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Conserved domains on  [gi|1907163435|ref|XP_036021019|]
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transmembrane protease serine 11F isoform X1 [Mus musculus]

Protein Classification

SEA and Tryp_SPc domain-containing protein( domain architecture ID 10475933)

SEA and Tryp_SPc domain-containing protein

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 ...
207-436 1.20e-100

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: 299.96  E-value: 1.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 207 IVQGRETAmEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWkNRDPTKWIVTFGTT----ITPPLVKRSVGKIII 282
Cdd:cd00190     1 IVGGSEAK-IGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSIVDDGPTQNKLRQARVETIGSDVCNRK 362
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907163435 363 DVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRDIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWIASK 436
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
60-159 2.63e-27

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 104.63  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  60 FYYLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNILIVLMFRYPSTDS 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEP 80
                          90       100
                  ....*....|....*....|
gi 1907163435 140 AERIKKRIERTFYQSLKIKQ 159
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNTT 100
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
207-436 1.20e-100

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: 299.96  E-value: 1.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 207 IVQGRETAmEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWkNRDPTKWIVTFGTT----ITPPLVKRSVGKIII 282
Cdd:cd00190     1 IVGGSEAK-IGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSIVDDGPTQNKLRQARVETIGSDVCNRK 362
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907163435 363 DVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRDIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWIASK 436
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
206-433 6.23e-97

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: 290.35  E-value: 6.23e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  206 RIVQGRETAmEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWkNRDPTKWIVTFGTT---ITPPLVKRSVGKIII 282
Cdd:smart00020   1 RIVGGSEAN-IGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHdlsSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSI-VDDGPTQNKLRQARVETIGSDVCNR 361
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907163435  362 KDVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRdIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
199-438 5.29e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.92  E-value: 5.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 199 PASSSTERIVQGRETAmEGEWPWQASLQLIG--AGHQCGATLISNTWLLTAAHCFwKNRDPTKWIVTFGTT--ITPPLVK 274
Cdd:COG5640    23 PAADAAPAIVGGTPAT-VGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTdlSTSGGTV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 275 RSVGKIIIHEEYHRDTNENDIALAQLTTRVefsNVVQRVCLPDSSMKLPPKTSVFVTGFGSIV-DDGPTQNKLRQARVET 353
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 354 IGSDVCNrkdVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRDIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:COG5640   178 VSDATCA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*
gi 1907163435 434 ASKTG 438
Cdd:COG5640   255 KSTAG 259
Trypsin pfam00089
Trypsin;
207-433 6.46e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 6.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 207 IVQGRETAMeGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFwknRDPTKWIVTFGTTIT----PPLVKRSVGKIII 282
Cdd:pfam00089   1 IVGGDEAQP-GSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIvlreGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSIVDDGPTQNkLRQARVETIGSDVCNRk 362
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907163435 363 dVYDGLITPGMLCAGFmeGKIDACKGDSGGPLVYDNRdiwYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
60-159 2.63e-27

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 104.63  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  60 FYYLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNILIVLMFRYPSTDS 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEP 80
                          90       100
                  ....*....|....*....|
gi 1907163435 140 AERIKKRIERTFYQSLKIKQ 159
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNTT 100
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
62-140 1.05e-06

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 47.41  E-value: 1.05e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907163435   62 YLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNilIVLMFRYPSTDSA 140
Cdd:smart00200  10 SVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVD--LGLLFNEGVTNGQ 86
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
207-436 1.20e-100

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: 299.96  E-value: 1.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 207 IVQGRETAmEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWkNRDPTKWIVTFGTT----ITPPLVKRSVGKIII 282
Cdd:cd00190     1 IVGGSEAK-IGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSIVDDGPTQNKLRQARVETIGSDVCNRK 362
Cdd:cd00190    79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907163435 363 DVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRDIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWIASK 436
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
206-433 6.23e-97

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: 290.35  E-value: 6.23e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  206 RIVQGRETAmEGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFWkNRDPTKWIVTFGTT---ITPPLVKRSVGKIII 282
Cdd:smart00020   1 RIVGGSEAN-IGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHdlsSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSI-VDDGPTQNKLRQARVETIGSDVCNR 361
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907163435  362 KDVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRdIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
199-438 5.29e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.92  E-value: 5.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 199 PASSSTERIVQGRETAmEGEWPWQASLQLIG--AGHQCGATLISNTWLLTAAHCFwKNRDPTKWIVTFGTT--ITPPLVK 274
Cdd:COG5640    23 PAADAAPAIVGGTPAT-VGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTdlSTSGGTV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 275 RSVGKIIIHEEYHRDTNENDIALAQLTTRVefsNVVQRVCLPDSSMKLPPKTSVFVTGFGSIV-DDGPTQNKLRQARVET 353
Cdd:COG5640   101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 354 IGSDVCNrkdVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNRDIWYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:COG5640   178 VSDATCA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*
gi 1907163435 434 ASKTG 438
Cdd:COG5640   255 KSTAG 259
Trypsin pfam00089
Trypsin;
207-433 6.46e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 6.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 207 IVQGRETAMeGEWPWQASLQLIGAGHQCGATLISNTWLLTAAHCFwknRDPTKWIVTFGTTIT----PPLVKRSVGKIII 282
Cdd:pfam00089   1 IVGGDEAQP-GSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIvlreGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 283 HEEYHRDTNENDIALAQLTTRVEFSNVVQRVCLPDSSMKLPPKTSVFVTGFGSIVDDGPTQNkLRQARVETIGSDVCNRk 362
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907163435 363 dVYDGLITPGMLCAGFmeGKIDACKGDSGGPLVYDNRdiwYIVGIVSWGQSCALPNKPGVYTRVTKYRDWI 433
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
60-159 2.63e-27

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 104.63  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435  60 FYYLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNILIVLMFRYPSTDS 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEP 80
                          90       100
                  ....*....|....*....|
gi 1907163435 140 AERIKKRIERTFYQSLKIKQ 159
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNTT 100
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
225-411 8.23e-18

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 81.26  E-value: 8.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 225 LQLIGAGHQCGATLISNTWLLTAAHCFW---KNRDPTKWIVTFGTTITPPlVKRSVGKIIIHEEYHRDTNEN-DIALAQL 300
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCVYdgaGGGWATNIVFVPGYNGGPY-GTATATRFRVPPGWVASGDAGyDYALLRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 301 TTRVEFSNVVQRVclpDSSMKLPPKTSVFVTGFGsivDDGPTQNKLRQArvetigsdvCNRKDVYDGLItpGMLCagfme 380
Cdd:COG3591    84 DEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYP---GDRPKDLSLDCS---------GRVTGVQGNRL--SYDC----- 141
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907163435 381 gkiDACKGDSGGPLVYDNRDIWYIVGIVSWG 411
Cdd:COG3591   142 ---DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
62-140 1.05e-06

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 47.41  E-value: 1.05e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907163435   62 YLASFQVTSIKYRENYGIRSSREFIERSHQIERMMSRIFRRSSGVGRFIKSHVIKISPDEQGVNilIVLMFRYPSTDSA 140
Cdd:smart00200  10 SVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVD--LGLLFNEGVTNGQ 86
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
219-319 3.17e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.53  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163435 219 WPWQASLQLIGAgHQCGATLISNTWLLTAAHCFWKNRDPTKWI-VTFGTTITPPLVKRSVGKIIIHEEYHrDTNENDIAL 297
Cdd:pfam09342   1 WPWIAKVYLDGN-MICSGVLIDASWVIVSGSCLRDTNLRHQYIsVVLGGAKTLKSIEGPYEQIVRVDCRH-DIPESEISL 78
                          90       100
                  ....*....|....*....|..
gi 1907163435 298 AQLTTRVEFSNVVQRVCLPDSS 319
Cdd:pfam09342  79 LHLASPASFSNHVLPTFVPETR 100
 
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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