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Conserved domains on  [gi|530415543|ref|XP_005258496|]
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kallikrein-11 isoform X3 [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 ...
 47-134 5.88e-43

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: 141.28  E-value: 5.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543    47 RLPHTLRCANITIIEHQKCENAYPGN--ITDTMVCASVQEGGKDSCQGDSGGPLVCNQS---LQGIISWGqDPCAITRKP 121
Cdd:smart00020 138 SLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKP 216

                           90
                   ....*....|...
gi 530415543   122 GVYTKVCKYVDWI 134
Cdd:smart00020 217 GVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 47-134 5.88e-43

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: 141.28  E-value: 5.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543    47 RLPHTLRCANITIIEHQKCENAYPGN--ITDTMVCASVQEGGKDSCQGDSGGPLVCNQS---LQGIISWGqDPCAITRKP 121
Cdd:smart00020 138 SLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKP 216

                           90
                   ....*....|...
gi 530415543   122 GVYTKVCKYVDWI 134
Cdd:smart00020 217 GVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 45-137 2.10e-42

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: 139.72  E-value: 2.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543  45 TVRLPHTLRCANITIIEHQKCENAY--PGNITDTMVCASVQEGGKDSCQGDSGGPLVCNQS----LQGIISWGQDpCAIT 118
Cdd:cd00190  135 GGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARP 213

                         90
                 ....*....|....*....
gi 530415543 119 RKPGVYTKVCKYVDWIQET 137
Cdd:cd00190  214 NYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
47-134 1.39e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 119.47  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543   47 RLPHTLRCANITIIEHQKCENAYPGNITDTMVCAsvQEGGKDSCQGDSGGPLVC-NQSLQGIISWGqDPCAITRKPGVYT 125
Cdd:pfam00089 134 GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA--GAGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYT 210


                  ....*....
gi 530415543  126 KVCKYVDWI 134
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 51-138 4.19e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 108.97  E-value: 4.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543  51 TLRCANITIIEHQKCeNAYPGNITDTMVCASVQEGGKDSCQGDSGGPLVCNQS----LQGIISWGQDPCAiTRKPGVYTK 126
Cdd:COG5640  169 TLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGggwvLVGVVSWGGGPCA-AGYPGVYTR 246

                         90
                 ....*....|..
gi 530415543 127 VCKYVDWIQETM 138
Cdd:COG5640  247 VSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 47-134 5.88e-43

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: 141.28  E-value: 5.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543    47 RLPHTLRCANITIIEHQKCENAYPGN--ITDTMVCASVQEGGKDSCQGDSGGPLVCNQS---LQGIISWGqDPCAITRKP 121
Cdd:smart00020 138 SLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWG-SGCARPGKP 216

                           90
                   ....*....|...
gi 530415543   122 GVYTKVCKYVDWI 134
Cdd:smart00020 217 GVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 45-137 2.10e-42

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: 139.72  E-value: 2.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543  45 TVRLPHTLRCANITIIEHQKCENAY--PGNITDTMVCASVQEGGKDSCQGDSGGPLVCNQS----LQGIISWGQDpCAIT 118
Cdd:cd00190  135 GGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARP 213

                         90
                 ....*....|....*....
gi 530415543 119 RKPGVYTKVCKYVDWIQET 137
Cdd:cd00190  214 NYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
47-134 1.39e-34

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 119.47  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543   47 RLPHTLRCANITIIEHQKCENAYPGNITDTMVCAsvQEGGKDSCQGDSGGPLVC-NQSLQGIISWGqDPCAITRKPGVYT 125
Cdd:pfam00089 134 GPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA--GAGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYT 210


                  ....*....
gi 530415543  126 KVCKYVDWI 134
Cdd:pfam00089 211 PVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 51-138 4.19e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 108.97  E-value: 4.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530415543  51 TLRCANITIIEHQKCeNAYPGNITDTMVCASVQEGGKDSCQGDSGGPLVCNQS----LQGIISWGQDPCAiTRKPGVYTK 126
Cdd:COG5640  169 TLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGggwvLVGVVSWGGGPCA-AGYPGVYTR 246

                         90
                 ....*....|..
gi 530415543 127 VCKYVDWIQETM 138
Cdd:COG5640  247 VSAYRDWIKSTA 258
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 71-127 2.91e-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: 36.13  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530415543  71 GNITDTMVCASVQEGG------KDSC--QGDSGGPLVCNQSLQGIISWGQDPCAITRKPGVYTKV 127
Cdd:cd21112  116 GTVTAVNVTVNYPGGTvtgltrTNACaePGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 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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