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Conserved domains on  [gi|1131345312|ref|NP_001335107|]
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kallikrein-13 isoform 3 precursor [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
PubMed:  18259688

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 16-109 1.52e-45

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: 147.42  E-value: 1.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  16 SGVNYPKTLQCANIQLRSDEECRQVY--PGKITDNMLCAGTKEGGKDSCEGDSGGPLVCNR----TLYGIVSWGDFpCGQ 89
Cdd:cd00190   134 EGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSG-CAR 212

                          90       100
                  ....*....|....*....|
gi 1131345312  90 PDRPGVYTRVSRYVLWIRET 109
Cdd:cd00190   213 PNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 16-109 1.52e-45

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: 147.42  E-value: 1.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  16 SGVNYPKTLQCANIQLRSDEECRQVY--PGKITDNMLCAGTKEGGKDSCEGDSGGPLVCNR----TLYGIVSWGDFpCGQ 89
Cdd:cd00190   134 EGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSG-CAR 212

                          90       100
                  ....*....|....*....|
gi 1131345312  90 PDRPGVYTRVSRYVLWIRET 109
Cdd:cd00190   213 PNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 12-106 8.68e-45

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: 145.13  E-value: 8.68e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312   12 TLALSGVNYPKTLQCANIQLRSDEECRQVYPG--KITDNMLCAGTKEGGKDSCEGDSGGPLVCN---RTLYGIVSWGDfP 86
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-G 209

                           90       100
                   ....*....|....*....|
gi 1131345312   87 CGQPDRPGVYTRVSRYVLWI 106
Cdd:smart00020 210 CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
19-106 7.23e-36

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 122.17  E-value: 7.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  19 NYPKTLQCANIQLRSDEECRQVYPGKITDNMLCAGTkeGGKDSCEGDSGGPLVC-NRTLYGIVSWGDfPCGQPDRPGVYT 97
Cdd:pfam00089 134 GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYT 210


                  ....*....
gi 1131345312  98 RVSRYVLWI 106
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 19-112 3.85e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 113.59  E-value: 3.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  19 NYPKTLQCANIQLRSDEECrQVYPGKITDNMLCAGTKEGGKDSCEGDSGGPLV----CNRTLYGIVSWGDFPCGqPDRPG 94
Cdd:COG5640   165 SQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPG 242

                          90
                  ....*....|....*...
gi 1131345312  95 VYTRVSRYVLWIRETIRK 112
Cdd:COG5640   243 VYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 16-109 1.52e-45

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: 147.42  E-value: 1.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  16 SGVNYPKTLQCANIQLRSDEECRQVY--PGKITDNMLCAGTKEGGKDSCEGDSGGPLVCNR----TLYGIVSWGDFpCGQ 89
Cdd:cd00190   134 EGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSG-CAR 212

                          90       100
                  ....*....|....*....|
gi 1131345312  90 PDRPGVYTRVSRYVLWIRET 109
Cdd:cd00190   213 PNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 12-106 8.68e-45

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: 145.13  E-value: 8.68e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312   12 TLALSGVNYPKTLQCANIQLRSDEECRQVYPG--KITDNMLCAGTKEGGKDSCEGDSGGPLVCN---RTLYGIVSWGDfP 86
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-G 209

                           90       100
                   ....*....|....*....|
gi 1131345312   87 CGQPDRPGVYTRVSRYVLWI 106
Cdd:smart00020 210 CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
19-106 7.23e-36

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 122.17  E-value: 7.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  19 NYPKTLQCANIQLRSDEECRQVYPGKITDNMLCAGTkeGGKDSCEGDSGGPLVC-NRTLYGIVSWGDfPCGQPDRPGVYT 97
Cdd:pfam00089 134 GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYT 210


                  ....*....
gi 1131345312  98 RVSRYVLWI 106
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 19-112 3.85e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 113.59  E-value: 3.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131345312  19 NYPKTLQCANIQLRSDEECrQVYPGKITDNMLCAGTKEGGKDSCEGDSGGPLV----CNRTLYGIVSWGDFPCGqPDRPG 94
Cdd:COG5640   165 SQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPG 242

                          90
                  ....*....|....*...
gi 1131345312  95 VYTRVSRYVLWIRETIRK 112
Cdd:COG5640   243 VYTRVSAYRDWIKSTAGG 260
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 64-99 3.17e-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: 41.14  E-value: 3.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1131345312  64 GDSGGPLVCNRTLYGIVSWGDFPCGQPDRPGVYTRV 99
Cdd:cd21112   145 GDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 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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