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Conserved domains on  [gi|998614217|ref|NP_001307261|]
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kallikrein-1 isoform 3 [Mus musculus]

Protein Classification

S1 family serine peptidase( domain architecture ID 12184331)

S1 family trypsin-like serine peptidase such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

CATH:  2.40.10.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S1
PubMed:  25664608|29785722|31895561|7845208
SCOP:  3000114

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 ...
 15-151 9.64e-66

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  Cd Length: 229  Bit Score: 199.83  E-value: 9.64e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217    15 YSNDLMLLRLKKPADITDVVKPIDLPT--EEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAKAH--IEKV 90
Cdd:smart00020  87 YDNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYsgGGAI 166

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998614217    91 TDDMLCAGDMDGGKDTCAGDSGGPLICD---GVLQGITSWGpSPCGKPNVPGIYTRVLNFNTWI 151
Cdd:smart00020 167 TDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 15-151 9.64e-66

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  Cd Length: 229  Bit Score: 199.83  E-value: 9.64e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217    15 YSNDLMLLRLKKPADITDVVKPIDLPT--EEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAKAH--IEKV 90
Cdd:smart00020  87 YDNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYsgGGAI 166

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998614217    91 TDDMLCAGDMDGGKDTCAGDSGGPLICD---GVLQGITSWGpSPCGKPNVPGIYTRVLNFNTWI 151
Cdd:smart00020 167 TDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 13-154 1.55e-64

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: 197.11  E-value: 1.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  13 DDYSNDLMLLRLKKPADITDVVKPIDLPT--EEPKLGSTCLASGWGSITPvKYEYPDELQCVNLKLLPNEDCAKAHI--E 88
Cdd:cd00190   85 STYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSE-GGPLPDVLQEVNVPIVSNAECKRAYSygG 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  89 KVTDDMLCAGDMDGGKDTCAGDSGGPLICD----GVLQGITSWGpSPCGKPNVPGIYTRVLNFNTWIRET 154
Cdd:cd00190  164 TITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
13-151 1.30e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 163.77  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217   13 DDYSNDLMLLRLKKPADITDVVKPIDLPTEEPKL--GSTCLASGWGSITPVKYeyPDELQCVNLKLLPNEDCAKAHIEKV 90
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSAYGGTV 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614217   91 TDDMLCAGdmDGGKDTCAGDSGGPLIC-DGVLQGITSWGPsPCGKPNVPGIYTRVLNFNTWI 151
Cdd:pfam00089 161 TDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 14-159 1.15e-43

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.79  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  14 DYSNDLMLLRLKKPADitdVVKPIDLPT--EEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAkAHIEKVT 91
Cdd:COG5640  116 TPGNDIALLKLATPVP---GVAPAPLATsaDAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDG 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614217  92 DDMLCAGDMDGGKDTCAGDSGGPLI----CDGVLQGITSWGPSPCGkPNVPGIYTRVLNFNTWIRETMAEND 159
Cdd:COG5640  192 GTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 15-151 9.64e-66

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  Cd Length: 229  Bit Score: 199.83  E-value: 9.64e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217    15 YSNDLMLLRLKKPADITDVVKPIDLPT--EEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAKAH--IEKV 90
Cdd:smart00020  87 YDNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYsgGGAI 166

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998614217    91 TDDMLCAGDMDGGKDTCAGDSGGPLICD---GVLQGITSWGpSPCGKPNVPGIYTRVLNFNTWI 151
Cdd:smart00020 167 TDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 13-154 1.55e-64

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: 197.11  E-value: 1.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  13 DDYSNDLMLLRLKKPADITDVVKPIDLPT--EEPKLGSTCLASGWGSITPvKYEYPDELQCVNLKLLPNEDCAKAHI--E 88
Cdd:cd00190   85 STYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSE-GGPLPDVLQEVNVPIVSNAECKRAYSygG 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  89 KVTDDMLCAGDMDGGKDTCAGDSGGPLICD----GVLQGITSWGpSPCGKPNVPGIYTRVLNFNTWIRET 154
Cdd:cd00190  164 TITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
13-151 1.30e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 163.77  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217   13 DDYSNDLMLLRLKKPADITDVVKPIDLPTEEPKL--GSTCLASGWGSITPVKYeyPDELQCVNLKLLPNEDCAKAHIEKV 90
Cdd:pfam00089  83 DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSAYGGTV 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614217   91 TDDMLCAGdmDGGKDTCAGDSGGPLIC-DGVLQGITSWGPsPCGKPNVPGIYTRVLNFNTWI 151
Cdd:pfam00089 161 TDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 14-159 1.15e-43

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.79  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998614217  14 DYSNDLMLLRLKKPADitdVVKPIDLPT--EEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAkAHIEKVT 91
Cdd:COG5640  116 TPGNDIALLKLATPVP---GVAPAPLATsaDAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDG 191

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998614217  92 DDMLCAGDMDGGKDTCAGDSGGPLI----CDGVLQGITSWGPSPCGkPNVPGIYTRVLNFNTWIRETMAEND 159
Cdd:COG5640  192 GTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGLG 262
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 105-144 1.81e-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: 1.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 998614217 105 DTCA--GDSGGPLICDGVLQGITSWGPSPCGKPNVPGIYTRV 144
Cdd:cd21112  139 NACAepGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 180
 
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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