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Conserved domains on  [gi|110625928|ref|NP_683742|]
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serine protease 44 precursor [Mus musculus]

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

 Zoom to residue level

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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 ...
112-340 4.40e-93

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: 278.01  E-value: 4.40e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 112 IVGGRPAPARKWPWQVSLQVHK-QHICGGSLISKWWVITAAHCVYG--HLDYAVFMGDADL--WSKRPVRIPVQDIIVHQ 186
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLssNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 187 DFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIELNIIRHEKCNQIL 266
Cdd:cd00190   81 NYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625928 267 KDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:cd00190  160 SYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
112-340 4.40e-93

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: 278.01  E-value: 4.40e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 112 IVGGRPAPARKWPWQVSLQVHK-QHICGGSLISKWWVITAAHCVYG--HLDYAVFMGDADL--WSKRPVRIPVQDIIVHQ 186
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLssNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 187 DFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIELNIIRHEKCNQIL 266
Cdd:cd00190   81 NYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625928 267 KDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:cd00190  160 SYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
111-340 1.05e-89

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: 269.16  E-value: 1.05e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928   111 RIVGGRPAPARKWPWQVSLQVHK-QHICGGSLISKWWVITAAHCVYG--HLDYAVFMGDADL-WSKRPVRIPVQDIIVHQ 186
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLsSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928   187 DFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKV-LEQGRSSRILQEIELNIIRHEKCNQI 265
Cdd:smart00020  81 NYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625928   266 LKDImgnifTLVQEGGVC-GYNEKGGDACQGDSGGPLVCEfNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:smart00020 160 YSGG-----GAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
112-340 1.62e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928  112 IVGGRPAPARKWPWQVSLQV-HKQHICGGSLISKWWVITAAHCVYGHLDYAVFMGDADL--WSKRPVRIPVQDIIVHQDF 188
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIvlREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928  189 SMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSrILQEIELNIIRHEKCNQilkd 268
Cdd:pfam00089  81 NP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRS---- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625928  269 imgNIFTLVQEGGVCGYnEKGGDACQGDSGGPLVCEFNKtwvQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:pfam00089 155 ---AYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
109-340 2.66e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 221.06  E-value: 2.66e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 109 TARIVGGRPAPARKWPWQVSLQV---HKQHICGGSLISKWWVITAAHCVYGHL--DYAVFMGDADLWSKRPVRIPVQDII 183
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGTVVKVARIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 184 VHQDFSMmRTVVHDIALVLLAFPVNysvNIQPVCIPEKSFLVQPGTLCWVTGWGKVLE-QGRSSRILQEIELNIIRHEKC 262
Cdd:COG5640  108 VHPDYDP-ATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625928 263 NQILKDIMGNIFTLvqeggvcGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:COG5640  184 AAYGGFDGGTMLCA-------GYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
112-340 4.40e-93

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: 278.01  E-value: 4.40e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 112 IVGGRPAPARKWPWQVSLQVHK-QHICGGSLISKWWVITAAHCVYG--HLDYAVFMGDADL--WSKRPVRIPVQDIIVHQ 186
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLssNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 187 DFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIELNIIRHEKCNQIL 266
Cdd:cd00190   81 NYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625928 267 KDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:cd00190  160 SYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
111-340 1.05e-89

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: 269.16  E-value: 1.05e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928   111 RIVGGRPAPARKWPWQVSLQVHK-QHICGGSLISKWWVITAAHCVYG--HLDYAVFMGDADL-WSKRPVRIPVQDIIVHQ 186
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLsSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928   187 DFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKV-LEQGRSSRILQEIELNIIRHEKCNQI 265
Cdd:smart00020  81 NYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625928   266 LKDImgnifTLVQEGGVC-GYNEKGGDACQGDSGGPLVCEfNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:smart00020 160 YSGG-----GAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
112-340 1.62e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 1.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928  112 IVGGRPAPARKWPWQVSLQV-HKQHICGGSLISKWWVITAAHCVYGHLDYAVFMGDADL--WSKRPVRIPVQDIIVHQDF 188
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIvlREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928  189 SMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSrILQEIELNIIRHEKCNQilkd 268
Cdd:pfam00089  81 NP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD-TLQEVTVPVVSRETCRS---- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625928  269 imgNIFTLVQEGGVCGYnEKGGDACQGDSGGPLVCEFNKtwvQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:pfam00089 155 ---AYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
109-340 2.66e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 221.06  E-value: 2.66e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 109 TARIVGGRPAPARKWPWQVSLQV---HKQHICGGSLISKWWVITAAHCVYGHL--DYAVFMGDADLWSKRPVRIPVQDII 183
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGTVVKVARIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 184 VHQDFSMmRTVVHDIALVLLAFPVNysvNIQPVCIPEKSFLVQPGTLCWVTGWGKVLE-QGRSSRILQEIELNIIRHEKC 262
Cdd:COG5640  108 VHPDYDP-ATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625928 263 NQILKDIMGNIFTLvqeggvcGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEVSYYRDWI 340
Cdd:COG5640  184 AAYGGFDGGTMLCA-------GYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
135-347 2.45e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.30  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 135 HICGGSLISKWWVITAAHCVYGHLD-----YAVFMgdADLWSKRPVRIPVQDIIVHQDFSMMRTVVHDIALVLLAFPVNY 209
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatNIVFV--PGYNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEPLGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928 210 SVNIQPVcipEKSFLVQPGTLCWVTGWGkvleQGRSSRilqeielnIIRHEKCNqilkdimgnifTLVQEGGVCGYNekg 289
Cdd:COG3591   90 TTGWLGL---AFNDAPLAGEPVTIIGYP----GDRPKD--------LSLDCSGR-----------VTGVQGNRLSYD--- 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 110625928 290 GDACQGDSGGPLVCEFNKTWVQVGIVSWglgcgriGYPGVYTEVSYYRDWIIKELSRA 347
Cdd:COG3591  141 CDTTGGSSGSPVLDDSDGGGRVVGVHSA-------GGADRANTGVRLTSAIVAALRAW 191
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
123-222 8.35e-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: 38.68  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625928  123 WPWQVSLQVHKQHICGGSLISKWWVITAAHCVYG----HLDYAVFMGDADlwSKRPVRIPVQDIIVHQDFSMMRTVvhDI 198
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlrHQYISVVLGGAK--TLKSIEGPYEQIVRVDCRHDIPES--EI 76
                          90       100
                  ....*....|....*....|....
gi 110625928  199 ALVLLAFPVNYSVNIQPVCIPEKS 222
Cdd:pfam09342  77 SLLHLASPASFSNHVLPTFVPETR 100
 
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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