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Conserved domains on  [gi|1370475511|ref|XP_024307379|]
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kallikrein-6 isoform X1 [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 ...
 1-130 4.59e-58

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: 179.41  E-value: 4.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511    1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGD--FPDTIQCAYIHLVSREECEHAYPGQ--ITQNML 74
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPicLPSSNYNVPAGTTCTVSGWGRTSEGAgsLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370475511   75 CAGDEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 130
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-130 4.59e-58

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: 179.41  E-value: 4.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511    1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGD--FPDTIQCAYIHLVSREECEHAYPGQ--ITQNML 74
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPicLPSSNYNVPAGTTCTVSGWGRTSEGAgsLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370475511   75 CAGDEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 130
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-133 7.03e-57

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: 176.70  E-value: 7.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGD-FPDTIQCAYIHLVSREECEHAY--PGQITQNMLC 75
Cdd:cd00190    92 ALLKLKRPVTLSDNVRPicLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLC 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475511  76 AGDEKYGKDSCQGDSGGPLVCGDH----LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWIQKT 133
Cdd:cd00190   172 AGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-130 1.72e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 1.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGD 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPicLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370475511  79 ekYGKDSCQGDSGGPLVCGDH-LRGLVSWGNiPCGSKEKPGVYTNVCRYTNWI 130
Cdd:pfam00089 170 --GGKDACQGDSGGPLVCSDGeLIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-134 8.88e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.91  E-value: 8.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   2 LLRLARPAKLselIQPLPL--ERDCSANTTSCHILGWGKTA--DGDFPDTIQCAYIHLVSREECEhAYPGQITQNMLCAG 77
Cdd:COG5640   123 LLKLATPVPG---VAPAPLatSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAG 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370475511  78 DEKYGKDSCQGDSGGPLV----CGDHLRGLVSWGNIPCGSKeKPGVYTNVCRYTNWIQKTI 134
Cdd:COG5640   199 YPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1-130 4.59e-58

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: 179.41  E-value: 4.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511    1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGD--FPDTIQCAYIHLVSREECEHAYPGQ--ITQNML 74
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPicLPSSNYNVPAGTTCTVSGWGRTSEGAgsLPDTLQEVNVPIVSNATCRRAYSGGgaITDNML 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370475511   75 CAGDEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 130
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1-133 7.03e-57

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: 176.70  E-value: 7.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGD-FPDTIQCAYIHLVSREECEHAY--PGQITQNMLC 75
Cdd:cd00190    92 ALLKLKRPVTLSDNVRPicLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLC 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475511  76 AGDEKYGKDSCQGDSGGPLVCGDH----LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWIQKT 133
Cdd:cd00190   172 AGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-130 1.72e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 1.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   1 MLLRLARPAKLSELIQP--LPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGD 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPicLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370475511  79 ekYGKDSCQGDSGGPLVCGDH-LRGLVSWGNiPCGSKEKPGVYTNVCRYTNWI 130
Cdd:pfam00089 170 --GGKDACQGDSGGPLVCSDGeLIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2-134 8.88e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.91  E-value: 8.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475511   2 LLRLARPAKLselIQPLPL--ERDCSANTTSCHILGWGKTA--DGDFPDTIQCAYIHLVSREECEhAYPGQITQNMLCAG 77
Cdd:COG5640   123 LLKLATPVPG---VAPAPLatSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAG 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370475511  78 DEKYGKDSCQGDSGGPLV----CGDHLRGLVSWGNIPCGSKeKPGVYTNVCRYTNWIQKTI 134
Cdd:COG5640   199 YPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPGVYTRVSAYRDWIKSTA 258
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 87-123 1.04e-04

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: 39.98  E-value: 1.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1370475511  87 QGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNV 123
Cdd:cd21112   144 PGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 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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