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Conserved domains on  [gi|527121930|ref|NP_001268360|]
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kallikrein-8 isoform 5 [Homo sapiens]

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
PubMed:  25664608|29785722|31895561

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 ...
 1-131 1.24e-54

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: 170.94  E-value: 1.24e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930     1 MLLQLRDQASLGSKVKPISLAD--HCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQ--ITDGMV 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 527121930    77 CAGSS-KGADTCQGDSGGPLVCDGA---LQGITSWGSdPCGRSDKPGVYTNICRYLDWI 131
Cdd:smart00020 172 CAGGLeGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-131 1.24e-54

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: 170.94  E-value: 1.24e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930     1 MLLQLRDQASLGSKVKPISLAD--HCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQ--ITDGMV 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 527121930    77 CAGSS-KGADTCQGDSGGPLVCDGA---LQGITSWGSdPCGRSDKPGVYTNICRYLDWI 131
Cdd:smart00020 172 CAGGLeGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-134 5.70e-53

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: 166.68  E-value: 5.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930   1 MLLQLRDQASLGSKVKPISLA--DHCTQPGQKCTVSGWGTvTSPRENFPDTLNCAEVKIFPQKKCEDAY--PGQITDGMV 76
Cdd:cd00190   92 ALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNML 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527121930  77 CAGSSK-GADTCQGDSGGPLVCD----GALQGITSWGSDpCGRSDKPGVYTNICRYLDWIKKI 134
Cdd:cd00190  171 CAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-131 1.21e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930    1 MLLQLRDQASLGSKVKPISLADHC--TQPGQKCTVSGWGTVTSPreNFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCA 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 527121930   79 GsSKGADTCQGDSGGPLVC-DGALQGITSWGsDPCGRSDKPGVYTNICRYLDWI 131
Cdd:pfam00089 168 G-AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 13-137 2.39e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.44  E-value: 2.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930  13 SKVKPISLAD--HCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCeDAYPGQITDGMVCAGSSKG-ADTCQG 89
Cdd:COG5640  131 PGVAPAPLATsaDAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGgKDACQG 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527121930  90 DSGGPLV----CDGALQGITSWGSDPCGRsDKPGVYTNICRYLDWIKKIIGS 137
Cdd:COG5640  210 DSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-131 1.24e-54

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: 170.94  E-value: 1.24e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930     1 MLLQLRDQASLGSKVKPISLAD--HCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQ--ITDGMV 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 527121930    77 CAGSS-KGADTCQGDSGGPLVCDGA---LQGITSWGSdPCGRSDKPGVYTNICRYLDWI 131
Cdd:smart00020 172 CAGGLeGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-134 5.70e-53

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: 166.68  E-value: 5.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930   1 MLLQLRDQASLGSKVKPISLA--DHCTQPGQKCTVSGWGTvTSPRENFPDTLNCAEVKIFPQKKCEDAY--PGQITDGMV 76
Cdd:cd00190   92 ALLKLKRPVTLSDNVRPICLPssGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNML 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527121930  77 CAGSSK-GADTCQGDSGGPLVCD----GALQGITSWGSDpCGRSDKPGVYTNICRYLDWIKKI 134
Cdd:cd00190  171 CAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-131 1.21e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930    1 MLLQLRDQASLGSKVKPISLADHC--TQPGQKCTVSGWGTVTSPreNFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCA 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 527121930   79 GsSKGADTCQGDSGGPLVC-DGALQGITSWGsDPCGRSDKPGVYTNICRYLDWI 131
Cdd:pfam00089 168 G-AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 13-137 2.39e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.44  E-value: 2.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527121930  13 SKVKPISLAD--HCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCeDAYPGQITDGMVCAGSSKG-ADTCQG 89
Cdd:COG5640  131 PGVAPAPLATsaDAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGgKDACQG 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527121930  90 DSGGPLV----CDGALQGITSWGSDPCGRsDKPGVYTNICRYLDWIKKIIGS 137
Cdd:COG5640  210 DSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVSAYRDWIKSTAGG 260
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 84-122 9.96e-05

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: 40.37  E-value: 9.96e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 527121930  84 ADTC--QGDSGGPLVCDGALQGITSWGSDPCGRSDKPGVYT 122
Cdd:cd21112  138 TNACaePGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQ 178
 
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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