NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|451173778|gb|AGF33800|]
View 

envelope glycoprotein, partial [Hepacivirus hominis]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HCV_env super family cl03255
Hepatitis C virus envelope glycoprotein E1;
1-52 1.04e-23

Hepatitis C virus envelope glycoprotein E1;


The actual alignment was detected with superfamily member pfam01539:

Pssm-ID: 110536  Cd Length: 190  Bit Score: 88.40  E-value: 1.04e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 451173778    1 TALVMAQVLRIPQAILDMVAGAHWGVLAGIAYFSMVGNWAKVAVVLLLFAGV 52
Cdd:pfam01539 138 ATMILAYALRVPEAVLDIIAGAHWGVLFGLAYFSMQGAWAKVLVILLLFAGV 189
HCV_NS1 super family cl03263
Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region ...
 57-86 1.06e-10

Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region of hepatitis C virus varies greatly between viral isolates. E2 is thought to encode a structurally unconstrained envelope protein.


The actual alignment was detected with superfamily member pfam01560:

Pssm-ID: 110557  Cd Length: 344  Bit Score: 55.63  E-value: 1.06e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 451173778   57 HVTGGSAGRTVAGLAGLFTQGPKQNIQLVN 86
Cdd:pfam01560   1 HVTGGSAARTTRGLVSLFSPGAKQNIQLIN 30
 
Name Accession Description Interval E-value
HCV_env pfam01539
Hepatitis C virus envelope glycoprotein E1;
1-52 1.04e-23

Hepatitis C virus envelope glycoprotein E1;


Pssm-ID: 110536  Cd Length: 190  Bit Score: 88.40  E-value: 1.04e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 451173778    1 TALVMAQVLRIPQAILDMVAGAHWGVLAGIAYFSMVGNWAKVAVVLLLFAGV 52
Cdd:pfam01539 138 ATMILAYALRVPEAVLDIIAGAHWGVLFGLAYFSMQGAWAKVLVILLLFAGV 189
HCV_NS1 pfam01560
Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region ...
 57-86 1.06e-10

Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region of hepatitis C virus varies greatly between viral isolates. E2 is thought to encode a structurally unconstrained envelope protein.


Pssm-ID: 110557  Cd Length: 344  Bit Score: 55.63  E-value: 1.06e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 451173778   57 HVTGGSAGRTVAGLAGLFTQGPKQNIQLVN 86
Cdd:pfam01560   1 HVTGGSAARTTRGLVSLFSPGAKQNIQLIN 30
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 24-77 2.37e-03

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 34.91  E-value: 2.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451173778  24 WGVLAGIAYFSMVGNWAKVA-----VVLLLFAGVGAET---HVTGGSAGRTVAGLAGLFTQG 77
Cdd:cd00707   74 WGRGANPNYPQAVNNTRVVGaelakFLDFLVDNTGLSLenvHLIGHSLGAHVAGFAGKRLNG 135
 
Name Accession Description Interval E-value
HCV_env pfam01539
Hepatitis C virus envelope glycoprotein E1;
1-52 1.04e-23

Hepatitis C virus envelope glycoprotein E1;


Pssm-ID: 110536  Cd Length: 190  Bit Score: 88.40  E-value: 1.04e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 451173778    1 TALVMAQVLRIPQAILDMVAGAHWGVLAGIAYFSMVGNWAKVAVVLLLFAGV 52
Cdd:pfam01539 138 ATMILAYALRVPEAVLDIIAGAHWGVLFGLAYFSMQGAWAKVLVILLLFAGV 189
HCV_NS1 pfam01560
Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region ...
 57-86 1.06e-10

Hepatitis C virus non-structural protein E2/NS1; The hypervariable region of the E2/NS1 region of hepatitis C virus varies greatly between viral isolates. E2 is thought to encode a structurally unconstrained envelope protein.


Pssm-ID: 110557  Cd Length: 344  Bit Score: 55.63  E-value: 1.06e-10
                          10        20        30
                  ....*....|....*....|....*....|
gi 451173778   57 HVTGGSAGRTVAGLAGLFTQGPKQNIQLVN 86
Cdd:pfam01560   1 HVTGGSAARTTRGLVSLFSPGAKQNIQLIN 30
Pancreat_lipase_like cd00707
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ...
 24-77 2.37e-03

Pancreatic lipase-like enzymes. 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: 238363 [Multi-domain]  Cd Length: 275  Bit Score: 34.91  E-value: 2.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 451173778  24 WGVLAGIAYFSMVGNWAKVA-----VVLLLFAGVGAET---HVTGGSAGRTVAGLAGLFTQG 77
Cdd:cd00707   74 WGRGANPNYPQAVNNTRVVGaelakFLDFLVDNTGLSLenvHLIGHSLGAHVAGFAGKRLNG 135
 
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