NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1625648995|ref|NP_665902|]
View 

kallikrein-12 isoform 3 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 37-131 7.07e-36

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: 123.17  E-value: 7.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90       100
                   ....*....|....*....|.
gi 1625648995  111 PCGQDGIPGVYTYICKYVDWI 131
Cdd:smart00020 209 GCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 37-131 7.07e-36

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: 123.17  E-value: 7.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90       100
                   ....*....|....*....|.
gi 1625648995  111 PCGQDGIPGVYTYICKYVDWI 131
Cdd:smart00020 209 GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 38-134 2.70e-35

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: 121.61  E-value: 2.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  38 LTAAADPFPDLLQCLNLSIVSHATCHGVY--PGRITSNMVCAGG-VPGQDACQGDSGGPLVCG----GVLQGLVSWGSVg 110
Cdd:cd00190   131 RTSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG- 209

                          90       100
                  ....*....|....*....|....
gi 1625648995 111 pCGQDGIPGVYTYICKYVDWIRMI 134
Cdd:cd00190   210 -CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
45-131 5.60e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 107.53  E-value: 5.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  45 FPDLLQCLNLSIVSHATCHGVYPGRITSNMVCAGGVpGQDACQGDSGGPLVC-GGVLQGLVSWGsvGPCGQDGIPGVYTY 123
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWG--YGCASGNYPGVYTP 211


                  ....*...
gi 1625648995 124 ICKYVDWI 131
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 37-132 1.26e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 86.63  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  37 RLTAAADPFPDLLQCLNLSIVSHATChGVYPGRITSNMVCAGGV-PGQDACQGDSGGPLV----CGGVLQGLVSWGSvGP 111
Cdd:COG5640   158 RTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPeGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG-GP 235

                          90       100
                  ....*....|....*....|.
gi 1625648995 112 CGqDGIPGVYTYICKYVDWIR 132
Cdd:COG5640   236 CA-AGYPGVYTRVSAYRDWIK 255
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 37-131 7.07e-36

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: 123.17  E-value: 7.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90       100
                   ....*....|....*....|.
gi 1625648995  111 PCGQDGIPGVYTYICKYVDWI 131
Cdd:smart00020 209 GCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 38-134 2.70e-35

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: 121.61  E-value: 2.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  38 LTAAADPFPDLLQCLNLSIVSHATCHGVY--PGRITSNMVCAGG-VPGQDACQGDSGGPLVCG----GVLQGLVSWGSVg 110
Cdd:cd00190   131 RTSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG- 209

                          90       100
                  ....*....|....*....|....
gi 1625648995 111 pCGQDGIPGVYTYICKYVDWIRMI 134
Cdd:cd00190   210 -CARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
45-131 5.60e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 107.53  E-value: 5.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  45 FPDLLQCLNLSIVSHATCHGVYPGRITSNMVCAGGVpGQDACQGDSGGPLVC-GGVLQGLVSWGsvGPCGQDGIPGVYTY 123
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWG--YGCASGNYPGVYTP 211


                  ....*...
gi 1625648995 124 ICKYVDWI 131
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 37-132 1.26e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 86.63  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625648995  37 RLTAAADPFPDLLQCLNLSIVSHATChGVYPGRITSNMVCAGGV-PGQDACQGDSGGPLV----CGGVLQGLVSWGSvGP 111
Cdd:COG5640   158 RTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPeGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG-GP 235

                          90       100
                  ....*....|....*....|.
gi 1625648995 112 CGqDGIPGVYTYICKYVDWIR 132
Cdd:COG5640   236 CA-AGYPGVYTRVSAYRDWIK 255
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 84-122 3.22e-03

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: 35.74  E-value: 3.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1625648995  84 DAC--QGDSGGPLVCGGVLQGLVSwGSVGPCGQDGIPGVYT 122
Cdd:cd21112   139 NACaePGDSGGPVFSGTQALGITS-GGSGNCGSGGGTSYFQ 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH