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Conserved domains on  [gi|385252059|pdb|4DJZ|D]
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Chain D, Mannan-binding lectin serine protease 1 light chain

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

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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 ...
1-246 3.01e-90

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: 266.06  E-value: 3.01e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpkdptlrdsdllSPSDFKIILGKHWRLRSDE 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 157
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D      158 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 237
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
4DJZ_D      238 HNKDWIQRV 246
Cdd:cd00190 224 SYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-246 3.01e-90

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: 266.06  E-value: 3.01e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpkdptlrdsdllSPSDFKIILGKHWRLRSDE 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 157
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D      158 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 237
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
4DJZ_D      238 HNKDWIQRV 246
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-243 2.54e-86

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: 256.07  E-value: 2.54e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D           1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpkdptlrdsdllSPSDFKIILGKHWRlRSDE 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSGE 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D          81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLMEI 156
Cdd:smart00020  67 EGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQEV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D         157 EIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSYI 236
Cdd:smart00020 147 NVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTRV 222

                   ....*..
4DJZ_D         237 HHNKDWI 243
Cdd:smart00020 223 SSYLDWI 229
Trypsin pfam00089
Trypsin;
1-243 9.31e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.55  E-value: 9.31e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D          1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpkdptlrdsdllSPSDFKIILGKHWRLRSDE 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D         81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 158
Cdd:pfam00089  65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        159 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 238
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214

                  ....*
4DJZ_D        239 NKDWI 243
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-249 5.00e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.66  E-value: 5.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        1 IFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpkdptlrdsDLLSPSDFKIILGKHwRLRS 78
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       79 DENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPETLM 154
Cdd:COG5640  96 SGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D      155 EIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGVYS 234
Cdd:COG5640 172 KADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                       250
                ....*....|....*
4DJZ_D      235 YIHHNKDWIQRVTGV 249
Cdd:COG5640 246 RVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-246 3.01e-90

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: 266.06  E-value: 3.01e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpkdptlrdsdllSPSDFKIILGKHWRLRSDE 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--------------APSNYTVRLGSHDLSSNEG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGK-QFLQRFPETLMEIE 157
Cdd:cd00190  67 GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnlPAGTTCTVSGWGRtSEGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D      158 IPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTlnRERGQWYLVGTVSWGDDCGKKDRYGVYSYIH 237
Cdd:cd00190 147 VPIVSNAECKRAY-SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC--NDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                ....*....
4DJZ_D      238 HNKDWIQRV 246
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-243 2.54e-86

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: 256.07  E-value: 2.54e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D           1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSldpkdptlrdsdllSPSDFKIILGKHWRlRSDE 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--------------DPSNIRVRLGSHDL-SSGE 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D          81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQ--EGAMVIVSGWGKQFL--QRFPETLMEI 156
Cdd:smart00020  67 EGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEgaGSLPDTLQEV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D         157 EIPIVDHSTCQKAYaPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNrerGQWYLVGTVSWGDDCGKKDRYGVYSYI 236
Cdd:smart00020 147 NVPIVSNATCRRAY-SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKPGVYTRV 222

                   ....*..
4DJZ_D         237 HHNKDWI 243
Cdd:smart00020 223 SSYLDWI 229
Trypsin pfam00089
Trypsin;
1-243 9.31e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.55  E-value: 9.31e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D          1 IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqsldpkdptlrdsdllSPSDFKIILGKHWRLRSDE 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS----------------GASDVKVVLGAHNIVLREG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D         81 NEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQ--QEGAMVIVSGWGKQFLQRFPETLMEIEI 158
Cdd:pfam00089  65 GEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        159 PIVDHSTCQKAYaplKKKVTRDMICAGekEGGKDACAGDSGGPMVTLNRergqwYLVGTVSWGDDCGKKDRYGVYSYIHH 238
Cdd:pfam00089 145 PVVSRETCRSAY---GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSS 214

                  ....*
4DJZ_D        239 NKDWI 243
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-249 5.00e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.66  E-value: 5.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D        1 IFNGRPAQKGTTPWIAMLSHLNG--QPFCGGSLLGSSWIVTAAHCLhqsldpkdptlrdsDLLSPSDFKIILGKHwRLRS 78
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCV--------------DGDGPSDLRVVIGST-DLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       79 DENEQHlGVKHTTLHPQYDPNTFENDVALVELlESPVlnAFVMPICLPEGPQQ--EGAMVIVSGWGK--QFLQRFPETLM 154
Cdd:COG5640  96 SGGTVV-KVARIVVHPDYDPATPGNDIALLKL-ATPV--PGVAPAPLATSADAaaPGTPATVAGWGRtsEGPGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D      155 EIEIPIVDHSTCQkAYAPLkkkVTRDMICAGEKEGGKDACAGDSGGPMVtlNRERGQWYLVGTVSWGDDCGKKDRYGVYS 234
Cdd:COG5640 172 KADVPVVSDATCA-AYGGF---DGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                       250
                ....*....|....*
4DJZ_D      235 YIHHNKDWIQRVTGV 249
Cdd:COG5640 246 RVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
15-223 4.02e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.76  E-value: 4.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       15 IAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHqslDPKDPTLrdsdllsPSDFKIILGkhwrlRSDENEQHLGVKHTTLHP 94
Cdd:COG3591   2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVY---DGAGGGW-------ATNIVFVPG-----YNGGPYGTATATRFRVPP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4DJZ_D       95 QYDPNT-FENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVS---GWGKQFLQRFPETLMEIEIPIVDHSTcqkay 170
Cdd:COG3591  67 GWVASGdAGYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGypgDRPKDLSLDCSGRVTGVQGNRLSYDC----- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
4DJZ_D      171 aplkkkvtrdmicagekeggkDACAGDSGGPMvtLNRERGQWYLVGTVSWGDD 223
Cdd:COG3591 142 ---------------------DTTGGSSGSPV--LDDSDGGGRVVGVHSAGGA 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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