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Conserved domains on  [gi|476147|gb|AAA61789|]
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Serine protease-like protein; Two of the three residues in the serine protease H/D/S charge relay triad are replaced in this protein by G-98 and P-247, suggesting that it is not a serine protease [Porphyra purpurea]

Protein Classification

serine protease (domain architecture ID 12184331)

trypsin-like serine protease such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
50-299 1.84e-34

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: 125.10  E-value: 1.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147       50 RIVGGREVDDYDedtgVHFIAKLFLPDGnGFYCSGSVISKSgHVLTRAGC---EPRVNDVVRLGGSRLYNG---VVARVA 123
Cdd:smart00020   1 RIVGGSEANIGS----FPWQVSLQYGGG-RHFCGGSLISPR-WVLTAAHCvrgSDPSNIRVRLGSHDLSSGeegQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      124 KVSIHPKYDPAGEVADVAVLKLKG-VSESRLLRAGVVPVFLNRVWDNPHGmYFTGYGATDKAAQSaGSLTLKRAYLPVAP 202
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEpVTLSDNVRPICLPSSNYNVPAGTTC-TVSGWGRTSEGAGS-LPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      203 WWNCRRitdtvvvpglSRPGLPISPAAQVC---LRGGRGAgalCERDPGGPMYrvsthRGVKIYTLYAVSSYWIGlgadn 279
Cdd:smart00020 153 NATCRR----------AYSGGGAITDNMLCaggLEGGKDA---CQGDSGGPLV-----CNDGRWVLVGIVSWGSG----- 209
                          250       260
                   ....*....|....*....|.
gi 476147      280 rCPRA-MPNVGSKVAFYYSWI 299
Cdd:smart00020 210 -CARPgKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
50-299 1.84e-34

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: 125.10  E-value: 1.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147       50 RIVGGREVDDYDedtgVHFIAKLFLPDGnGFYCSGSVISKSgHVLTRAGC---EPRVNDVVRLGGSRLYNG---VVARVA 123
Cdd:smart00020   1 RIVGGSEANIGS----FPWQVSLQYGGG-RHFCGGSLISPR-WVLTAAHCvrgSDPSNIRVRLGSHDLSSGeegQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      124 KVSIHPKYDPAGEVADVAVLKLKG-VSESRLLRAGVVPVFLNRVWDNPHGmYFTGYGATDKAAQSaGSLTLKRAYLPVAP 202
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEpVTLSDNVRPICLPSSNYNVPAGTTC-TVSGWGRTSEGAGS-LPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      203 WWNCRRitdtvvvpglSRPGLPISPAAQVC---LRGGRGAgalCERDPGGPMYrvsthRGVKIYTLYAVSSYWIGlgadn 279
Cdd:smart00020 153 NATCRR----------AYSGGGAITDNMLCaggLEGGKDA---CQGDSGGPLV-----CNDGRWVLVGIVSWGSG----- 209
                          250       260
                   ....*....|....*....|.
gi 476147      280 rCPRA-MPNVGSKVAFYYSWI 299
Cdd:smart00020 210 -CARPgKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
51-302 2.87e-34

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  Cd Length: 232  Bit Score: 124.70  E-value: 2.87e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147    51 IVGGREVDDYDedtgVHFIAKLFLPDGnGFYCSGSVISKSgHVLTRAGC---EPRVNDVVRLGGSRLYN----GVVARVA 123
Cdd:cd00190   1 IVGGSEAKIGS----FPWQVSLQYTGG-RHFCGGSLISPR-WVLTAAHCvysSAPSNYTVRLGSHDLSSneggGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147   124 KVSIHPKYDPAGEVADVAVLKLKGVSEsrlLRAGVVPVFL---NRVWDNPHGMYFTGYGATDKAAQSagSLTLKRAYLPV 200
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVT---LSDNVRPICLpssGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147   201 APWWNCRRItdtvvvpglSRPGLPISPaAQVC---LRGGRGAgalCERDPGGPMyrvsTHRGVKIYTLYAVSSYWIGlga 277
Cdd:cd00190 150 VSNAECKRA---------YSYGGTITD-NMLCaggLEGGKDA---CQGDSGGPL----VCNDNGRGVLVGIVSWGSG--- 209
                       250       260
                ....*....|....*....|....*.
gi 476147   278 dnrCPRA-MPNVGSKVAFYYSWIQNQ 302
Cdd:cd00190 210 ---CARPnYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
51-299 3.31e-10

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 58.99  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      51 IVGGREVDDYDEDtgvhFIAKLFLPdGNGFYCSGSVISKSgHVLTRAGC-EPRVNDVVRLGGSRLYNG----VVARVAKV 125
Cdd:pfam00089   1 IVGGDEAQPGSFP----WQVSLQLS-SGKHFCGGSLISEN-WVLTAAHCvSGASDVKVVLGAHNIVLReggeQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147     126 SIHPKYDPAGEVADVAVLKLKgvsESRLLRAGVVPVFL---NRVWDNPHGMYFTGYGATDKAAQsagSLTLKRAYLPVAP 202
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLE---SPVTLGDTVRPICLpdaSSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147     203 WWNCRRITDTVVVPGlsrpglpispaaQVCLrGGRGAGAlCERDPGGPMYRVSThrgvkiyTLYAVSSYWIGLGADNRcp 282
Cdd:pfam00089 149 RETCRSAYGGTVTDT------------MICA-GAGGKDA-CQGDSGGPLVCSDG-------ELIGIVSWGYGCASGNY-- 205
                         250
                  ....*....|....*..
gi 476147     283 ramPNVGSKVAFYYSWI 299
Cdd:pfam00089 206 ---PGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
50-299 1.84e-34

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: 125.10  E-value: 1.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147       50 RIVGGREVDDYDedtgVHFIAKLFLPDGnGFYCSGSVISKSgHVLTRAGC---EPRVNDVVRLGGSRLYNG---VVARVA 123
Cdd:smart00020   1 RIVGGSEANIGS----FPWQVSLQYGGG-RHFCGGSLISPR-WVLTAAHCvrgSDPSNIRVRLGSHDLSSGeegQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      124 KVSIHPKYDPAGEVADVAVLKLKG-VSESRLLRAGVVPVFLNRVWDNPHGmYFTGYGATDKAAQSaGSLTLKRAYLPVAP 202
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEpVTLSDNVRPICLPSSNYNVPAGTTC-TVSGWGRTSEGAGS-LPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      203 WWNCRRitdtvvvpglSRPGLPISPAAQVC---LRGGRGAgalCERDPGGPMYrvsthRGVKIYTLYAVSSYWIGlgadn 279
Cdd:smart00020 153 NATCRR----------AYSGGGAITDNMLCaggLEGGKDA---CQGDSGGPLV-----CNDGRWVLVGIVSWGSG----- 209
                          250       260
                   ....*....|....*....|.
gi 476147      280 rCPRA-MPNVGSKVAFYYSWI 299
Cdd:smart00020 210 -CARPgKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
51-302 2.87e-34

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  Cd Length: 232  Bit Score: 124.70  E-value: 2.87e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147    51 IVGGREVDDYDedtgVHFIAKLFLPDGnGFYCSGSVISKSgHVLTRAGC---EPRVNDVVRLGGSRLYN----GVVARVA 123
Cdd:cd00190   1 IVGGSEAKIGS----FPWQVSLQYTGG-RHFCGGSLISPR-WVLTAAHCvysSAPSNYTVRLGSHDLSSneggGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147   124 KVSIHPKYDPAGEVADVAVLKLKGVSEsrlLRAGVVPVFL---NRVWDNPHGMYFTGYGATDKAAQSagSLTLKRAYLPV 200
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVT---LSDNVRPICLpssGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147   201 APWWNCRRItdtvvvpglSRPGLPISPaAQVC---LRGGRGAgalCERDPGGPMyrvsTHRGVKIYTLYAVSSYWIGlga 277
Cdd:cd00190 150 VSNAECKRA---------YSYGGTITD-NMLCaggLEGGKDA---CQGDSGGPL----VCNDNGRGVLVGIVSWGSG--- 209
                       250       260
                ....*....|....*....|....*.
gi 476147   278 dnrCPRA-MPNVGSKVAFYYSWIQNQ 302
Cdd:cd00190 210 ---CARPnYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
51-299 3.31e-10

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 58.99  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147      51 IVGGREVDDYDEDtgvhFIAKLFLPdGNGFYCSGSVISKSgHVLTRAGC-EPRVNDVVRLGGSRLYNG----VVARVAKV 125
Cdd:pfam00089   1 IVGGDEAQPGSFP----WQVSLQLS-SGKHFCGGSLISEN-WVLTAAHCvSGASDVKVVLGAHNIVLReggeQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147     126 SIHPKYDPAGEVADVAVLKLKgvsESRLLRAGVVPVFL---NRVWDNPHGMYFTGYGATDKAAQsagSLTLKRAYLPVAP 202
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLE---SPVTLGDTVRPICLpdaSSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476147     203 WWNCRRITDTVVVPGlsrpglpispaaQVCLrGGRGAGAlCERDPGGPMYRVSThrgvkiyTLYAVSSYWIGLGADNRcp 282
Cdd:pfam00089 149 RETCRSAYGGTVTDT------------MICA-GAGGKDA-CQGDSGGPLVCSDG-------ELIGIVSWGYGCASGNY-- 205
                         250
                  ....*....|....*..
gi 476147     283 ramPNVGSKVAFYYSWI 299
Cdd:pfam00089 206 ---PGVYTPVSSYLDWI 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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