfam12697  75 AAA--AAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESL------------ARGFLDDLP-ADAEWAAA 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006541049 177 WLSLTKSVNPYLGKIQSSISHIP-TLFIMGQEDHLFIKSVKSIAQKAKTATVKIITGAGHvCNIDKPDAFNRI 248
Cdd:pfam12697 140 LARLAALLAALALLPLAAWRDLPvPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPEEVAEA 211
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
9-255 2.14e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 64.65  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   9 KDESLPWVTFVHGAGGS-SAIWYKQMREYKKH-FNVLLVDLRGHGQSgRGTWEEGDHfsevsQDIVEVLDHLQ---ITDS 83
Cdd:COG1506    19 DGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGES-AGDWGGDEV-----DDVLAAIDYLAarpYVDP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  84 HFIGI---SLGTIVIQTIAQNHPERVASMILGGAITelNWRTrfliaianltkymlpymlLYKLFAWIIMPKRNHLESRH 160
Cdd:COG1506    93 DRIGIyghSYGGYMALLAAARHPDRFKAAVALAGVS--DLRS------------------YYGTTREYTERLMGGPWEDP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 161 AFVRQAakmcqkefinwlsltkSVNPYLGKIQssishIPTLFIMGQEDHLF-IKSVKSIAQKA----KTATVKIITGAGH 235
Cdd:COG1506   153 EAYAAR----------------SPLAYADKLK-----TPLLLIHGEADDRVpPEQAERLYEALkkagKPVELLVYPGEGH 211

                         250       260
                  ....*....|....*....|
gi 1006541049 236 VCNIDKPDAFNRITIDFINR 255
Cdd:COG1506   212 GFSGAGAPDYLERILDFLDR 231
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
18-255 5.48e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 63.81  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  18 FVHGAGGSSAiwykQMRE-----YKKHFNVLLVDLRGHGqsgrGTWEEgdhFSEVS-----QDIVEVLDHL-QITDS-HF 85
Cdd:COG1647    20 LLHGFTGSPA----EMRPlaealAKAGYTVYAPRLPGHG----TSPED---LLKTTwedwlEDVEEAYEILkAGYDKvIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  86 IGISLGTIVIQTIAQNHPErVASMIL-GGAITELNWRTRFLIAIANLTKYmlpymllyklfawiIMPKRNHLESRHAFVR 164
Cdd:COG1647    89 IGLSMGGLLALLLAARYPD-VAGLVLlSPALKIDDPSAPLLPLLKYLARS--------------LRGIGSDIEDPEVAEY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 165 QAAKMCQKEFINWLSLTKSVNPYLGKIqssisHIPTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIIT--GAGHV--CNI 239
Cdd:COG1647   154 AYDRTPLRALAELQRLIREVRRDLPKI-----TAPTLIIQSRKDEVVpPESARYIYERLGSPDKELVWleDSGHVitLDK 228

                         250
                  ....*....|....*.
gi 1006541049 240 DKPDAFNRItIDFINR 255
Cdd:COG1647   229 DREEVAEEI-LDFLER 243
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 16-235 1.67e-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: 62.23  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  16 VTFVHGAGGSSAiWYKQMREY--KKHFNVLLVDLRGHGQSG--RGTWeegDHFSEVSQDIVEVLDHLQ---ITDSHFI-G 87
Cdd:pfam12146   7 VVLVHGLGEHSG-RYAHLADAlaAQGFAVYAYDHRGHGRSDgkRGHV---PSFDDYVDDLDTFVDKIReehPGLPLFLlG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  88 ISLGTIVIQTIAQNHPERVASMILGGAIteLNWRTRFLIAIANLTKYMLPyMLLYKLfaWIIMPKRNHLESRH-AFVRQA 166
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPA--LKIKPYLAPPILKLLAKLLG-KLFPRL--RVPNNLLPDSLSRDpEVVAAY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 167 AK---MCQKEFINW----LSLTKSVNPYLGKIQssishIPTLFIMGQEDHL--------FIKSVKSiaqkaKTATVKIIT 231
Cdd:pfam12146 158 AAdplVHGGISARTlyelLDAGERLLRRAAAIT-----VPLLLLHGGADRVvdpagsreFYERAGS-----TDKTLKLYP 227


                  ....
gi 1006541049 232 GAGH 235
Cdd:pfam12146 228 GLYH 231
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 10-255 9.24e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 57.62  E-value: 9.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  10 DESLPWVTFVHGAGGS---SAIWYKQMREYKkhFNVLLVDLRGHGQSGrGTW-EEGDHFsevSQDIVEVLDHLQITDSH- 84
Cdd:COG1073    34 SKKYPAVVVAHGNGGVkeqRALYAQRLAELG--FNVLAFDYRGYGESE-GEPrEEGSPE---RRDARAAVDYLRTLPGVd 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  85 -----FIGISLGTIVIQTIAQNHPeRVASMILGGAITELNWRTRFLIAIANLTKY-MLPYMLLYKLFAWIimpkRNHLES 158
Cdd:COG1073   108 perigLLGISLGGGYALNAAATDP-RVKAVILDSPFTSLEDLAAQRAKEARGAYLpGVPYLPNVRLASLL----NDEFDP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 159 RHafvrqaakmcqkefinwlsltksvnpYLGKIqssisHIPTLFIMGQEDHL--FIKSVKSIAQKAKTATVKIITGAGHV 236
Cdd:COG1073   183 LA--------------------------KIEKI-----SRPLLFIHGEKDEAvpFYMSEDLYEAAAEPKELLIVPGAGHV 231

                         250       260
                  ....*....|....*....|.
gi 1006541049 237 CNIDKPD--AFNRITiDFINR 255
Cdd:COG1073   232 DLYDRPEeeYFDKLA-EFFKK 251
PRK10673 PRK10673
esterase;
12-111 2.04e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 56.66  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  12 SLPwVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGtwEEGDhFSEVSQDIVEVLDHLQITDSHFIGISLG 91
Cdd:PRK10673   16 NSP-IVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRD--PVMN-YPAMAQDLLDTLDALQIEKATFIGHSMG 91

                          90       100
                  ....*....|....*....|
gi 1006541049  92 TIVIQTIAQNHPERVASMIL 111
Cdd:PRK10673   92 GKAVMALTALAPDRIDKLVA 111
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 14-255 8.18e-09

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 54.46  E-value: 8.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  14 PWVTFVHGAGGSSAIWyKQMREYKKHFNVLLVDLRGHGQSgRGTweEGDHFSEVSQDIVEVLDHLQITDSHFIGISLG-T 92
Cdd:PRK11126    3 PWLVFLHGLLGSGQDW-QPVGEALPDYPRLYIDLPGHGGS-AAI--SVDGFADVSRLLSQTLQSYNILPYWLVGYSLGgR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  93 IVIQTIAQNHPERVASMILGGA--------------ITELNWRTRFLI-AIANLtkymlpymllykLFAWIIMPKRNHL- 156
Cdd:PRK11126   79 IAMYYACQGLAGGLCGLIVEGGnpglqnaeerqarwQNDRQWAQRFRQePLEQV------------LADWYQQPVFASLn 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 157 -ESRHAFV--RQA------AKMCQKefinwLSLTKsvNPYLG-KIQSsiSHIPTLFIMGQEDHLFiksvKSIAQKAKtAT 226
Cdd:PRK11126  147 aEQRQQLVakRSNnngaavAAMLEA-----TSLAK--QPDLRpALQA--LTFPFYYLCGERDSKF----QALAQQLA-LP 212

                         250       260
                  ....*....|....*....|....*....
gi 1006541049 227 VKIITGAGHVCNIDKPDAFNRITIDFINR 255
Cdd:PRK11126  213 LHVIPNAGHNAHRENPAAFAASLAQILRL 241
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 14-253 2.92e-08

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: 52.90  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  14 PWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSgrgTWEEGDHFSEVSQDIVEVLDHLQItdshFIGISLGTI 93
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS---RGFGPLSLADMAEAIAAQAPDPAI----WLGWSLGGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  94 VIQTIAQNHPERVASMILGGAITEL----NWR--------TRFLIAI-ANLTKYMLPYMLLYKLFA----WIIMPKRNHL 156
Cdd:TIGR01738  78 VALHIAATHPDRVRALVTVASSPCFsareDWPegikpdvlTGFQQQLsDDYQRTIERFLALQTLGTptarQDARALKQTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 157 ESRHAFVRQAakmcqkeFINWLSLTKSVNpylgkIQSSISHI--PTLFIMGQEDHLF-IKSVKSIAQKAKTATVKIITGA 233
Cdd:TIGR01738 158 LARPTPNVQV-------LQAGLEILATVD-----LRQPLQNIsvPFLRLYGYLDGLVpAKVVPMLDKLAPHSELYIFAKA 225

                         250       260
                  ....*....|....*....|
gi 1006541049 234 GHVCNIDKPDAFNRITIDFI 253
Cdd:TIGR01738 226 AHAPFLSHAEAFCALLVAFK 245
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
16-110 9.34e-07

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 48.86  E-value: 9.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  16 VTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQS-GRGTWEEGDHFSEVSQDIVEvldhlqitDSHFIGISLGTIV 94
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSrGFGALSLADMAEAVLQQAPD--------KAIWLGWSLGGLV 87

                          90
                  ....*....|....*.
gi 1006541049  95 IQTIAQNHPERVASMI 110
Cdd:PRK10349   88 ASQIALTHPERVQALV 103
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 33-244 1.36e-06

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: 48.50  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  33 MREYKKHFNVLLVDLRGHgQSGRGTWEEGDHFSEVSQ---DIVEVLDHLQITDSHFIGISLGTIVIQTIAQNHPERVASM 109
Cdd:pfam03096  49 MQEILENFCIYHVDAPGQ-EDGAASFPGGYPYPSMDDladMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 110 ILGGAI-TELNWRTRFLIAIANLTKY------MLPYMLLYKLFAwiimpkRNHLESRHAFVRQaakmCQKEF---INWLS 179
Cdd:pfam03096 128 VLINPTpKAAGWIEWFYNKLSSKLLYyygmtdSAKDYLLAHYFG------KEELSNNSDIVQE----YRKFLkerLNPKN 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006541049 180 LTKSVNPYLG------KIQSSISHIPTLFIMG-QEDHL-FIKSVKSIAQKAKTATVKIITGAGHVcNIDKPDA 244
Cdd:pfam03096 198 LQLYLEAYNSrrdltiERPGLETKCPVLLVVGdNSPHVdAVVECNTKLDPTKTTLLKVADCGGLV-QQEQPGK 269
PRK05855 PRK05855
SDR family oxidoreductase;
14-76 2.88e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 44.97  E-value: 2.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006541049  14 PWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGTWEEGDHFSEVSQDIVEVLD 76
Cdd:PRK05855   26 PTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVID 88
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 18-113 3.18e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 42.12  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  18 FVHGAGGSSAIWYKqMREY--KKHFNVLLVDLrghgQSGRGTWEegDHFSEVSQDIVEVLDHLQITDSHFIGISLGTIVI 95
Cdd:COG1075    10 LVHGLGGSAASWAP-LAPRlrAAGYPVYALNY----PSTNGSIE--DSAEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82

                          90       100
                  ....*....|....*....|.
gi 1006541049  96 QTIAQNH--PERVASMI-LGG 113
Cdd:COG1075    83 RYYLKRLggAAKVARVVtLGT 103
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 6-246 4.20e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 44.13  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   6 TYVKDESLPWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGR-----GTWEEGDHFSEVSqdIVEVLDHLQI 80
Cdd:PLN02894   98 TFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRpdftcKSTEETEAWFIDS--FEEWRKAKNL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049  81 TDSHFIGISLGTIVIQTIAQNHPERVASMILGGAI-------TELNWRTRFLI----AIANL--TKYMLPYMLLYKLFAW 147
Cdd:PLN02894  176 SNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAgfssesdDKSEWLTKFRAtwkgAVLNHlwESNFTPQKIIRGLGPW 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049 148 -------IIMPKRNHLESRHAFVRQAAKMCQKEFINWLSLTKSVNPYLGKIQS-----------SISH--IPTLFIMGQE 207
Cdd:PLN02894  256 gpnlvrrYTTARFGAHSTGDILSEEESKLLTDYVYHTLAAKASGELCLKYIFSfgafarkplleSASEwkVPTTFIYGRH 335

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1006541049 208 DHLFIKSVKSIAQKAKT-ATVKIITGAGHVCNIDKPDAFN 246
Cdd:PLN02894  336 DWMNYEGAVEARKRMKVpCEIIRVPQGGHFVFLDNPSGFH 375
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 7-114 3.58e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 37.91  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541049   7 YVKDESLPWVTFVHGAGGSSAIWYKQMREYKKHFNVLLVDLRGHGQSGRGTwEEGDHFSEVSQDIVEVLDHLQITDSHFI 86
Cdd:PRK03204   28 YIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPS-GFGYQIDEHARVIGEFVDHLGLDRYLSM 106

                          90       100
                  ....*....|....*....|....*...
gi 1006541049  87 GISLGTIVIQTIAQNHPERVASMILGGA 114
Cdd:PRK03204  107 GQDWGGPISMAVAVERADRVRGVVLGNT 134
 
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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