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Conserved domains on  [gi|1034608419|ref|XP_016882432|]
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kallikrein-15 isoform X4 [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 ...
25-120 2.71e-41

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: 136.25  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190     4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                          90       100
                  ....*....|....*....|.
gi 1034608419 100 ARSHRNDIMLLRLVQPARLNP 120
Cdd:cd00190    84 PSTYDNDIALLKLKRPVTLSD 104
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-120 2.71e-41

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: 136.25  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190     4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                          90       100
                  ....*....|....*....|.
gi 1034608419 100 ARSHRNDIMLLRLVQPARLNP 120
Cdd:cd00190    84 PSTYDNDIALLKLKRPVTLSD 104
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-120 1.50e-38

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: 128.95  E-value: 1.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419   25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100
                   ....*....|....*....|.
gi 1034608419  100 ARSHRNDIMLLRLVQPARLNP 120
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSD 104
Trypsin pfam00089
Trypsin;
25-120 4.05e-37

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 125.25  E-value: 4.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  25 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 101
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90
                  ....*....|....*....
gi 1034608419 102 SHRNDIMLLRLVQPARLNP 120
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGD 102
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-118 1.09e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 96.64  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  12 ASTAAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpe 84
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034608419  85 QLRTTSRVIPHPRYEARSHRNDIMLLRL------VQPARL 118
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLatpvpgVAPAPL 138
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-120 2.71e-41

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: 136.25  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:cd00190     4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                          90       100
                  ....*....|....*....|.
gi 1034608419 100 ARSHRNDIMLLRLVQPARLNP 120
Cdd:cd00190    84 PSTYDNDIALLKLKRPVTLSD 104
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-120 1.50e-38

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: 128.95  E-value: 1.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419   25 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 99
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100
                   ....*....|....*....|.
gi 1034608419  100 ARSHRNDIMLLRLVQPARLNP 120
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSD 104
Trypsin pfam00089
Trypsin;
25-120 4.05e-37

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 125.25  E-value: 4.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  25 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 101
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90
                  ....*....|....*....
gi 1034608419 102 SHRNDIMLLRLVQPARLNP 120
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGD 102
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-118 1.09e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 96.64  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  12 ASTAAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpe 84
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034608419  85 QLRTTSRVIPHPRYEARSHRNDIMLLRL------VQPARL 118
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLatpvpgVAPAPL 138
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-115 4.36e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.12  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608419  42 RGRFNCGASLISPHWVLSAAHC--------QSRFMRVRLGEHNlrkrdGPEQLRTTSRVIPHPRYEARSH-RNDIMLLRL 112
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDaGYDYALLRL 83

                  ...
gi 1034608419 113 VQP 115
Cdd:COG3591    84 DEP 86
 
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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