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Conserved domains on  [gi|13374559|ref|NP_075671|]
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chymotrypsin-like protease CTRL-1 precursor [Mus musculus]

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 ...
34-260 4.49e-100

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: 291.49  E-value: 4.49e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  34 IVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSNAEPVQVLSIARAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 112 NWNANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNvTPARLQQVVLPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13374559 192 --GARITDAMICAGGS--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCN-IQAPAMYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCArPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-260 4.49e-100

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: 291.49  E-value: 4.49e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  34 IVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSNAEPVQVLSIARAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 112 NWNANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNvTPARLQQVVLPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13374559 192 --GARITDAMICAGGS--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCN-IQAPAMYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCArPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 4.86e-98

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: 286.50  E-value: 4.86e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559     33 RIVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSNaEPVQVLSIARAITH 110
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559    111 PNWNANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNVTPARLQQVVLPLVTVNQCRQY 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13374559    191 WGAR--ITDAMICAGGS--GASSCQGDSGGPLVCQkGNTWVLIGIVSWGTKNCNIQAPAMYTRVSKFSTWI 257
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-257 8.04e-81

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.35  E-value: 8.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559    34 IVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHCQVTPGRHFVVLGEYDRSSNAEPVQVLSIARAITHPNW 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559   114 NANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGnvTPARLQQVVLPLVTVNQCRQYWGA 193
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13374559   194 RITDAMICAGGSGASSCQGDSGGPLVCQKGntwVLIGIVSWGTKNCNIQAPAMYTRVSKFSTWI 257
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
20-262 2.50e-80

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 242.63  E-value: 2.50e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  20 GVPAITPAlsynQRIVNGENAVPGSWPWQVSLQDNTGF--HFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSN 95
Cdd:COG5640  21 AAPAADAA----PAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvdGDGPSDLRVVIGSTDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  96 AEpvQVLSIARAITHPNWNANTMNNDLTLLKLASPArytAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNVTPARLQ 175
Cdd:COG5640  97 GG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 176 QVVLPLVTVNQCRQYWGArITDAMICAGGS--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNIQAPAMYTRVSKF 253
Cdd:COG5640 172 KADVPVVSDATCAAYGGF-DGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                ....*....
gi 13374559 254 STWINQVMA 262
Cdd:COG5640 251 RDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-260 4.49e-100

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: 291.49  E-value: 4.49e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  34 IVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSNAEPVQVLSIARAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 112 NWNANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNvTPARLQQVVLPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13374559 192 --GARITDAMICAGGS--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCN-IQAPAMYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCArPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 4.86e-98

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: 286.50  E-value: 4.86e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559     33 RIVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSNaEPVQVLSIARAITH 110
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559    111 PNWNANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNVTPARLQQVVLPLVTVNQCRQY 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13374559    191 WGAR--ITDAMICAGGS--GASSCQGDSGGPLVCQkGNTWVLIGIVSWGTKNCNIQAPAMYTRVSKFSTWI 257
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-257 8.04e-81

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.35  E-value: 8.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559    34 IVNGENAVPGSWPWQVSLQDNTGFHFCGGSLISPNWVVTAAHCQVTPGRHFVVLGEYDRSSNAEPVQVLSIARAITHPNW 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559   114 NANTMNNDLTLLKLASPARYTAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGnvTPARLQQVVLPLVTVNQCRQYWGA 193
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13374559   194 RITDAMICAGGSGASSCQGDSGGPLVCQKGntwVLIGIVSWGTKNCNIQAPAMYTRVSKFSTWI 257
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
20-262 2.50e-80

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 242.63  E-value: 2.50e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  20 GVPAITPAlsynQRIVNGENAVPGSWPWQVSLQDNTGF--HFCGGSLISPNWVVTAAHC--QVTPGRHFVVLGEYDRSSN 95
Cdd:COG5640  21 AAPAADAA----PAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvdGDGPSDLRVVIGSTDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  96 AEpvQVLSIARAITHPNWNANTMNNDLTLLKLASPArytAQVSPVCLASTNEALPSGLTCVTTGWGRISGVGNVTPARLQ 175
Cdd:COG5640  97 GG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 176 QVVLPLVTVNQCRQYWGArITDAMICAGGS--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNIQAPAMYTRVSKF 253
Cdd:COG5640 172 KADVPVVSDATCAAYGGF-DGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                ....*....
gi 13374559 254 STWINQVMA 262
Cdd:COG5640 251 RDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-250 3.20e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.24  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559  51 LQDNTGFHFCGGSLISPNWVVTAAHCQVTPGR-------HFVVlgeydrSSNAEPVQVLSIARAITHPNWNANTM-NNDL 122
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwatniVFVP------GYNGGPYGTATATRFRVPPGWVASGDaGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559 123 TLLKLASPARYTAQVSPVclaSTNEALPSGLTCVTTGWgrisgvgnvtparlqqvvlPLVTVNQCRQYWGARITDAmicA 202
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGL---AFNDAPLAGEPVTIIGY-------------------PGDRPKDLSLDCSGRVTGV---Q 133
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 13374559 203 GGS---GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNIQAPAMYTRV 250
Cdd:COG3591 134 GNRlsyDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRLTSAI 184
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
62-231 2.24e-04

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 40.48  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559    62 GSLISPN-WVVTAAHCqVTPGRHFVVLGEYDRSSNAEPVQVLSIARaithpnwnanTMNNDLTLLKLASPARytaQVSPV 140
Cdd:pfam13365   3 GFVVSSDgLVLTNAHV-VDDAEEAAVELVSVVLADGREYPATVVAR----------DPDLDLALLRVSGDGR---GLPPL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13374559   141 CLASTNEALPsGLTCVTTGWGRISGVGNVTPARLQQVvlplvTVNQCRQYWGARITDAMICAGGSgasscqgdSGGPLVC 220
Cdd:pfam13365  69 PLGDSEPLVG-GERVYAVGYPLGGEKLSLSEGIVSGV-----DEGRDGGDDGRVIQTDAALSPGS--------SGGPVFD 134
                         170
                  ....*....|.
gi 13374559   221 QKGNtwvLIGI 231
Cdd:pfam13365 135 ADGR---VVGI 142
 
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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