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Conserved domains on  [gi|1622906407|ref|XP_028699881|]
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serine protease 44 isoform X1 [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

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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 ...
115-346 2.35e-96

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: 286.48  E-value: 2.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 115 IIGGLPALNRKWPWQVSLQ-TEDKHLCGASLIDRRWVLTAAHCVFSDL--EYKVKLGDTNLNAGSENTLVIPVKDIIFPS 191
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 192 NFDFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSERvsGSGPFVLREAKLNILRHEQCRET 271
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622906407 272 ikkksAAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCELNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:cd00190   159 -----YSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
115-346 2.35e-96

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: 286.48  E-value: 2.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 115 IIGGLPALNRKWPWQVSLQ-TEDKHLCGASLIDRRWVLTAAHCVFSDL--EYKVKLGDTNLNAGSENTLVIPVKDIIFPS 191
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 192 NFDFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSERvsGSGPFVLREAKLNILRHEQCRET 271
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622906407 272 ikkksAAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCELNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:cd00190   159 -----YSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
114-346 1.76e-93

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: 279.18  E-value: 1.76e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407  114 RIIGGLPALNRKWPWQVSLQTED-KHLCGASLIDRRWVLTAAHCVFSDLE--YKVKLGDTNLNAGSENTlVIPVKDIIFP 190
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPsnIRVRLGSHDLSSGEEGQ-VIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407  191 SNFDFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSErVSGSGPFVLREAKLNILRHEQCRE 270
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622906407  271 TikkksAAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCElNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:smart00020 159 A-----YSGGGAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
115-346 2.14e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 2.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 115 IIGGLPALNRKWPWQVSLQ-TEDKHLCGASLIDRRWVLTAAHCVFSDLEYKVKLGDTNLNAGSENTLVIPVKDIIFPSNF 193
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 194 DFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSErvsGSGPFVLREAKLNILRHEQCRETIk 273
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCRSAY- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622906407 274 kksaakSKMVTRGTVC-GYNdqGKDSCQGDSGGPLVCELNgtwFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:pfam00089 157 ------GGTVTDTMICaGAG--GKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
113-351 1.18e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.12  E-value: 1.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 113 SRIIGGLPALNRKWPWQVSLQTED---KHLCGASLIDRRWVLTAAHCVFSDL--EYKVKLGDTNLNAGSENtlVIPVKDI 187
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGT--VVKVARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 188 IFPSNFDFASLTNDIALALLAYSVnysSHIQPVCLPKELFEVETGTECWVTGWGRVSERvSGSGPFVLREAKLNILRHEQ 267
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEG-PGSQSGTLRKADVPVVSDAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 268 CRetikkksaAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCELNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:COG5640   183 CA--------AYGGFDGGTMLCaGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*
gi 1622906407 347 IDRLR 351
Cdd:COG5640   255 KSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
115-346 2.35e-96

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: 286.48  E-value: 2.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 115 IIGGLPALNRKWPWQVSLQ-TEDKHLCGASLIDRRWVLTAAHCVFSDL--EYKVKLGDTNLNAGSENTLVIPVKDIIFPS 191
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 192 NFDFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSERvsGSGPFVLREAKLNILRHEQCRET 271
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622906407 272 ikkksAAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCELNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:cd00190   159 -----YSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
114-346 1.76e-93

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: 279.18  E-value: 1.76e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407  114 RIIGGLPALNRKWPWQVSLQTED-KHLCGASLIDRRWVLTAAHCVFSDLE--YKVKLGDTNLNAGSENTlVIPVKDIIFP 190
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPsnIRVRLGSHDLSSGEEGQ-VIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407  191 SNFDFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSErVSGSGPFVLREAKLNILRHEQCRE 270
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622906407  271 TikkksAAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCElNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:smart00020 159 A-----YSGGGAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
115-346 2.14e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.01  E-value: 2.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 115 IIGGLPALNRKWPWQVSLQ-TEDKHLCGASLIDRRWVLTAAHCVFSDLEYKVKLGDTNLNAGSENTLVIPVKDIIFPSNF 193
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 194 DFASLTNDIALALLAYSVNYSSHIQPVCLPKELFEVETGTECWVTGWGRVSErvsGSGPFVLREAKLNILRHEQCRETIk 273
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCRSAY- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622906407 274 kksaakSKMVTRGTVC-GYNdqGKDSCQGDSGGPLVCELNgtwFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:pfam00089 157 ------GGTVTDTMICaGAG--GKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
113-351 1.18e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.12  E-value: 1.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 113 SRIIGGLPALNRKWPWQVSLQTED---KHLCGASLIDRRWVLTAAHCVFSDL--EYKVKLGDTNLNAGSENtlVIPVKDI 187
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGT--VVKVARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 188 IFPSNFDFASLTNDIALALLAYSVnysSHIQPVCLPKELFEVETGTECWVTGWGRVSERvSGSGPFVLREAKLNILRHEQ 267
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEG-PGSQSGTLRKADVPVVSDAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 268 CRetikkksaAKSKMVTRGTVC-GYNDQGKDSCQGDSGGPLVCELNGTWFQVGIVSWGVGCGRKGYPGVYTEVSFYKKWI 346
Cdd:COG5640   183 CA--------AYGGFDGGTMLCaGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*
gi 1622906407 347 IDRLR 351
Cdd:COG5640   255 KSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
138-326 4.62e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.67  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 138 HLCGASLIDRRWVLTAAHCVFSDL------EYKVKLGDTNLNAGSENtlvipVKDIIFPSNFDFASLTN-DIALALLAYS 210
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPGYNGGPYGTAT-----ATRFRVPPGWVASGDAGyDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622906407 211 VNYSSHIQPVCLPKELFeveTGTECWVTGWGrvservsGSGPFVLReaklnilRHEQCRetikkksaaksKMVTRGTVCG 290
Cdd:COG3591    87 LGDTTGWLGLAFNDAPL---AGEPVTIIGYP-------GDRPKDLS-------LDCSGR-----------VTGVQGNRLS 138
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622906407 291 YNdqgKDSCQGDSGGPLVCELNGTWFQVGIVSWGVG 326
Cdd:COG3591   139 YD---CDTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 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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