NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|768009860|ref|XP_011525390|]
View 

kallikrein-15 isoform X3 [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

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 cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-151 1.96e-50

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: 161.29  E-value: 1.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768009860 100 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 151
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGP 137
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-151 1.96e-50

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: 161.29  E-value: 1.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768009860 100 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 151
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-151 3.24e-47

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: 152.83  E-value: 3.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860    25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 768009860   100 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEP 151
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG 137
Trypsin pfam00089
Trypsin;
25-151 3.39e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 3.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860   25 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 101
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768009860  102 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 151
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-155 5.39e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.04  E-value: 5.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  12 ASTAAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpe 84
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768009860  85 QLRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPGTAG 155
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSG 168
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-151 1.96e-50

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: 161.29  E-value: 1.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768009860 100 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 151
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-151 3.24e-47

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: 152.83  E-value: 3.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860    25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 768009860   100 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEP 151
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG 137
Trypsin pfam00089
Trypsin;
25-151 3.39e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 3.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860   25 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 101
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768009860  102 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 151
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-155 5.39e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 107.04  E-value: 5.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  12 ASTAAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpe 84
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768009860  85 QLRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPGTAG 155
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSG 168
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
34-133 4.12e-04

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.91  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860   34 PWQVALYERGRFNCGASLISPHWVLSAAHC------QSRFMRVRLGEH-NLRKRDGP-EQLRttsrviphpRYEARSH-- 103
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSClrdtnlRHQYISVVLGGAkTLKSIEGPyEQIV---------RVDCRHDip 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 768009860  104 RNDIMLLRLVQPARLNPQVRPAVLPTRCPH 133
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNE 102
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-157 6.49e-04

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.50  E-value: 6.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009860  42 RGRFNCGASLISPHWVLSAAHC--------QSRFMRVRLGEHNlrkrdGPEQLRTTSRVIPHPRYEARSH-RNDIMLLRL 112
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDaGYDYALLRL 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768009860 113 vqPARLNPQVRPavLPTRCP-------------HPG---------EACVVSGW--GLVSHN---EPGTAGSP 157
Cdd:COG3591   84 --DEPLGDTTGW--LGLAFNdaplagepvtiigYPGdrpkdlsldCSGRVTGVqgNRLSYDcdtTGGSSGSP 151
 
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