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Conserved domains on  [gi|205360907|ref|NP_001128559|]
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serine protease 41 precursor [Rattus norvegicus]

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 ...
55-292 2.73e-89

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: 266.45  E-value: 2.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  55 IVGGIESVRGRWPWQASLRLRKF-HRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQLTSKpsfwNREAFSGRYRVKD 133
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLS----SNEGGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 134 IIINS--EDKLKYHDLALLRLASSVTYNKFIQPVCvLPSaSMSQHQP--RCWVTGWGALQEDLkplPPPYHLREVQVTVL 209
Cdd:cd00190   76 VIVHPnyNPSTYDNDIALLKLKRPVTLSDNVRPIC-LPS-SGYNLPAgtTCTVSGWGRTSEGG---PLPDVLQEVNVPIV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 210 NLSRCQELFSFASRyhlITRDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSRGVGCGRPKLPGIYTNVSHHYD 289
Cdd:cd00190  151 SNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                 ...
gi 205360907 290 WIK 292
Cdd:cd00190  228 WIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
55-292 2.73e-89

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: 266.45  E-value: 2.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  55 IVGGIESVRGRWPWQASLRLRKF-HRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQLTSKpsfwNREAFSGRYRVKD 133
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLS----SNEGGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 134 IIINS--EDKLKYHDLALLRLASSVTYNKFIQPVCvLPSaSMSQHQP--RCWVTGWGALQEDLkplPPPYHLREVQVTVL 209
Cdd:cd00190   76 VIVHPnyNPSTYDNDIALLKLKRPVTLSDNVRPIC-LPS-SGYNLPAgtTCTVSGWGRTSEGG---PLPDVLQEVNVPIV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 210 NLSRCQELFSFASRyhlITRDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSRGVGCGRPKLPGIYTNVSHHYD 289
Cdd:cd00190  151 SNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                 ...
gi 205360907 290 WIK 292
Cdd:cd00190  228 WIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
54-291 8.05e-88

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: 262.61  E-value: 8.05e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907    54 RIVGGIESVRGRWPWQASLRLRKF-HRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQltskpSFWNREAFSGRYRVK 132
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGS-----HDLSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   133 DIIINS--EDKLKYHDLALLRLASSVTYNKFIQPVCVLPSASMSQHQPRCWVTGWGALQEDlkPLPPPYHLREVQVTVLN 210
Cdd:smart00020  75 KVIIHPnyNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG--AGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   211 LSRCQELFSfasRYHLITRDVFCAGAEDGSADTCSGDSGGPLVCNmDGLWYQIGIVSRGVGCGRPKLPGIYTNVSHHYDW 290
Cdd:smart00020 153 NATCRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 205360907   291 I 291
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
40-295 1.13e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  40 LLSMPCGRRNDIRSRIVGGIESVRGRWPWQASLRLRK---FHRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQLtsk 116
Cdd:COG5640   16 ALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGST--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 117 psfwNREAFSG-RYRVKDIIINSE--DKLKYHDLALLRLASSVTynkFIQPVCVLPSASMSQHQPRCWVTGWGALQEDLK 193
Cdd:COG5640   92 ----DLSTSGGtVVKVARIVVHPDydPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 194 PLPPpyHLREVQVTVLNLSRCQELFSFasryhlITRDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSRGVGCG 273
Cdd:COG5640  165 SQSG--TLRKADVPVVSDATCAAYGGF------DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPC 236
                        250       260
                 ....*....|....*....|..
gi 205360907 274 RPKLPGIYTNVSHHYDWIKTMM 295
Cdd:COG5640  237 AAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
55-291 2.61e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 194.58  E-value: 2.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   55 IVGGIESVRGRWPWQASLRLR-KFHRCGGSLLSHRWVLTAAHCFRkflDPKKWTVQLGQLTSKpsfwNREAFSGRYRVKD 133
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIV----LREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  134 III--NSEDKLKYHDLALLRLASSVTYNKFIQPVCVLPSASMSQHQPRCWVTGWGalqeDLKPLPPPYHLREVQVTVLNL 211
Cdd:pfam00089  74 IIVhpNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG----NTKTLGPSDTLQEVTVPVVSR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  212 SRCQElfsfaSRYHLITRDVFCAGAedGSADTCSGDSGGPLVCnMDGlwYQIGIVSRGVGCGRPKLPGIYTNVSHHYDWI 291
Cdd:pfam00089 150 ETCRS-----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
55-292 2.73e-89

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: 266.45  E-value: 2.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  55 IVGGIESVRGRWPWQASLRLRKF-HRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQLTSKpsfwNREAFSGRYRVKD 133
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLS----SNEGGGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 134 IIINS--EDKLKYHDLALLRLASSVTYNKFIQPVCvLPSaSMSQHQP--RCWVTGWGALQEDLkplPPPYHLREVQVTVL 209
Cdd:cd00190   76 VIVHPnyNPSTYDNDIALLKLKRPVTLSDNVRPIC-LPS-SGYNLPAgtTCTVSGWGRTSEGG---PLPDVLQEVNVPIV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 210 NLSRCQELFSFASRyhlITRDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSRGVGCGRPKLPGIYTNVSHHYD 289
Cdd:cd00190  151 SNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                 ...
gi 205360907 290 WIK 292
Cdd:cd00190  228 WIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
54-291 8.05e-88

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: 262.61  E-value: 8.05e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907    54 RIVGGIESVRGRWPWQASLRLRKF-HRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQltskpSFWNREAFSGRYRVK 132
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGS-----HDLSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   133 DIIINS--EDKLKYHDLALLRLASSVTYNKFIQPVCVLPSASMSQHQPRCWVTGWGALQEDlkPLPPPYHLREVQVTVLN 210
Cdd:smart00020  75 KVIIHPnyNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG--AGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   211 LSRCQELFSfasRYHLITRDVFCAGAEDGSADTCSGDSGGPLVCNmDGLWYQIGIVSRGVGCGRPKLPGIYTNVSHHYDW 290
Cdd:smart00020 153 NATCRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 205360907   291 I 291
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
40-295 1.13e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  40 LLSMPCGRRNDIRSRIVGGIESVRGRWPWQASLRLRK---FHRCGGSLLSHRWVLTAAHCFRKFlDPKKWTVQLGQLtsk 116
Cdd:COG5640   16 ALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGST--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 117 psfwNREAFSG-RYRVKDIIINSE--DKLKYHDLALLRLASSVTynkFIQPVCVLPSASMSQHQPRCWVTGWGALQEDLK 193
Cdd:COG5640   92 ----DLSTSGGtVVKVARIVVHPDydPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 194 PLPPpyHLREVQVTVLNLSRCQELFSFasryhlITRDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSRGVGCG 273
Cdd:COG5640  165 SQSG--TLRKADVPVVSDATCAAYGGF------DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPC 236
                        250       260
                 ....*....|....*....|..
gi 205360907 274 RPKLPGIYTNVSHHYDWIKTMM 295
Cdd:COG5640  237 AAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
55-291 2.61e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 194.58  E-value: 2.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907   55 IVGGIESVRGRWPWQASLRLR-KFHRCGGSLLSHRWVLTAAHCFRkflDPKKWTVQLGQLTSKpsfwNREAFSGRYRVKD 133
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIV----LREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  134 III--NSEDKLKYHDLALLRLASSVTYNKFIQPVCVLPSASMSQHQPRCWVTGWGalqeDLKPLPPPYHLREVQVTVLNL 211
Cdd:pfam00089  74 IIVhpNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG----NTKTLGPSDTLQEVTVPVVSR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  212 SRCQElfsfaSRYHLITRDVFCAGAedGSADTCSGDSGGPLVCnMDGlwYQIGIVSRGVGCGRPKLPGIYTNVSHHYDWI 291
Cdd:pfam00089 150 ETCRS-----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
78-271 2.29e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.22  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907  78 HRCGGSLLSHRWVLTAAHCFRKFLD---PKKWTVQLGqltskpsfWNREAFsGRYRVKDIIINSEDKLKY---HDLALLR 151
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPG--------YNGGPY-GTATATRFRVPPGWVASGdagYDYALLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360907 152 LASSVTYnkfiqpvcvlpsasmsqhqprcwVTGWGALQEDLKPLPPPyhlrevQVTVlnlsrcqelFSF-ASRYHLITRD 230
Cdd:COG3591   83 LDEPLGD-----------------------TTGWLGLAFNDAPLAGE------PVTI---------IGYpGDRPKDLSLD 124
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 205360907 231 VFCA--GAEDG----SADTCSGDSGGPLVCNMDGLWYQIGIVSRGVG 271
Cdd:COG3591  125 CSGRvtGVQGNrlsyDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
 
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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