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Conserved domains on  [gi|2117768244|ref|XP_044271010|]
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chymotrypsin-1-like isoform X2 [Tribolium madens]

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 ...
60-250 1.73e-38

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: 134.33  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  60 VFLNNPTTNKFCVGTLITNDTILTAAHCI--SDANEISILLGINDLTDN---GVQLESSEFAVHKNFTNNTtpYNHDIGL 134
Cdd:cd00190    16 VSLQYTGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNeggGQVIKVKKVIVHPNYNPST--YDNDIAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 135 IFLSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNND-FNDKLLE---KLVSlKEECFL----------SNICA 199
Cdd:cd00190    94 LKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGpLPDVLQEvnvPIVS-NAECKRaysyggtitdNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 200 FGENG---PYKGDSGGPLNCES----TQIGIVSGGD--EDNDGLSIYTDVGSYNKWIDDQ 250
Cdd:cd00190   173 GGLEGgkdACQGDSGGPLVCNDngrgVLVGIVSWGSgcARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
60-250 1.73e-38

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: 134.33  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  60 VFLNNPTTNKFCVGTLITNDTILTAAHCI--SDANEISILLGINDLTDN---GVQLESSEFAVHKNFTNNTtpYNHDIGL 134
Cdd:cd00190    16 VSLQYTGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNeggGQVIKVKKVIVHPNYNPST--YDNDIAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 135 IFLSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNND-FNDKLLE---KLVSlKEECFL----------SNICA 199
Cdd:cd00190    94 LKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGpLPDVLQEvnvPIVS-NAECKRaysyggtitdNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 200 FGENG---PYKGDSGGPLNCES----TQIGIVSGGD--EDNDGLSIYTDVGSYNKWIDDQ 250
Cdd:cd00190   173 GGLEGgkdACQGDSGGPLVCNDngrgVLVGIVSWGSgcARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
60-247 1.34e-36

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: 129.33  E-value: 1.34e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244   60 VFLNNPTTNKFCVGTLITNDTILTAAHCI--SDANEISILLGINDLT--DNGVQLESSEFAVHKNFtnNTTPYNHDIGLI 135
Cdd:smart00020  17 VSLQYGGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSsgEEGQVIKVSKVIIHPNY--NPSTYDNDIALL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  136 FLSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNND--FNDKLLE---KLVSlKEEC----------FLSNICA 199
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgRTSEGAgsLPDTLQEvnvPIVS-NATCrraysgggaiTDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117768244  200 FGENG---PYKGDSGGPLNCES---TQIGIVSGGD--EDNDGLSIYTDVGSYNKWI 247
Cdd:smart00020 174 GGLEGgkdACQGDSGGPLVCNDgrwVLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
60-247 1.07e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  60 VFLNNPTTNKFCVGTLITNDTILTAAHCISDANEISILLGINDL--TDNGVQ-LESSEFAVHKNFTNNTTpyNHDIGLIF 136
Cdd:pfam00089  16 VSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIvlREGGEQkFDVEKIIVHPNYNPDTL--DNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 137 LSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNNDFNDKLLEKLVSL--KEECFLSN--------ICA-FGENG 204
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWgNTKTLGPSDTLQEVTVPVvsRETCRSAYggtvtdtmICAgAGGKD 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2117768244 205 PYKGDSGGPLNCES-TQIGIVSGGDEDNDGL--SIYTDVGSYNKWI 247
Cdd:pfam00089 174 ACQGDSGGPLVCSDgELIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-251 4.50e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 113.21  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  70 FCVGTLITNDTILTAAHCISD--ANEISILLGINDL-TDNGVQLESSEFAVHKNFTNNTtpYNHDIGLIFLSQSIilnDK 146
Cdd:COG5640    58 FCGGTLIAPRWVLTAAHCVDGdgPSDLRVVIGSTDLsTSGGTVVKVARIVVHPDYDPAT--PGNDIALLKLATPV---PG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 147 INTVALSNNPFFYTYEKSCFTLGW-ATSNND--FNDKLLE---KLVSLkEECFL-------SNICAFGENG---PYKGDS 210
Cdd:COG5640   133 VAPAPLATSADAAAPGTPATVAGWgRTSEGPgsQSGTLRKadvPVVSD-ATCAAyggfdggTMLCAGYPEGgkdACQGDS 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2117768244 211 GGPL----NCESTQIGIVSGGDED--NDGLSIYTDVGSYNKWIDDQI 251
Cdd:COG5640   212 GGPLvvkdGGGWVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
60-250 1.73e-38

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: 134.33  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  60 VFLNNPTTNKFCVGTLITNDTILTAAHCI--SDANEISILLGINDLTDN---GVQLESSEFAVHKNFTNNTtpYNHDIGL 134
Cdd:cd00190    16 VSLQYTGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNeggGQVIKVKKVIVHPNYNPST--YDNDIAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 135 IFLSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNND-FNDKLLE---KLVSlKEECFL----------SNICA 199
Cdd:cd00190    94 LKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGpLPDVLQEvnvPIVS-NAECKRaysyggtitdNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 200 FGENG---PYKGDSGGPLNCES----TQIGIVSGGD--EDNDGLSIYTDVGSYNKWIDDQ 250
Cdd:cd00190   173 GGLEGgkdACQGDSGGPLVCNDngrgVLVGIVSWGSgcARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
60-247 1.34e-36

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: 129.33  E-value: 1.34e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244   60 VFLNNPTTNKFCVGTLITNDTILTAAHCI--SDANEISILLGINDLT--DNGVQLESSEFAVHKNFtnNTTPYNHDIGLI 135
Cdd:smart00020  17 VSLQYGGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSsgEEGQVIKVSKVIIHPNY--NPSTYDNDIALL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  136 FLSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNND--FNDKLLE---KLVSlKEEC----------FLSNICA 199
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgRTSEGAgsLPDTLQEvnvPIVS-NATCrraysgggaiTDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117768244  200 FGENG---PYKGDSGGPLNCES---TQIGIVSGGD--EDNDGLSIYTDVGSYNKWI 247
Cdd:smart00020 174 GGLEGgkdACQGDSGGPLVCNDgrwVLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
60-247 1.07e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  60 VFLNNPTTNKFCVGTLITNDTILTAAHCISDANEISILLGINDL--TDNGVQ-LESSEFAVHKNFTNNTTpyNHDIGLIF 136
Cdd:pfam00089  16 VSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIvlREGGEQkFDVEKIIVHPNYNPDTL--DNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 137 LSQSIILNDKINTVALSNNPFFYTYEKSCFTLGW-ATSNNDFNDKLLEKLVSL--KEECFLSN--------ICA-FGENG 204
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWgNTKTLGPSDTLQEVTVPVvsRETCRSAYggtvtdtmICAgAGGKD 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2117768244 205 PYKGDSGGPLNCES-TQIGIVSGGDEDNDGL--SIYTDVGSYNKWI 247
Cdd:pfam00089 174 ACQGDSGGPLVCSDgELIGIVSWGYGCASGNypGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-251 4.50e-30

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 113.21  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  70 FCVGTLITNDTILTAAHCISD--ANEISILLGINDL-TDNGVQLESSEFAVHKNFTNNTtpYNHDIGLIFLSQSIilnDK 146
Cdd:COG5640    58 FCGGTLIAPRWVLTAAHCVDGdgPSDLRVVIGSTDLsTSGGTVVKVARIVVHPDYDPAT--PGNDIALLKLATPV---PG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 147 INTVALSNNPFFYTYEKSCFTLGW-ATSNND--FNDKLLE---KLVSLkEECFL-------SNICAFGENG---PYKGDS 210
Cdd:COG5640   133 VAPAPLATSADAAAPGTPATVAGWgRTSEGPgsQSGTLRKadvPVVSD-ATCAAyggfdggTMLCAGYPEGgkdACQGDS 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2117768244 211 GGPL----NCESTQIGIVSGGDED--NDGLSIYTDVGSYNKWIDDQI 251
Cdd:COG5640   212 GGPLvvkdGGGWVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
59-240 1.22e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.39  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  59 VVFLNNPTTNKFCVGTLITNDTILTAAHCISD------ANEISILLGINDLTDNGVQleSSEFAVHKNFTNNTTPyNHDI 132
Cdd:COG3591     2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwATNIVFVPGYNGGPYGTAT--ATRFRVPPGWVASGDA-GYDY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244 133 GLIFLSQSIILNDKINTVALSNNPffyTYEKSCFTLGWAtsnndfNDKLleKLVSLKEECFLSNI--------CAFgeng 204
Cdd:COG3591    79 ALLRLDEPLGDTTGWLGLAFNDAP---LAGEPVTIIGYP------GDRP--KDLSLDCSGRVTGVqgnrlsydCDT---- 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2117768244 205 pYKGDSGGPL----NCESTQIGIVSGGDED--NDGLSIYTDV 240
Cdd:COG3591   144 -TGGSSGSPVlddsDGGGRVVGVHSAGGADraNTGVRLTSAI 184
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
73-214 8.25e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 35.86  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117768244  73 GTLITND-TILTAAHCISDANEISILLgINDLTDNGVQLESSEFAVHKnftnnttpyNHDIGLIFLSQSiilNDKINTVA 151
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVEL-VSVVLADGREYPATVVARDP---------DLDLALLRVSGD---GRGLPPLP 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117768244 152 LSNNPFFYtYEKSCFTLGWATSNNDFND------KLLEKLVSLKEECFLSNICAfgengPYKGDSGGPL 214
Cdd:pfam13365  70 LGDSEPLV-GGERVYAVGYPLGGEKLSLsegivsGVDEGRDGGDDGRVIQTDAA-----LSPGSSGGPV 132
 
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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