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Conserved domains on  [gi|1902393534|dbj|GGI77362|]
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serine protease [Saccharopolyspora subtropica]

Protein Classification

S1 family peptidase( domain architecture ID 15340045)

S1 family peptidase is a member of a family with a wide range of functions and specificities, containing the catalytic triad His, Asp and Ser

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 180-361 1.45e-79

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: 241.83  E-value: 1.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 180 IIGGDAYYM--GGRCSVGFSVRTSSGAGGFVTAGHCGTAGTAV--QGYNGVSMGTFRDSSFPGNDYAWVA-TNSSWTPQP 254
Cdd:cd21112     1 LRGGDGIYSggGGRCSLGFNVTDGSGTPYFLTAGHCGNGGGTVyaDGALGVPIGTVVASSFPGNDYALVRvTNPGWTPPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 255 RVNLYNGSTRLVSGASVAPVGSSICRSGSTTGWHCGSVQALNQTVRYPQGTVYGLTRTNVCAEPGDSGGSFISGNQAQGM 334
Cdd:cd21112    81 EVRTYGGGTVPITGSAEPVVGAPVCKSGRTTGWTCGTVTAVNVTVNYPGGTVTGLTRTNACAEPGDSGGPVFSGTQALGI 160

                         170       180
                  ....*....|....*....|....*...
gi 1902393534 335 TSGGSGDCTFG-GTTYFQPVQEALSAYN 361
Cdd:cd21112   161 TSGGSGNCGSGgGTSYFQPVNPVLSAYG 188
 
Name Accession Description Interval E-value
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 180-361 1.45e-79

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: 241.83  E-value: 1.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 180 IIGGDAYYM--GGRCSVGFSVRTSSGAGGFVTAGHCGTAGTAV--QGYNGVSMGTFRDSSFPGNDYAWVA-TNSSWTPQP 254
Cdd:cd21112     1 LRGGDGIYSggGGRCSLGFNVTDGSGTPYFLTAGHCGNGGGTVyaDGALGVPIGTVVASSFPGNDYALVRvTNPGWTPPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 255 RVNLYNGSTRLVSGASVAPVGSSICRSGSTTGWHCGSVQALNQTVRYPQGTVYGLTRTNVCAEPGDSGGSFISGNQAQGM 334
Cdd:cd21112    81 EVRTYGGGTVPITGSAEPVVGAPVCKSGRTTGWTCGTVTAVNVTVNYPGGTVTGLTRTNACAEPGDSGGPVFSGTQALGI 160

                         170       180
                  ....*....|....*....|....*...
gi 1902393534 335 TSGGSGDCTFG-GTTYFQPVQEALSAYN 361
Cdd:cd21112   161 TSGGSGNCGSGgGTSYFQPVNPVLSAYG 188
Trypsin pfam00089
Trypsin;
180-358 1.20e-18

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 83.65  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 180 IIGGDAYYMG-GRCSVGFSVRTSS-GAGGF-------VTAGHCGTAGTAVQGYNG---------------VSMGTF---R 232
Cdd:pfam00089   1 IVGGDEAQPGsFPWQVSLQLSSGKhFCGGSlisenwvLTAAHCVSGASDVKVVLGahnivlreggeqkfdVEKIIVhpnY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 233 DSSFPGNDYAWVATNSSWTPQPRVNLYNgstrLVSGASVAPVGSSICRSGSTTGWHCGSVQALNQ-TVR-YPQGTV---- 306
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPIC----LPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEvTVPvVSRETCrsay 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1902393534 307 -YGLTRTNVCAE-------PGDSGGSFISGNQ-AQGMTSGGSGdCTFGGT-TYFQPVQEALS 358
Cdd:pfam00089 157 gGTVTDTMICAGaggkdacQGDSGGPLVCSDGeLIGIVSWGYG-CASGNYpGVYTPVSSYLD 217
 
Name Accession Description Interval E-value
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 180-361 1.45e-79

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: 241.83  E-value: 1.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 180 IIGGDAYYM--GGRCSVGFSVRTSSGAGGFVTAGHCGTAGTAV--QGYNGVSMGTFRDSSFPGNDYAWVA-TNSSWTPQP 254
Cdd:cd21112     1 LRGGDGIYSggGGRCSLGFNVTDGSGTPYFLTAGHCGNGGGTVyaDGALGVPIGTVVASSFPGNDYALVRvTNPGWTPPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 255 RVNLYNGSTRLVSGASVAPVGSSICRSGSTTGWHCGSVQALNQTVRYPQGTVYGLTRTNVCAEPGDSGGSFISGNQAQGM 334
Cdd:cd21112    81 EVRTYGGGTVPITGSAEPVVGAPVCKSGRTTGWTCGTVTAVNVTVNYPGGTVTGLTRTNACAEPGDSGGPVFSGTQALGI 160

                         170       180
                  ....*....|....*....|....*...
gi 1902393534 335 TSGGSGDCTFG-GTTYFQPVQEALSAYN 361
Cdd:cd21112   161 TSGGSGNCGSGgGTSYFQPVNPVLSAYG 188
Trypsin pfam00089
Trypsin;
180-358 1.20e-18

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 83.65  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 180 IIGGDAYYMG-GRCSVGFSVRTSS-GAGGF-------VTAGHCGTAGTAVQGYNG---------------VSMGTF---R 232
Cdd:pfam00089   1 IVGGDEAQPGsFPWQVSLQLSSGKhFCGGSlisenwvLTAAHCVSGASDVKVVLGahnivlreggeqkfdVEKIIVhpnY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1902393534 233 DSSFPGNDYAWVATNSSWTPQPRVNLYNgstrLVSGASVAPVGSSICRSGSTTGWHCGSVQALNQ-TVR-YPQGTV---- 306
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPIC----LPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEvTVPvVSRETCrsay 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1902393534 307 -YGLTRTNVCAE-------PGDSGGSFISGNQ-AQGMTSGGSGdCTFGGT-TYFQPVQEALS 358
Cdd:pfam00089 157 gGTVTDTMICAGaggkdacQGDSGGPLVCSDGeLIGIVSWGYG-CASGNYpGVYTPVSSYLD 217
 
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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