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Conserved domains on  [gi|459212750|ref|NP_001264011|]
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kallikrein-15 isoform 6 preproprotein [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

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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 ...
24-150 2.11e-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: 2.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 459212750  99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 150
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 ...
24-150 2.11e-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: 2.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 459212750  99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 150
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-150 3.41e-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: 3.41e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750    24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 459212750    99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEP 150
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG 137
Trypsin pfam00089
Trypsin;
24-150 3.42e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 3.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750   24 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 100
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 459212750  101 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 150
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-154 1.95e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.50  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  12 ASTAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpeQ 84
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--T 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 459212750  85 LRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPGTAG 154
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSG 168
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-150 2.11e-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: 2.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 459212750  99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 150
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-150 3.41e-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: 3.41e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750    24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 459212750    99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEP 150
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG 137
Trypsin pfam00089
Trypsin;
24-150 3.42e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 3.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750   24 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 100
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 459212750  101 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEP 150
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-154 1.95e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.50  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  12 ASTAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpeQ 84
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--T 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 459212750  85 LRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPGTAG 154
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSG 168
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
33-132 4.72e-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: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750   33 PWQVALYERGRFNCGASLISPHWVLSAAHC------QSRFMRVRLGEH-NLRKRDGP-EQLRttsrviphpRYEARSH-- 102
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSClrdtnlRHQYISVVLGGAkTLKSIEGPyEQIV---------RVDCRHDip 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 459212750  103 RNDIMLLRLVQPARLNPQVRPAVLPTRCPH 132
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNE 102
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-156 5.42e-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: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212750  41 RGRFNCGASLISPHWVLSAAHC--------QSRFMRVRLGEHNlrkrdGPEQLRTTSRVIPHPRYEARSH-RNDIMLLRL 111
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDaGYDYALLRL 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 459212750 112 vqPARLNPQVRPavLPTRCP-------------HPG---------EACVVSGW--GLVSHN---EPGTAGSP 156
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.
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