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Conserved domains on  [gi|17507095|ref|NP_492421|]
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Fatty acid synthase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 55-167 2.36e-23

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


:

Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 92.70  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095    55 DLPKKRGKKKDLNKFDAGILPGTSKQNNPMDPQVRLLLEASWEAMVDAGINPRGLRGSQIGDFDECATPGTSGTQKQNP- 133
Cdd:pfam00109  55 KIYTKWGGLDDIFDFDPLFFGISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEd 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17507095   134 --VTEMGCIMSDTVPSMFSNRISYTFDLQGPSHSAD 167
Cdd:pfam00109 135 ggPRRGSPFAVGTMPSVIAGRISYFLGLRGPSVTVD 170
 
Name Accession Description Interval E-value
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 55-167 2.36e-23

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 92.70  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095    55 DLPKKRGKKKDLNKFDAGILPGTSKQNNPMDPQVRLLLEASWEAMVDAGINPRGLRGSQIGDFDECATPGTSGTQKQNP- 133
Cdd:pfam00109  55 KIYTKWGGLDDIFDFDPLFFGISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEd 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17507095   134 --VTEMGCIMSDTVPSMFSNRISYTFDLQGPSHSAD 167
Cdd:pfam00109 135 ggPRRGSPFAVGTMPSVIAGRISYFLGLRGPSVTVD 170
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 34-167 7.55e-23

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 94.16  E-value: 7.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095  34 MLLACDDVVTEDQLSW--APGFTDLPKKRGKK--------KDLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAMV 100
Cdd:cd00833  24 NLLEGRDAISEIPEDRwdADGYYPDPGKPGKTytrrggflDDVDAFDAaffGISPREAEA---MDPQQRLLLEVAWEALE 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507095 101 DAGINPRGLRGSQIGDFDECATPGTSGTQKQNPVTEMGCIMSDTVPSMFSNRISYTFDLQGPSHSAD 167
Cdd:cd00833 101 DAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVD 167
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 34-163 2.60e-21

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 90.32  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095   34 MLLACDDVVTE---DQLSWAPGFTDLPKKRGKK--------KDLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAM 99
Cdd:COG3321   27 NLRAGRDAITEvpaDRWDADAYYDPDPDAPGKTyvrwggflDDVDEFDAlffGISPREAEA---MDPQQRLLLEVAWEAL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17507095  100 VDAGINPRGLRGSQIGDFdecAtpGTSGT-----QKQNPVTEMGCIMSDTVPSMFSNRISYTFDLQGPS 163
Cdd:COG3321  104 EDAGYDPESLAGSRTGVF---V--GASSNdyallLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPS 167
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 65-115 5.84e-14

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 68.12  E-value: 5.84e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 17507095     65 DLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAMVDAGINPRGLRGSQIG 115
Cdd:smart00825  29 DVDLFDAaffGISPREAEA---MDPQQRLLLEVAWEALEDAGIDPESLRGSRTG 79
 
Name Accession Description Interval E-value
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 55-167 2.36e-23

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 92.70  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095    55 DLPKKRGKKKDLNKFDAGILPGTSKQNNPMDPQVRLLLEASWEAMVDAGINPRGLRGSQIGDFDECATPGTSGTQKQNP- 133
Cdd:pfam00109  55 KIYTKWGGLDDIFDFDPLFFGISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEd 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17507095   134 --VTEMGCIMSDTVPSMFSNRISYTFDLQGPSHSAD 167
Cdd:pfam00109 135 ggPRRGSPFAVGTMPSVIAGRISYFLGLRGPSVTVD 170
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 34-167 7.55e-23

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 94.16  E-value: 7.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095  34 MLLACDDVVTEDQLSW--APGFTDLPKKRGKK--------KDLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAMV 100
Cdd:cd00833  24 NLLEGRDAISEIPEDRwdADGYYPDPGKPGKTytrrggflDDVDAFDAaffGISPREAEA---MDPQQRLLLEVAWEALE 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507095 101 DAGINPRGLRGSQIGDFDECATPGTSGTQKQNPVTEMGCIMSDTVPSMFSNRISYTFDLQGPSHSAD 167
Cdd:cd00833 101 DAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVD 167
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 34-163 2.60e-21

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 90.32  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507095   34 MLLACDDVVTE---DQLSWAPGFTDLPKKRGKK--------KDLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAM 99
Cdd:COG3321   27 NLRAGRDAITEvpaDRWDADAYYDPDPDAPGKTyvrwggflDDVDEFDAlffGISPREAEA---MDPQQRLLLEVAWEAL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17507095  100 VDAGINPRGLRGSQIGDFdecAtpGTSGT-----QKQNPVTEMGCIMSDTVPSMFSNRISYTFDLQGPS 163
Cdd:COG3321  104 EDAGYDPESLAGSRTGVF---V--GASSNdyallLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPS 167
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 65-115 5.84e-14

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 68.12  E-value: 5.84e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 17507095     65 DLNKFDA---GILPGTSKQnnpMDPQVRLLLEASWEAMVDAGINPRGLRGSQIG 115
Cdd:smart00825  29 DVDLFDAaffGISPREAEA---MDPQQRLLLEVAWEALEDAGIDPESLRGSRTG 79
 
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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