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Conserved domains on  [gi|1148299638|gb|AQR57583|]
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kallikrein-related peptidase 6 transcript variant 9 [Homo sapiens]

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 ...
 6-131 4.31e-42

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: 138.96  E-value: 4.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638    6 TRHLTPTKLPST-----PRATCSVVGSlsihcGSSQLPtakNRDFPDTIQCAYIHLVSREECEHAYPGQ--ITQNMLCAG 78
Cdd:smart00020 103 SDNVRPICLPSSnynvpAGTTCTVSGW-----GRTSEG---AGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAG 174

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148299638   79 DEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 131
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 6-131 4.31e-42

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: 138.96  E-value: 4.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638    6 TRHLTPTKLPST-----PRATCSVVGSlsihcGSSQLPtakNRDFPDTIQCAYIHLVSREECEHAYPGQ--ITQNMLCAG 78
Cdd:smart00020 103 SDNVRPICLPSSnynvpAGTTCTVSGW-----GRTSEG---AGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAG 174

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148299638   79 DEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 131
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 6-134 4.04e-41

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: 136.64  E-value: 4.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638   6 TRHLTPTKLPST-----PRATCSVVGSlsihcGSsqlpTAKNRDFPDTIQCAYIHLVSREECEHAY--PGQITQNMLCAG 78
Cdd:cd00190   103 SDNVRPICLPSSgynlpAGTTCTVSGW-----GR----TSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAG 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  79 DEKYGKDSCQGDSGGPLVCGDH----LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWIQKT 134
Cdd:cd00190   174 GLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
18-131 2.71e-33

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 116.00  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  18 PRATCSVVGSlsihcgssqlPTAKNRDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDekYGKDSCQGDSGGPLVC 97
Cdd:pfam00089 118 VGTTCTVSGW----------GNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC 185

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1148299638  98 GDH-LRGLVSWGNiPCGSKEKPGVYTNVCRYTNWI 131
Cdd:pfam00089 186 SDGeLIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 44-135 9.37e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 95.10  E-value: 9.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  44 DFPDTIQCAYIHLVSREECEhAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLV----CGDHLRGLVSWGNIPCGSKeKPG 119
Cdd:COG5640   165 SQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPG 242

                          90
                  ....*....|....*.
gi 1148299638 120 VYTNVCRYTNWIQKTI 135
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 6-131 4.31e-42

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: 138.96  E-value: 4.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638    6 TRHLTPTKLPST-----PRATCSVVGSlsihcGSSQLPtakNRDFPDTIQCAYIHLVSREECEHAYPGQ--ITQNMLCAG 78
Cdd:smart00020 103 SDNVRPICLPSSnynvpAGTTCTVSGW-----GRTSEG---AGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAG 174

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148299638   79 DEKYGKDSCQGDSGGPLVCGDH---LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWI 131
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 6-134 4.04e-41

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: 136.64  E-value: 4.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638   6 TRHLTPTKLPST-----PRATCSVVGSlsihcGSsqlpTAKNRDFPDTIQCAYIHLVSREECEHAY--PGQITQNMLCAG 78
Cdd:cd00190   103 SDNVRPICLPSSgynlpAGTTCTVSGW-----GR----TSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAG 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  79 DEKYGKDSCQGDSGGPLVCGDH----LRGLVSWGnIPCGSKEKPGVYTNVCRYTNWIQKT 134
Cdd:cd00190   174 GLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
18-131 2.71e-33

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 116.00  E-value: 2.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  18 PRATCSVVGSlsihcgssqlPTAKNRDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDekYGKDSCQGDSGGPLVC 97
Cdd:pfam00089 118 VGTTCTVSGW----------GNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC 185

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1148299638  98 GDH-LRGLVSWGNiPCGSKEKPGVYTNVCRYTNWI 131
Cdd:pfam00089 186 SDGeLIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 44-135 9.37e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 95.10  E-value: 9.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148299638  44 DFPDTIQCAYIHLVSREECEhAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLV----CGDHLRGLVSWGNIPCGSKeKPG 119
Cdd:COG5640   165 SQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPG 242

                          90
                  ....*....|....*.
gi 1148299638 120 VYTNVCRYTNWIQKTI 135
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 88-124 3.09e-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: 38.83  E-value: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1148299638  88 QGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNV 124
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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