NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22122331|ref|NP_666033|]
View 

S-acyl fatty acid synthase thioesterase, medium chain [Mus musculus]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 22-242 5.57e-66

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


:

Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 205.09  E-value: 5.57e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331  22 KPDALFKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGRETRFEEPFSNDIYQIAEEVVTALLPIIrDKAFAFFGHS 101
Cdd:COG3208   2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL-DRPFALFGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331 102 FGSYIAFITALHLKEKYKMEPLHIFVSSASAPHseFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLK 181
Cdd:COG3208  81 MGALLAFELARRLERRGRPLPAHLFVSGRRAPH--LPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22122331 182 ADVDIVKKFIFDKPskALLSRDITCFIGSEDV---VKDIEGWKDITSGKFDVLKLPGDHFYLME 242
Cdd:COG3208 159 ADFRLLETYRYTPG--PPLDCPITALGGDDDPlvsPEELAAWREHTTGPFRLRVFPGGHFFLRD 220
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 22-242 5.57e-66

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 205.09  E-value: 5.57e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331  22 KPDALFKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGRETRFEEPFSNDIYQIAEEVVTALLPIIrDKAFAFFGHS 101
Cdd:COG3208   2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL-DRPFALFGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331 102 FGSYIAFITALHLKEKYKMEPLHIFVSSASAPHseFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLK 181
Cdd:COG3208  81 MGALLAFELARRLERRGRPLPAHLFVSGRRAPH--LPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22122331 182 ADVDIVKKFIFDKPskALLSRDITCFIGSEDV---VKDIEGWKDITSGKFDVLKLPGDHFYLME 242
Cdd:COG3208 159 ADFRLLETYRYTPG--PPLDCPITALGGDDDPlvsPEELAAWREHTTGPFRLRVFPGGHFFLRD 220
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 27-242 1.28e-58

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: 186.05  E-value: 1.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331    27 FKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGREtrFEEPFSNDIYQIAEEVVTALLPIIRDKAFAFFGHSFGSYI 106
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRG--RGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331   107 AFITALHLKEKyKMEPLHIFVSSASAPHSEfRPQVPDinKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLKADVDI 186
Cdd:pfam00975  79 AFEVARRLERQ-GEAVRSLFLSDASAPHTV-RYEASR--APDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331   187 VKKFIfdKPSKALLSrdITCFIGSEDVVKDI----EGWKDITSGKFDVLKLPGDHFYLME 242
Cdd:pfam00975 155 LESYS--CPPLDAQS--ATLFYGSDDPLHDAddlaEWVRDHTPGEFDVHVFDGDHFYLIE 210
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 54-178 6.09e-03

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 36.99  E-value: 6.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331  54 EVHAVRLAGRETRFEEPFSNDIY---------QIAEEVVTALLPIiRDKAFAFFGHSFGS-YIAFITALHLKEKYKMEPL 123
Cdd:cd09815  28 EDKDSKLLSLVLRAILKDGKRIYdlhdpnveeEMAELLLEEARQG-KDVAFLSPGDPGVAgTGAELVERAEREGVEVKVI 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22122331 124 HiFVSSASA----------------PHSEFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIP 178
Cdd:cd09815 107 P-GVSAADAaaaalgidlgesflfvTASDLLENPRLLVLKALAKERRHLVLFLDGHRFLKALERLLKELGE 176
 
Name Accession Description Interval E-value
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 22-242 5.57e-66

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


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 205.09  E-value: 5.57e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331  22 KPDALFKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGRETRFEEPFSNDIYQIAEEVVTALLPIIrDKAFAFFGHS 101
Cdd:COG3208   2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLL-DRPFALFGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331 102 FGSYIAFITALHLKEKYKMEPLHIFVSSASAPHseFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLK 181
Cdd:COG3208  81 MGALLAFELARRLERRGRPLPAHLFVSGRRAPH--LPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22122331 182 ADVDIVKKFIFDKPskALLSRDITCFIGSEDV---VKDIEGWKDITSGKFDVLKLPGDHFYLME 242
Cdd:COG3208 159 ADFRLLETYRYTPG--PPLDCPITALGGDDDPlvsPEELAAWREHTTGPFRLRVFPGGHFFLRD 220
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 27-242 1.28e-58

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: 186.05  E-value: 1.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331    27 FKLICFPWAGGGSTHFAKWGRKINGLLEVHAVRLAGREtrFEEPFSNDIYQIAEEVVTALLPIIRDKAFAFFGHSFGSYI 106
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRG--RGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331   107 AFITALHLKEKyKMEPLHIFVSSASAPHSEfRPQVPDinKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIPLLKADVDI 186
Cdd:pfam00975  79 AFEVARRLERQ-GEAVRSLFLSDASAPHTV-RYEASR--APDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331   187 VKKFIfdKPSKALLSrdITCFIGSEDVVKDI----EGWKDITSGKFDVLKLPGDHFYLME 242
Cdd:pfam00975 155 LESYS--CPPLDAQS--ATLFYGSDDPLHDAddlaEWVRDHTPGEFDVHVFDGDHFYLIE 210
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 37-171 9.92e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 45.54  E-value: 9.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331    37 GGSTHFAKWGRKINGLLEVHAVRLAGRETRFEEPFSndiYQIAEEVVTALLPIIRDKAFAFFGHSFGSYIAFITALHLKe 116
Cdd:pfam12697   6 GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLD---LADLADLAALLDELGAARPVVLVGHSLGGAVALAAAAAAL- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22122331   117 kykmePLHIFVSSASAPHSEFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQD 171
Cdd:pfam12697  82 -----VVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLP 131
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 54-178 6.09e-03

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 36.99  E-value: 6.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122331  54 EVHAVRLAGRETRFEEPFSNDIY---------QIAEEVVTALLPIiRDKAFAFFGHSFGS-YIAFITALHLKEKYKMEPL 123
Cdd:cd09815  28 EDKDSKLLSLVLRAILKDGKRIYdlhdpnveeEMAELLLEEARQG-KDVAFLSPGDPGVAgTGAELVERAEREGVEVKVI 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22122331 124 HiFVSSASA----------------PHSEFRPQVPDINKLSEEQIRDHLLIFGGTPKHLIEDQDFLKQCIP 178
Cdd:cd09815 107 P-GVSAADAaaaalgidlgesflfvTASDLLENPRLLVLKALAKERRHLVLFLDGHRFLKALERLLKELGE 176
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH