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Conserved domains on  [gi|2738865|gb|AAB94558|]
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Protein Classification

CLIP and Tryp_SPc domain-containing protein (domain architecture ID 11643046)

CLIP and Tryp_SPc domain-containing protein

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 ...
161-399 4.49e-73

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: 227.95  E-value: 4.49e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIAAGWGLLEDRGATPSDVMQKVIVKKIRKVTCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     318 RDYPGDTsavaakYDSESQLCYGDRQEKKDTCHGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNRPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 2738865     398 WI 399
Cdd:smart00020 228 WI 229
CLIP super family cl02731
Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the ...
26-66 1.09e-03

Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively.


The actual alignment was detected with superfamily member smart00680:

Pssm-ID: 413454  Cd Length: 52  Bit Score: 36.72  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2738865      26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 4.49e-73

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: 227.95  E-value: 4.49e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIAAGWGLLEDRGATPSDVMQKVIVKKIRKVTCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     318 RDYPGDTsavaakYDSESQLCYGDRQEKKDTCHGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNRPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 2738865     398 WI 399
Cdd:smart00020 228 WI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
161-402 2.68e-71

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: 223.31  E-value: 2.68e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTP-ENTYKVKRS 239
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-VRLGSHDLSSNEGgGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  240 VRHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIAAGWGLLEDRGaTPSDVMQKVIVKKIRKVTC 316
Cdd:cd00190  77 IVHPNYNPSTYdNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  317 QRDYPGDtsavaaKYDSESQLCYGDRQEKKDTCHGDSGGPLQLKHkkiNCMYLVIGVTSGGKGCALRNRPGLYSKVSHYL 396
Cdd:cd00190 156 KRAYSYG------GTITDNMLCAGGLEGGKDACQGDSGGPLVCND---NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                ....*.
gi 2738865  397 DWIESI 402
Cdd:cd00190 227 DWIQKT 232
Trypsin pfam00089
Trypsin;
161-399 1.21e-49

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 167.23  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    161 IVGGVNASRNEFPHMVLLGFnttTGISWMCGGSLISEKFILTAGHCVmhKDFGDVK-YASIGVLSRGEVTpENTYKVKRS 239
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV--SGASDVKvVLGAHNIVLREGG-EQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    240 VRHPQYRID-VYNDIAVIELEKEVTLDAFTVPACL-------HVGDPIdysraIAAGWGLLEDRGatPSDVMQKVIVKKI 311
Cdd:pfam00089  75 IVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLpdassdlPVGTTC-----TVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    312 RKVTCQRDYPGDTSavaakydsESQLCYGDRqeKKDTCHGDSGGPLQLKHKKincmylVIGVTSGGKGCALRNRPGLYSK 391
Cdd:pfam00089 148 SRETCRSAYGGTVT--------DTMICAGAG--GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTP 211

                  ....*...
gi 2738865    392 VSHYLDWI 399
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
156-400 6.80e-19

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 87.62  E-value: 6.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  156 NADEL---IVGGVNASRNEFPHMV-LLGFNTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKYaSIGVLSRGEVTPE 231
Cdd:COG5640  25 TADEVssrIIGGSNANAGEYPSLVaLVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDV-NRVVVDLNDSSQA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  232 NTYKVKRSVRHPQYRIDVY-NDIAVIELEKEVTLDAFTVpaclHVGDPIDYSRAIAAGWGLLEDRG---ATPSDV----- 302
Cdd:COG5640 104 ERGHVRTIYVHEFYSPGNLgNDIAVLELARAASLPRVKI----TSFDASDTFLNSVTTVSPMTNGTfgvTTPSDVprssp 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  303 ----MQKVIVKKIRKVTCQRdYPGDTSAvAAKYDSESQLCYGdrQEKKDTCHGDSGGPLQLKHkkiNCMYLVIGVTSGGK 378
Cdd:COG5640 180 kgtiLHEVAVLFVPLSTCAQ-YKGCANA-SDGATGLTGFCAG--RPPKDACQGDSGGPIFHKG---EEGRVQRGVVSWGD 252
                       250       260
                ....*....|....*....|...
gi 2738865  379 G-CALRNRPGLYSKVSHYLDWIE 400
Cdd:COG5640 253 GgCGGTLIPGVYTNVSNYQDWIA 275
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
26-66 1.09e-03

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 36.72  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2738865      26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 4.49e-73

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: 227.95  E-value: 4.49e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIAAGWGLLEDRGATPSDVMQKVIVKKIRKVTCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865     318 RDYPGDTsavaakYDSESQLCYGDRQEKKDTCHGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNRPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 2738865     398 WI 399
Cdd:smart00020 228 WI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
161-402 2.68e-71

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: 223.31  E-value: 2.68e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTP-ENTYKVKRS 239
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-VRLGSHDLSSNEGgGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  240 VRHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIAAGWGLLEDRGaTPSDVMQKVIVKKIRKVTC 316
Cdd:cd00190  77 IVHPNYNPSTYdNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  317 QRDYPGDtsavaaKYDSESQLCYGDRQEKKDTCHGDSGGPLQLKHkkiNCMYLVIGVTSGGKGCALRNRPGLYSKVSHYL 396
Cdd:cd00190 156 KRAYSYG------GTITDNMLCAGGLEGGKDACQGDSGGPLVCND---NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                ....*.
gi 2738865  397 DWIESI 402
Cdd:cd00190 227 DWIQKT 232
Trypsin pfam00089
Trypsin;
161-399 1.21e-49

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 167.23  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    161 IVGGVNASRNEFPHMVLLGFnttTGISWMCGGSLISEKFILTAGHCVmhKDFGDVK-YASIGVLSRGEVTpENTYKVKRS 239
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV--SGASDVKvVLGAHNIVLREGG-EQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    240 VRHPQYRID-VYNDIAVIELEKEVTLDAFTVPACL-------HVGDPIdysraIAAGWGLLEDRGatPSDVMQKVIVKKI 311
Cdd:pfam00089  75 IVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLpdassdlPVGTTC-----TVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865    312 RKVTCQRDYPGDTSavaakydsESQLCYGDRqeKKDTCHGDSGGPLQLKHKKincmylVIGVTSGGKGCALRNRPGLYSK 391
Cdd:pfam00089 148 SRETCRSAYGGTVT--------DTMICAGAG--GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTP 211

                  ....*...
gi 2738865    392 VSHYLDWI 399
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
156-400 6.80e-19

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 87.62  E-value: 6.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  156 NADEL---IVGGVNASRNEFPHMV-LLGFNTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKYaSIGVLSRGEVTPE 231
Cdd:COG5640  25 TADEVssrIIGGSNANAGEYPSLVaLVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDV-NRVVVDLNDSSQA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  232 NTYKVKRSVRHPQYRIDVY-NDIAVIELEKEVTLDAFTVpaclHVGDPIDYSRAIAAGWGLLEDRG---ATPSDV----- 302
Cdd:COG5640 104 ERGHVRTIYVHEFYSPGNLgNDIAVLELARAASLPRVKI----TSFDASDTFLNSVTTVSPMTNGTfgvTTPSDVprssp 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738865  303 ----MQKVIVKKIRKVTCQRdYPGDTSAvAAKYDSESQLCYGdrQEKKDTCHGDSGGPLQLKHkkiNCMYLVIGVTSGGK 378
Cdd:COG5640 180 kgtiLHEVAVLFVPLSTCAQ-YKGCANA-SDGATGLTGFCAG--RPPKDACQGDSGGPIFHKG---EEGRVQRGVVSWGD 252
                       250       260
                ....*....|....*....|...
gi 2738865  379 G-CALRNRPGLYSKVSHYLDWIE 400
Cdd:COG5640 253 GgCGGTLIPGVYTNVSNYQDWIA 275
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
26-66 1.09e-03

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 36.72  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2738865      26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
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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