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Conserved domains on  [gi|767902044|ref|XP_011538852|]
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chymotrypsin-C isoform X1 [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
30-173 2.41e-53

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: 173.23  E-value: 2.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902044 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWRGLRWPTEL 173
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL 142
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-173 2.41e-53

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: 173.23  E-value: 2.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902044 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWRGLRWPTEL 173
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL 142
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-163 3.56e-51

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: 167.47  E-value: 3.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044    29 RVVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISN--TRTYRVAVGKNNLEVEDEEgsLFVGVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767902044   107 IHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRL 163
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT 132
Trypsin pfam00089
Trypsin;
30-166 5.62e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 146.05  E-value: 5.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044   30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVeDEEGSLFVGVDTIHV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767902044  110 HKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWRG 166
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL 133
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-166 1.00e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.52  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044   1 MLGITVLAALLACASSCGVPSFPPN-LSARVVGGEDARPHSWPWQISLQYlKNDTWRHTCGGTLIASNFVLTAAHCISNT 79
Cdd:COG5640    1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  80 R--TYRVAVGKNNLEVEDEEgslFVGVDTIHVHKRWNALLLRNDIALIKLAEHVelsDTIQVACLPEKDSLLPKDYPCYV 157
Cdd:COG5640   80 GpsDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATV 153

                 ....*....
gi 767902044 158 TGWGRLWRG 166
Cdd:COG5640  154 AGWGRTSEG 162
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-173 2.41e-53

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: 173.23  E-value: 2.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902044 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWRGLRWPTEL 173
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL 142
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-163 3.56e-51

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: 167.47  E-value: 3.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044    29 RVVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISN--TRTYRVAVGKNNLEVEDEEgsLFVGVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767902044   107 IHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRL 163
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT 132
Trypsin pfam00089
Trypsin;
30-166 5.62e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 146.05  E-value: 5.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044   30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVeDEEGSLFVGVDTIHV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767902044  110 HKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWRG 166
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL 133
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-166 1.00e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.52  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044   1 MLGITVLAALLACASSCGVPSFPPN-LSARVVGGEDARPHSWPWQISLQYlKNDTWRHTCGGTLIASNFVLTAAHCISNT 79
Cdd:COG5640    1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  80 R--TYRVAVGKNNLEVEDEEgslFVGVDTIHVHKRWNALLLRNDIALIKLAEHVelsDTIQVACLPEKDSLLPKDYPCYV 157
Cdd:COG5640   80 GpsDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATV 153

                 ....*....
gi 767902044 158 TGWGRLWRG 166
Cdd:COG5640  154 AGWGRTSEG 162
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-131 1.89e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 47.36  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902044  49 YLKNDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVgknNLEVE---DEEGSLFVGVDTIHVHKRW-NALLLRNDIAL 124
Cdd:COG3591    4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAT---NIVFVpgyNGGPYGTATATRFRVPPGWvASGDAGYDYAL 80

                 ....*..
gi 767902044 125 IKLAEHV 131
Cdd:COG3591   81 LRLDEPL 87
 
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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