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Conserved domains on  [gi|1625649079|ref|NP_001357055|]
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kallikrein-12 isoform 4 [Homo sapiens]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 37-126 1.33e-30

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.


The actual alignment was detected with superfamily member smart00020:

Pssm-ID: 473915  Cd Length: 229  Bit Score: 109.69  E-value: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90
                   ....*....|....*.
gi 1625649079  111 PCGQDGIPGVYTYICN 126
Cdd:smart00020 209 GCARPGKPGVYTRVSS 224
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 37-126 1.33e-30

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: 109.69  E-value: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90
                   ....*....|....*.
gi 1625649079  111 PCGQDGIPGVYTYICN 126
Cdd:smart00020 209 GCARPGKPGVYTRVSS 224
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 38-126 3.46e-29

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: 106.21  E-value: 3.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  38 LTAAADPFPDLLQCLNLSIVSHATCHGVY--PGRITSNMVCAGG-VPGQDACQGDSGGPLVCG----GVLQGLVSWGSVg 110
Cdd:cd00190   131 RTSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG- 209

                          90
                  ....*....|....*.
gi 1625649079 111 pCGQDGIPGVYTYICN 126
Cdd:cd00190   210 -CARPNYPGVYTRVSS 224
Trypsin pfam00089
Trypsin;
45-126 2.16e-25

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 95.97  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  45 FPDLLQCLNLSIVSHATCHGVYPGRITSNMVCAGGVpGQDACQGDSGGPLVC-GGVLQGLVSWGsvGPCGQDGIPGVYTY 123
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWG--YGCASGNYPGVYTP 211


                  ...
gi 1625649079 124 ICN 126
Cdd:pfam00089 212 VSS 214
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 37-122 2.66e-18

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 78.15  E-value: 2.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  37 RLTAAADPFPDLLQCLNLSIVSHATChGVYPGRITSNMVCAGGV-PGQDACQGDSGGPLV----CGGVLQGLVSWGSvGP 111
Cdd:COG5640   158 RTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPeGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG-GP 235

                          90
                  ....*....|.
gi 1625649079 112 CGqDGIPGVYT 122
Cdd:COG5640   236 CA-AGYPGVYT 245
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 37-126 1.33e-30

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: 109.69  E-value: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079   37 RLTAAADPFPDLLQCLNLSIVSHATCHGVYPGR--ITSNMVCAGGVP-GQDACQGDSGGPLVCG---GVLQGLVSWGSvg 110
Cdd:smart00020 131 RTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEgGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-- 208

                           90
                   ....*....|....*.
gi 1625649079  111 PCGQDGIPGVYTYICN 126
Cdd:smart00020 209 GCARPGKPGVYTRVSS 224
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 38-126 3.46e-29

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: 106.21  E-value: 3.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  38 LTAAADPFPDLLQCLNLSIVSHATCHGVY--PGRITSNMVCAGG-VPGQDACQGDSGGPLVCG----GVLQGLVSWGSVg 110
Cdd:cd00190   131 RTSEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG- 209

                          90
                  ....*....|....*.
gi 1625649079 111 pCGQDGIPGVYTYICN 126
Cdd:cd00190   210 -CARPNYPGVYTRVSS 224
Trypsin pfam00089
Trypsin;
45-126 2.16e-25

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 95.97  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  45 FPDLLQCLNLSIVSHATCHGVYPGRITSNMVCAGGVpGQDACQGDSGGPLVC-GGVLQGLVSWGsvGPCGQDGIPGVYTY 123
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWG--YGCASGNYPGVYTP 211


                  ...
gi 1625649079 124 ICN 126
Cdd:pfam00089 212 VSS 214
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 37-122 2.66e-18

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 78.15  E-value: 2.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649079  37 RLTAAADPFPDLLQCLNLSIVSHATChGVYPGRITSNMVCAGGV-PGQDACQGDSGGPLV----CGGVLQGLVSWGSvGP 111
Cdd:COG5640   158 RTSEGPGSQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPeGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG-GP 235

                          90
                  ....*....|.
gi 1625649079 112 CGqDGIPGVYT 122
Cdd:COG5640   236 CA-AGYPGVYT 245
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 84-122 9.61e-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: 34.59  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1625649079  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.
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