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Conserved domains on  [gi|987650141|gb|AME15784|]
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putative P1 protein, partial [Pepper vein yellows virus]

Protein Classification

Peptidase_S39 domain-containing protein( domain architecture ID 10489322)

Peptidase_S39 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S39 pfam02122
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.
 9-128 3.64e-56

Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.


:

Pssm-ID: 111059  Cd Length: 203  Bit Score: 174.87  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987650141    9 FMLMSGPPNWESLLGCKGAHFVSVSQLAKSKMRFFFIEKNEWMADHGEIVGPrDHWFATTLCNSEPGHSGTPIFNGKTIV 88
Cdd:pfam02122  82 ILILVGPPNWESILGCKAVHFTTADQLAKGPASFYTLRKDEWPSSSAKIPGS-EGKFASVLSNTSPGHSGTPYFSGKNVV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 987650141   89 GVHAG---GENEQNFNVMATIPPVPGLTTPQYVFETTAPQGRV 128
Cdd:pfam02122 161 GVHKGsasGSERENYNLMSPIPPIPGLTSPKYVFETTAPQGRV 203
 
Name Accession Description Interval E-value
Peptidase_S39 pfam02122
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.
 9-128 3.64e-56

Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.


Pssm-ID: 111059  Cd Length: 203  Bit Score: 174.87  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987650141    9 FMLMSGPPNWESLLGCKGAHFVSVSQLAKSKMRFFFIEKNEWMADHGEIVGPrDHWFATTLCNSEPGHSGTPIFNGKTIV 88
Cdd:pfam02122  82 ILILVGPPNWESILGCKAVHFTTADQLAKGPASFYTLRKDEWPSSSAKIPGS-EGKFASVLSNTSPGHSGTPYFSGKNVV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 987650141   89 GVHAG---GENEQNFNVMATIPPVPGLTTPQYVFETTAPQGRV 128
Cdd:pfam02122 161 GVHKGsasGSERENYNLMSPIPPIPGLTSPKYVFETTAPQGRV 203
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 65-94 8.03e-04

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 38.06  E-value: 8.03e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 987650141  65 FATTLCnSEPGHSGTPIFNGKTIVGVHAGG 94
Cdd:cd21112  136 TRTNAC-AEPGDSGGPVFSGTQALGITSGG 164
 
Name Accession Description Interval E-value
Peptidase_S39 pfam02122
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.
 9-128 3.64e-56

Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses.


Pssm-ID: 111059  Cd Length: 203  Bit Score: 174.87  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987650141    9 FMLMSGPPNWESLLGCKGAHFVSVSQLAKSKMRFFFIEKNEWMADHGEIVGPrDHWFATTLCNSEPGHSGTPIFNGKTIV 88
Cdd:pfam02122  82 ILILVGPPNWESILGCKAVHFTTADQLAKGPASFYTLRKDEWPSSSAKIPGS-EGKFASVLSNTSPGHSGTPYFSGKNVV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 987650141   89 GVHAG---GENEQNFNVMATIPPVPGLTTPQYVFETTAPQGRV 128
Cdd:pfam02122 161 GVHKGsasGSERENYNLMSPIPPIPGLTSPKYVFETTAPQGRV 203
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 65-94 8.03e-04

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 38.06  E-value: 8.03e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 987650141  65 FATTLCnSEPGHSGTPIFNGKTIVGVHAGG 94
Cdd:cd21112  136 TRTNAC-AEPGDSGGPVFSGTQALGITSGG 164
 
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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