NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622906416|ref|XP_014986612|]
View 

serine protease 45 isoform X3 [Macaca mulatta]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
5-233 4.61e-81

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: 243.34  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNfSSALQVPVRDIIMHPKYWGRTFImG 81
Cdd:cd00190    12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVHPNYNPSTYD-N 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSTLtpelQEAEVFIMDNKRCDQHYHKKSFF 161
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL----QEVNVPIVSNAECKRAYSYGGTI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622906416 162 PPvvplvlgDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACAKAQNPGVYTRVTKYTKWIKKQ 233
Cdd:cd00190   166 TD-------NMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
5-233 4.61e-81

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: 243.34  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNfSSALQVPVRDIIMHPKYWGRTFImG 81
Cdd:cd00190    12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVHPNYNPSTYD-N 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSTLtpelQEAEVFIMDNKRCDQHYHKKSFF 161
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL----QEVNVPIVSNAECKRAYSYGGTI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622906416 162 PPvvplvlgDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACAKAQNPGVYTRVTKYTKWIKKQ 233
Cdd:cd00190   166 TD-------NMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
5-230 1.05e-74

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: 226.79  E-value: 1.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416    5 WPWEVSLRMEN-EHVCGGALIDPSWVVTAAHCIQG--TKEYSVVLGTSKLQPMNfsSALQVPVRDIIMHPKYwGRTFIMG 81
Cdd:smart00020  13 FPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGE--EGQVIKVSKVIIHPNY-NPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKqrfSANSTLTPELQEAEVFIMDNKRCDQHYHKKSFF 161
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS---EGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAI 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622906416  162 PPvvplvlgDMICATNY--GENLCYGDSGGPLACEVeGRWILAGVLSWEKACAKAQNPGVYTRVTKYTKWI 230
Cdd:smart00020 167 TD-------NMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-230 2.06e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 2.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   3 RHWPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGTKEYSVVLGTSKLQpMNFSSALQVPVRDIIMHPKYWGRTfIMG 81
Cdd:pfam00089  10 GSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNYNPDT-LDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKqrfsaNSTLTPELQEAEVFIMDNKRCDQHYHKKsff 161
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK-----TLGPSDTLQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622906416 162 ppvvplVLGDMICATNYGENLCYGDSGGPLACEVEgrwILAGVLSWEKACAKAQNPGVYTRVTKYTKWI 230
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-234 8.42e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 8.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRMEN---EHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPmnfSSALQVPVRDIIMHPKYWGRTFi 79
Cdd:COG5640    42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLST---SGGTVVKVARIVVHPDYDPATP- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  80 MGDVALVHLQAPVTFseyVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSTltpELQEAEVFIMDNKRCdqhyhkkS 159
Cdd:COG5640   118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG---TLRKADVPVVSDATC-------A 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622906416 160 FFPPVVPlvlGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSW-EKACAkAQNPGVYTRVTKYTKWIKKQM 234
Cdd:COG5640   185 AYGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCA-AGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
5-233 4.61e-81

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: 243.34  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNfSSALQVPVRDIIMHPKYWGRTFImG 81
Cdd:cd00190    12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVHPNYNPSTYD-N 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSTLtpelQEAEVFIMDNKRCDQHYHKKSFF 161
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVL----QEVNVPIVSNAECKRAYSYGGTI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622906416 162 PPvvplvlgDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACAKAQNPGVYTRVTKYTKWIKKQ 233
Cdd:cd00190   166 TD-------NMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
5-230 1.05e-74

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: 226.79  E-value: 1.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416    5 WPWEVSLRMEN-EHVCGGALIDPSWVVTAAHCIQG--TKEYSVVLGTSKLQPMNfsSALQVPVRDIIMHPKYwGRTFIMG 81
Cdd:smart00020  13 FPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGE--EGQVIKVSKVIIHPNY-NPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKqrfSANSTLTPELQEAEVFIMDNKRCDQHYHKKSFF 161
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS---EGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAI 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622906416  162 PPvvplvlgDMICATNY--GENLCYGDSGGPLACEVeGRWILAGVLSWEKACAKAQNPGVYTRVTKYTKWI 230
Cdd:smart00020 167 TD-------NMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-230 2.06e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 2.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   3 RHWPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGTKEYSVVLGTSKLQpMNFSSALQVPVRDIIMHPKYWGRTfIMG 81
Cdd:pfam00089  10 GSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNYNPDT-LDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  82 DVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKqrfsaNSTLTPELQEAEVFIMDNKRCDQHYHKKsff 161
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK-----TLGPSDTLQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622906416 162 ppvvplVLGDMICATNYGENLCYGDSGGPLACEVEgrwILAGVLSWEKACAKAQNPGVYTRVTKYTKWI 230
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-234 8.42e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 8.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRMEN---EHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPmnfSSALQVPVRDIIMHPKYWGRTFi 79
Cdd:COG5640    42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLST---SGGTVVKVARIVVHPDYDPATP- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  80 MGDVALVHLQAPVTFseyVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSTltpELQEAEVFIMDNKRCdqhyhkkS 159
Cdd:COG5640   118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG---TLRKADVPVVSDATC-------A 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622906416 160 FFPPVVPlvlGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSW-EKACAkAQNPGVYTRVTKYTKWIKKQM 234
Cdd:COG5640   185 AYGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCA-AGYPGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
5-120 2.51e-09

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: 53.71  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416   5 WPWEVSLRMENEHVCGGALIDPSWVVTAAHCIQGTK---EY-SVVLGTSKLQPM---NFSSALQVPVRDIImhPKywgrt 77
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNlrhQYiSVVLGGAKTLKSiegPYEQIVRVDCRHDI--PE----- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622906416  78 fimGDVALVHLQAPVTFSEYVQPICLPEPNFNLKVGTQCWVTG 120
Cdd:pfam09342  74 ---SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
17-207 6.01e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  17 HVCGGALIDPSWVVTAAHCIQGTKeysvvlGTSKLQPMNFSSALQ------VPVRDIIMHPKYWGRTFIMGDVALVHLQA 90
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGA------GGGWATNIVFVPGYNggpygtATATRFRVPPGWVASGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906416  91 PVTFSEYVQPIclpEPNFNLKVGTQCWVTGWSQVK-QRFSANSTLTPELQEAEVFIMDnkrcdqhyhkksffppvvplvl 169
Cdd:COG3591    86 PLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDRpKDLSLDCSGRVTGVQGNRLSYD---------------------- 140
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622906416 170 gdmiCATnygenlCYGDSGGPLACEVEGRWILAGVLSW 207
Cdd:COG3591   141 ----CDT------TGGSSGSPVLDDSDGGGRVVGVHSA 168
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH