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Conserved domains on  [gi|4699764|pdb|1NPM|A]
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Chain A, NEUROPSIN

Protein Classification

serine protease( domain architecture ID 12184331)

trypsin-like serine protease such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

Gene Ontology:  GO:0008236|GO:0006508

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 4.90e-97

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


:

Pssm-ID: 214473 [Multi-domain]  Cd Length: 229  Bit Score: 282.26  E-value: 4.90e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A           1 ILEGRECIPHSQPWQAAL-FQGERLICGGVLVGDRWVLTAAHC----KKQKYSVRLGDHSLQSRDqPEQEIQVAQSIQHP 75
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGE-EGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A          76 CYNnsnPEDHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCE 153
Cdd:smart00020  81 NYN---PSTYDNDIALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1NPM_A         154 RAYPG--KITEGMVCAGSSN-GADTCQGDSGGPLVCD---GMLQGITSWGSdPCGKPEKPGVYTKICRYTTWI 220
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 4.90e-97

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473 [Multi-domain]  Cd Length: 229  Bit Score: 282.26  E-value: 4.90e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A           1 ILEGRECIPHSQPWQAAL-FQGERLICGGVLVGDRWVLTAAHC----KKQKYSVRLGDHSLQSRDqPEQEIQVAQSIQHP 75
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGE-EGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A          76 CYNnsnPEDHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCE 153
Cdd:smart00020  81 NYN---PSTYDNDIALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1NPM_A         154 RAYPG--KITEGMVCAGSSN-GADTCQGDSGGPLVCD---GMLQGITSWGSdPCGKPEKPGVYTKICRYTTWI 220
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-223 2.06e-96

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 280.70  E-value: 2.06e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A        1 ILEGRECIPHSQPWQAALFQGE-RLICGGVLVGDRWVLTAAHC----KKQKYSVRLGDHSLQSRDQPEQEIQVAQSIQHP 75
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       76 CYNNSNpedHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTvTSPQENFPNTLNCAEVKIYSQNKCE 153
Cdd:cd00190  81 NYNPST---YDNDIALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NPM_A      154 RAY--PGKITEGMVCAGSSN-GADTCQGDSGGPLVCD----GMLQGITSWGSDpCGKPEKPGVYTKICRYTTWIKKT 223
Cdd:cd00190 157 RAYsyGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-220 1.63e-80

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 240.04  E-value: 1.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A          1 ILEGRECIPHSQPWQAAL-FQGERLICGGVLVGDRWVLTAAHCKK--QKYSVRLGDHSLQSRDQPEQEIQVAQSIQHPCY 77
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A         78 NnsnPEDHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTVTSPqeNFPNTLNCAEVKIYSQNKCERA 155
Cdd:pfam00089  81 N---PDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1NPM_A        156 YPGKITEGMVCAGsSNGADTCQGDSGGPLVC-DGMLQGITSWGsDPCGKPEKPGVYTKICRYTTWI 220
Cdd:pfam00089 156 YGGTVTDTMICAG-AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-224 1.80e-22

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 94.17  E-value: 1.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       12 QPWQAALFQGERL-----ICGGVLVGDRWVLTAAHC--KKQKYS--VRLGDHSLQSRDQPEQeIQVAQSIQHPCYNNSN- 81
Cdd:COG5640  44 YPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCadASSPISsdVNRVVVDLNDSSQAER-GHVRTIYVHEFYSPGNl 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       82 --------PEDHShDIMLIRLQNSANlgdkvkPVQLANLCPKVGQKCIIsGWGTVT--SPQENFPN-------TLNCAEV 144
Cdd:COG5640 123 gndiavleLARAA-SLPRVKITSFDA------SDTFLNSVTTVSPMTNG-TFGVTTpsDVPRSSPKgtilhevAVLFVPL 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A      145 KIYSQNK-CERAYPGKITEGMVCAGSSnGADTCQGDSGGPLVCDG----MLQGITSWGSDPCGKPEKPGVYTKICRYTTW 219
Cdd:COG5640 195 STCAQYKgCANASDGATGLTGFCAGRP-PKDACQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTLIPGVYTNVSNYQDW 273

                ....*
1NPM_A      220 IKKTM 224
Cdd:COG5640 274 IAAMT 278
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 4.90e-97

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473 [Multi-domain]  Cd Length: 229  Bit Score: 282.26  E-value: 4.90e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A           1 ILEGRECIPHSQPWQAAL-FQGERLICGGVLVGDRWVLTAAHC----KKQKYSVRLGDHSLQSRDqPEQEIQVAQSIQHP 75
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGE-EGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A          76 CYNnsnPEDHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCE 153
Cdd:smart00020  81 NYN---PSTYDNDIALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1NPM_A         154 RAYPG--KITEGMVCAGSSN-GADTCQGDSGGPLVCD---GMLQGITSWGSdPCGKPEKPGVYTKICRYTTWI 220
Cdd:smart00020 158 RAYSGggAITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-223 2.06e-96

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 280.70  E-value: 2.06e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A        1 ILEGRECIPHSQPWQAALFQGE-RLICGGVLVGDRWVLTAAHC----KKQKYSVRLGDHSLQSRDQPEQEIQVAQSIQHP 75
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       76 CYNNSNpedHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTvTSPQENFPNTLNCAEVKIYSQNKCE 153
Cdd:cd00190  81 NYNPST---YDNDIALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NPM_A      154 RAY--PGKITEGMVCAGSSN-GADTCQGDSGGPLVCD----GMLQGITSWGSDpCGKPEKPGVYTKICRYTTWIKKT 223
Cdd:cd00190 157 RAYsyGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-220 1.63e-80

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 240.04  E-value: 1.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A          1 ILEGRECIPHSQPWQAAL-FQGERLICGGVLVGDRWVLTAAHCKK--QKYSVRLGDHSLQSRDQPEQEIQVAQSIQHPCY 77
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A         78 NnsnPEDHSHDIMLIRLQNSANLGDKVKPVQLA--NLCPKVGQKCIISGWGTVTSPqeNFPNTLNCAEVKIYSQNKCERA 155
Cdd:pfam00089  81 N---PDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1NPM_A        156 YPGKITEGMVCAGsSNGADTCQGDSGGPLVC-DGMLQGITSWGsDPCGKPEKPGVYTKICRYTTWI 220
Cdd:pfam00089 156 YGGTVTDTMICAG-AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-224 1.80e-22

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 94.17  E-value: 1.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       12 QPWQAALFQGERL-----ICGGVLVGDRWVLTAAHC--KKQKYS--VRLGDHSLQSRDQPEQeIQVAQSIQHPCYNNSN- 81
Cdd:COG5640  44 YPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCadASSPISsdVNRVVVDLNDSSQAER-GHVRTIYVHEFYSPGNl 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       82 --------PEDHShDIMLIRLQNSANlgdkvkPVQLANLCPKVGQKCIIsGWGTVT--SPQENFPN-------TLNCAEV 144
Cdd:COG5640 123 gndiavleLARAA-SLPRVKITSFDA------SDTFLNSVTTVSPMTNG-TFGVTTpsDVPRSSPKgtilhevAVLFVPL 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A      145 KIYSQNK-CERAYPGKITEGMVCAGSSnGADTCQGDSGGPLVCDG----MLQGITSWGSDPCGKPEKPGVYTKICRYTTW 219
Cdd:COG5640 195 STCAQYKgCANASDGATGLTGFCAGRP-PKDACQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTLIPGVYTNVSNYQDW 273

                ....*
1NPM_A      220 IKKTM 224
Cdd:COG5640 274 IAAMT 278
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
32-213 5.67e-06

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: 45.37  E-value: 5.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A       32 GDRWVLTAAHCKKQKYSVRLGDHSLQsrdqpeqEIQVAQSIQHPcynnsnpedhSHDIMLIRLQNSA--------NLGDK 103
Cdd:cd21112  26 GTPYFLTAGHCGNGGGTVYADGALGV-------PIGTVVASSFP----------GNDYALVRVTNPGwtpppevrTYGGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A      104 VKPVQLANLcPKVGQK-C---IISGW--GTVTSpqenfpntLNCaevkiySQNkceraYPGKITEGMVcagssnGADTC- 176
Cdd:cd21112  89 TVPITGSAE-PVVGAPvCksgRTTGWtcGTVTA--------VNV------TVN-----YPGGTVTGLT------RTNACa 142
                       170       180       190
                ....*....|....*....|....*....|....*...
1NPM_A      177 -QGDSGGPLVCDGMLQGITSWGSDPCGKPEKPGVYTKI 213
Cdd:cd21112 143 ePGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 180
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
28-193 4.02e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.25  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A         28 GVLVG-DRWVLTAAHCKKQKYSVRLGDHSLQSRDQPEQEIQVAQSiqhpcynnsnpeDHSHDIMLIRLQNSanlGDKVKP 106
Cdd:pfam13365   3 GFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR------------DPDLDLALLRVSGD---GRGLPP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NPM_A        107 VQLAN-LCPKVGQKCIISGWgtvtsPQENFPNTLNCAEVkiysqNKCERAYPGKITEGMVCAgssnGADTCQGDSGGPLV 185
Cdd:pfam13365  68 LPLGDsEPLVGGERVYAVGY-----PLGGEKLSLSEGIV-----SGVDEGRDGGDDGRVIQT----DAALSPGSSGGPVF 133

                  ....*....
1NPM_A        186 -CDGMLQGI 193
Cdd:pfam13365 134 dADGRVVGI 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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