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Conserved domains on  [gi|613253558|gb|EZY59622|]
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hypothetical protein V061_02758 [Staphylococcus aureus R0353]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CVT17 super family cl44199
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 10-87 6.28e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG5153:

Pssm-ID: 444061  Cd Length: 405  Bit Score: 43.85  E-value: 6.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613253558  10 DRTPAKFAPSQMDESDAFTESVKKKYPDSEIHPIGHSLGAFLAQYNLIKHNLDNgTTFAAPNL-YHSFTGDFKKEIDNG 87
Cdd:COG5153   91 EQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVATGLSK-VTFAAPGSgNHALADDLGKRIDAG 168
 
Name Accession Description Interval E-value
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 10-87 6.28e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 43.85  E-value: 6.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613253558  10 DRTPAKFAPSQMDESDAFTESVKKKYPDSEIHPIGHSLGAFLAQYNLIKHNLDNgTTFAAPNL-YHSFTGDFKKEIDNG 87
Cdd:COG5153   91 EQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVATGLSK-VTFAAPGSgNHALADDLGKRIDAG 168
Lipase_3 pfam01764
Lipase (class 3);
29-103 5.76e-04

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613253558   29 ESVKKKYPDSEIHPIGHSLG---AFLAQYNLIKHNLDNGT-----TFAAPnlyhsFTGD--FKKEIDNGVyDSKIRNIGH 98
Cdd:pfam01764  54 KRLLEKYPDYSIVVTGHSLGgalASLAALDLVENGLRLSSrvtvvTFGQP-----RVGNleFAKLHDSQG-PKFSYRVVH 127


                  ....*
gi 613253558   99 FDDPI 103
Cdd:pfam01764 128 QRDIV 132
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 29-103 9.46e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 34.01  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613253558  29 ESVKKKYPDSEIHPIGHSLG---AFLAQYNLIKHNLDNG---TTFAAPNLyhsFTGDFKKEIDNGVYDSKIRNIGHFDDP 102
Cdd:cd00741   19 KSALAQYPDYKIHVTGHSLGgalAGLAGLDLRGRGLGRLvrvYTFGPPRV---GNAAFAEDRLDPSDALFVDRIVNDNDI 95


                 .
gi 613253558 103 I 103
Cdd:cd00741   96 V 96
 
Name Accession Description Interval E-value
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 10-87 6.28e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 43.85  E-value: 6.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613253558  10 DRTPAKFAPSQMDESDAFTESVKKKYPDSEIHPIGHSLGAFLAQYNLIKHNLDNgTTFAAPNL-YHSFTGDFKKEIDNG 87
Cdd:COG5153   91 EQYAAQVMDLDYDGAEELAAEVKKQYPDAELSLTGHSLGGALASLVAVATGLSK-VTFAAPGSgNHALADDLGKRIDAG 168
Lipase_3 pfam01764
Lipase (class 3);
29-103 5.76e-04

Lipase (class 3);


Pssm-ID: 396362 [Multi-domain]  Cd Length: 139  Bit Score: 37.24  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613253558   29 ESVKKKYPDSEIHPIGHSLG---AFLAQYNLIKHNLDNGT-----TFAAPnlyhsFTGD--FKKEIDNGVyDSKIRNIGH 98
Cdd:pfam01764  54 KRLLEKYPDYSIVVTGHSLGgalASLAALDLVENGLRLSSrvtvvTFGQP-----RVGNleFAKLHDSQG-PKFSYRVVH 127


                  ....*
gi 613253558   99 FDDPI 103
Cdd:pfam01764 128 QRDIV 132
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
8-52 5.05e-03

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


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 35.24  E-value: 5.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 613253558   8 IGDRTPAKFAPSQMDESD-------AFTESVKKKYPDSEIHPIGHSLGAFLA 52
Cdd:COG4757   70 IGLSRPGSLRGFDAGYRDwgeldlpAVLDALRARFPGLPLLLVGHSLGGQLL 121
Lipase cd00741
Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and ...
 29-103 9.46e-03

Lipase. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation", the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238382 [Multi-domain]  Cd Length: 153  Bit Score: 34.01  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613253558  29 ESVKKKYPDSEIHPIGHSLG---AFLAQYNLIKHNLDNG---TTFAAPNLyhsFTGDFKKEIDNGVYDSKIRNIGHFDDP 102
Cdd:cd00741   19 KSALAQYPDYKIHVTGHSLGgalAGLAGLDLRGRGLGRLvrvYTFGPPRV---GNAAFAEDRLDPSDALFVDRIVNDNDI 95


                 .
gi 613253558 103 I 103
Cdd:cd00741   96 V 96
 
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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