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Conserved domains on  [gi|447151593|ref|WP_001228849|]
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MULTISPECIES: thioesterase II family protein [Bacillus]

Protein Classification

thioesterase II family protein( domain architecture ID 10007057)

thioesterase II family protein such as gramicidin S biosynthesis protein GrsT, S-acyl fatty acid synthase thioesterase, and the surfactin synthase thioesterase subunit, which is involved in the surfactin biosynthesis pathway

CATH:  3.40.50.1820
EC:  3.1.2.-
Gene Ontology:  GO:0009058
PubMed:  3732600

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 18-239 1.74e-65

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 203.16  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLS-PLVDNIDDLVNLYLMEMQPILEGEVTLFGHSMGGIIVHR 96
Cdd:COG3208    9 LFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGePPLTSLEELADDLAEELAPLLDRPFALFGHSMGALLAFE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  97 MAQILESKGI-NPKNVIISAMNPPEI---RRKTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSDFRAIENYI 172
Cdd:COG3208   89 LARRLERRGRpLPAHLFVSGRRAPHLprrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRLLETYR 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447151593 173 NDDTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGN-EVHFLTVNGGHMFLLHQADIVGELIMKILDRV 239
Cdd:COG3208  169 YTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTgPFRLRVFPGGHFFLRDHPAELLALIRAALAAL 236
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 18-239 1.74e-65

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 203.16  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLS-PLVDNIDDLVNLYLMEMQPILEGEVTLFGHSMGGIIVHR 96
Cdd:COG3208    9 LFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGePPLTSLEELADDLAEELAPLLDRPFALFGHSMGALLAFE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  97 MAQILESKGI-NPKNVIISAMNPPEI---RRKTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSDFRAIENYI 172
Cdd:COG3208   89 LARRLERRGRpLPAHLFVSGRRAPHLprrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRLLETYR 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447151593 173 NDDTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGN-EVHFLTVNGGHMFLLHQADIVGELIMKILDRV 239
Cdd:COG3208  169 YTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTgPFRLRVFPGGHFFLRDHPAELLALIRAALAAL 236
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 18-236 2.21e-39

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: 135.59  E-value: 2.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLSPLvDNIDDLVNLYLMEMQPIL-EGEVTLFGHSMGGIIVHR 96
Cdd:pfam00975   3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPL-NSIEALADEYAEALRQIQpEGPYALFGHSMGGMLAFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   97 MAQILESKGINPKNVIISAMNPPEIRR--KTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSDFRAIENYIND 174
Cdd:pfam00975  82 VARRLERQGEAVRSLFLSDASAPHTVRyeASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALESYSCP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447151593  175 DTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGNEVHFLTVNGGHMFLLHQADIVGELIMKIL 236
Cdd:pfam00975 162 PLDAQSATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDHFYLIEHLEAVLEIIEAKL 223
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
18-105 1.44e-06

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 48.89  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLsPLVDNIDDLVNLYL---MEMQPilEGEVTLFGHSMGGIIV 94
Cdd:PRK10252 1071 LFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPM-QTATSLDEVCEAHLatlLEQQP--HGPYHLLGYSLGGTLA 1147

                          90
                  ....*....|.
gi 447151593   95 HRMAQILESKG 105
Cdd:PRK10252 1148 QGIAARLRARG 1158
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 82-112 2.13e-03

Thioesterase; 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: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 37.97  E-value: 2.13e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 447151593    82 VTLFGHSMGGIIVHRMAQILESKGINPKNVI 112
Cdd:smart00824  66 FVLVGHSSGGLLAHAVAARLEARGIPPAAVV 96
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 18-239 1.74e-65

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 203.16  E-value: 1.74e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLS-PLVDNIDDLVNLYLMEMQPILEGEVTLFGHSMGGIIVHR 96
Cdd:COG3208    9 LFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGePPLTSLEELADDLAEELAPLLDRPFALFGHSMGALLAFE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  97 MAQILESKGI-NPKNVIISAMNPPEI---RRKTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSDFRAIENYI 172
Cdd:COG3208   89 LARRLERRGRpLPAHLFVSGRRAPHLprrRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADFRLLETYR 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447151593 173 NDDTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGN-EVHFLTVNGGHMFLLHQADIVGELIMKILDRV 239
Cdd:COG3208  169 YTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTgPFRLRVFPGGHFFLRDHPAELLALIRAALAAL 236
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 18-236 2.21e-39

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: 135.59  E-value: 2.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLSPLvDNIDDLVNLYLMEMQPIL-EGEVTLFGHSMGGIIVHR 96
Cdd:pfam00975   3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPL-NSIEALADEYAEALRQIQpEGPYALFGHSMGGMLAFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   97 MAQILESKGINPKNVIISAMNPPEIRR--KTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSDFRAIENYIND 174
Cdd:pfam00975  82 VARRLERQGEAVRSLFLSDASAPHTVRyeASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALESYSCP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447151593  175 DTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGNEVHFLTVNGGHMFLLHQADIVGELIMKIL 236
Cdd:pfam00975 162 PLDAQSATLFYGSDDPLHDADDLAEWVRDHTPGEFDVHVFDGDHFYLIEHLEAVLEIIEAKL 223
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 18-241 1.95e-18

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: 83.98  E-value: 1.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLSPLvDNIDDLVNLYLMEM---QPilEGEVTLFGHSMGGIIV 94
Cdd:COG3319  604 LFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPP-ASVEEMAARYVEAIravQP--EGPYHLLGWSFGGLVA 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  95 HRMAQILESKGINPKNV-IISAMNPPEIRRKTNH-------------------------LDDKDFIDYIKSLG---GLPD 145
Cdd:COG3319  681 YEMARQLEAQGEEVALLvLLDSYAPGALARLDEAellaallrdlargvdlpldaeelraLDPEERLARLLERLreaGLPA 760

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593 146 EVlqHQELLNYILPVIRSDFRAIENY----INDDTTLLKAPLYIISGTTDsnyTVKGAKKWVEWGNEVHflTVNGGHMFL 221
Cdd:COG3319  761 GL--DAERLRRLLRVFRANLRALRRYrprpYDGPVLLFRAEEDPPGRADD---PALGWRPLVAGGLEVH--DVPGDHFSM 833

                        250       260
                 ....*....|....*....|..
gi 447151593 222 L--HQADIVGELIMKILDRVKS 241
Cdd:COG3319  834 LrePHVAELAAALRAALAAAEA 855
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-239 7.07e-13

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: 65.41  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGpnLSPLVD---NIDDLVN--LYLMEMQPIleGEVTLFGHSMGGI 92
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHG--RSDKPAggyTLDDLADdlAALLDALGL--ERVVLVGHSMGGM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  93 IVHRMAqileskginpknviisAMNPPEIRRktnhlddkdFIdyikSLGGLPDEVLQHQELLNYILPVIRSDFRAIENY- 171
Cdd:COG0596  102 VALELA----------------ARHPERVAG---------LV----LVDEVLAALAEPLRRPGLAPEALAALLRALARTd 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447151593 172 INDDTTLLKAPLYIISGTTDSNYTVKGAKKWVEWGNEVHFLTV-NGGHMFLLHQADIVGELIMKILDRV 239
Cdd:COG0596  153 LRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLpGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 18-228 3.83e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 60.57  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPyagGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLSPLVD--NIDDLVNLYLmemQPILEGEVTLFGHSMGGIIVH 95
Cdd:pfam12697   1 VVLVH---GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDlaDLADLAALLD---ELGAARPVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   96 RMAQILESKGI----NPKNVIISAMNPPEIRRKTNHLDDKDFIDYIKSLGGLPDEVLQHQELLNYILPVIRSdFRAIENY 171
Cdd:pfam12697  75 AAAAAALVVGVlvapLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAAL-LAALALL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 447151593  172 INDDTTLLKAPLYIIsGTTDSNYTVKGAKKWVEWGNEVHFLTVNGGHMFLLHQADIV 228
Cdd:pfam12697 154 PLAAWRDLPVPVLVL-AEEDRLVPELAQRLLAALAGARLVVLPGAGHLPLDDPEEVA 209
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-222 2.86e-08

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: 52.89  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPYAGGYSNSFLPLKNYLPKDI-KLISFDPPGHGPNLSPLVDN---IDDLVNLYLMEMQPILEGEVTLFGHSMGGII 93
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRPKAQDdyrTDDLAEDLEYILEALGLEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   94 VHRMAQILESK--------GINPKNVIISA-----MNPPE----IRRKTNHLDDKDFID--------YIKSLGGLPDEVL 148
Cdd:pfam00561  83 ALAYAAKYPDRvkalvllgALDPPHELDEAdrfilALFPGffdgFVADFAPNPLGRLVAkllallllRLRLLKALPLLNK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  149 QhqeLLNYILPVIRSDFRAIENYINDDTTLLKA--------PLYIISGTTDSNYTVKGAKKWVEW-GNEVHFLTVNGGHM 219
Cdd:pfam00561 163 R---FPSGDYALAKSLVTGALLFIETWSTELRAkflgrldePTLIIWGDQDPLVPPQALEKLAQLfPNARLVVIPDAGHF 239


                  ...
gi 447151593  220 FLL 222
Cdd:pfam00561 240 AFL 242
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
18-105 1.44e-06

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 48.89  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNLsPLVDNIDDLVNLYL---MEMQPilEGEVTLFGHSMGGIIV 94
Cdd:PRK10252 1071 LFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPM-QTATSLDEVCEAHLatlLEQQP--HGPYHLLGYSLGGTLA 1147

                          90
                  ....*....|.
gi 447151593   95 HRMAQILESKG 105
Cdd:PRK10252 1148 QGIAARLRARG 1158
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 18-99 5.41e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  18 LVCVPYAGGYSNSFLPLKNYLPKDIKLISFDPPGHGPNlSPLVD--NIDDLVN--LYLMEMQPIleGEVTLFGHSMGGII 93
Cdd:PRK14875 134 VVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGAS-SKAVGagSLDELAAavLAFLDALGI--ERAHLVGHSMGGAV 210


                 ....*.
gi 447151593  94 VHRMAQ 99
Cdd:PRK14875 211 ALRLAA 216
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 47-191 7.07e-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: 39.89  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   47 FDPPGHG---------PNLSPLVDNIDDLVNLyLMEMQPILEgeVTLFGHSMGGIIV---------HRMAQILESkginP 108
Cdd:pfam12146  37 YDHRGHGrsdgkrghvPSFDDYVDDLDTFVDK-IREEHPGLP--LFLLGHSMGGLIAalyalrypdKVDGLILSA----P 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  109 kNVIISAMNPPEIRRKTNHLDDKDFIDYIKSLGGLPDEV---LQHQELLN---YILPVIRSDF-----RAIEnYINDDTT 177
Cdd:pfam12146 110 -ALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLsrdPEVVAAYAadpLVHGGISARTlyellDAGE-RLLRRAA 187

                         170
                  ....*....|....
gi 447151593  178 LLKAPLYIISGTTD 191
Cdd:pfam12146 188 AITVPLLLLHGGAD 201
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
25-222 9.01e-04

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.21  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  25 GGYSNSFLPLKNYL-PKDIKLISFDPPGHGPNLSPLV------DNIDDLVNLY-LMEMQPilEGEVTLFGHSMGGIIVHR 96
Cdd:COG2267   38 GEHSGRYAELAEALaAAGYAVLAFDLRGHGRSDGPRGhvdsfdDYVDDLRAALdALRARP--GLPVVLLGHSMGGLIALL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  97 MAQileSKGINPKNVIISAmnppeirrkTNHLDDKDFIDYIKSLGGLpdevlqhqellnyilpvirsdfraienYINDDT 176
Cdd:COG2267  116 YAA---RYPDRVAGLVLLA---------PAYRADPLLGPSARWLRAL---------------------------RLAEAL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 447151593 177 TLLKAPLYIISGTTDSNYTVKGAKKWVE-WGNEVHFLTV-NGGHMFLL 222
Cdd:COG2267  157 ARIDVPVLVLHGGADRVVPPEAARRLAArLSPDVELVLLpGARHELLN 204
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 26-104 9.14e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 40.23  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593   26 GYSNSFLPLKNYLPKDIKLISFDPPGHG--------------PNLSplVDNIDDLvnLYLMeMQPILEGEVTLFGHSMGG 91
Cdd:PLN02980 1382 GTGEDWIPIMKAISGSARCISIDLPGHGgskiqnhaketqtePTLS--VELVADL--LYKL-IEHITPGKVTLVGYSMGA 1456

                          90
                  ....*....|...
gi 447151593   92 IIVHRMAQILESK 104
Cdd:PLN02980 1457 RIALYMALRFSDK 1469
NorV COG0426
Flavorubredoxin [Energy production and conversion];
41-123 1.35e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.43  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  41 DIKLISfdpPGHGPnlsPLVDNIDDLVNLYLMEMQPILEGEVTLFGHSMGG---IIVHRMAQILESKGINPKNVIISAMN 117
Cdd:COG0426  214 DIDMIA---PSHGP---IWRGNPKEILDWYRKWSSYQPEKKVVIVYASMYGnteKMAEAIAEGLTEEGVKVKLYDLEKTD 287


                 ....*.
gi 447151593 118 PPEIRR 123
Cdd:COG0426  288 PSEIIT 293
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
25-239 1.79e-03

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 38.77  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  25 GGYSNSFLPLKNYL-PKDIKLISFDPPGHGPNLSPLV-----DNIDDLVNLYLmEMQPILEgEVTLFGHSMGGIIVHRMA 98
Cdd:COG1647   25 TGSPAEMRPLAEALaKAGYTVYAPRLPGHGTSPEDLLkttweDWLEDVEEAYE-ILKAGYD-KVIVIGLSMGGLLALLLA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447151593  99 QILES-KGInpknVIISAmnPPEIRRKTNHLDD--KDFIDYIKSLGG-LPDEVLQHQELLNYILPVIRSdFRAIENYIND 174
Cdd:COG1647  103 ARYPDvAGL----VLLSP--ALKIDDPSAPLLPllKYLARSLRGIGSdIEDPEVAEYAYDRTPLRALAE-LQRLIREVRR 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447151593 175 DTTLLKAPLYIISGTTDSNYTVKGAKKWVE-WGNEVHFLTV--NGGHMFLL-HQADIVGELIMKILDRV 239
Cdd:COG1647  176 DLPKITAPTLIIQSRKDEVVPPESARYIYErLGSPDKELVWleDSGHVITLdKDREEVAEEILDFLERL 244
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 82-112 2.13e-03

Thioesterase; 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: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 37.97  E-value: 2.13e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 447151593    82 VTLFGHSMGGIIVHRMAQILESKGINPKNVI 112
Cdd:smart00824  66 FVLVGHSSGGLLAHAVAARLEARGIPPAAVV 96
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 25-99 4.55e-03

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.58  E-value: 4.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447151593  25 GGYSNSFLPLKNYLPKD-IKLISFDPPGHGPNLSPLVDNIDDLVNLYLMEMQpilEGEVTLFGHSMGGIIVHRMAQ 99
Cdd:COG1075   15 GGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAEQLAAFVDAVLAATG---AEKVDLVGHSMGGLVARYYLK 87
 
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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