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Conserved domains on  [gi|84794609|ref|NP_001028405|]
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transmembrane protease serine 11A [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 ...
158-386 1.70e-99

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: 294.95  E-value: 1.70e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 158 IVSGNPAAKGAWPWQVSLQRSNI-HQCGGTLIGNMWVVTAAHCFRtNSNPRQWTLSFGTT----INPPLMKRDVRRIIMH 232
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQNELREARVQIISNDICKKRH 312
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794609 313 VYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkDTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWIASK 386
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
39-132 1.41e-24

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: 96.54  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    39 FLVFDIQVNSNSGQKSSNQLKDLQETNENLVDEIFIDSALNNRYIKNHVVGLTPEEDDTKADIVMVFQPPATGRRTVGKK 118
Cdd:pfam01390   7 FKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEPALDREK 86
                          90
                  ....*....|....
gi 84794609   119 THHSILDQKTRNAR 132
Cdd:pfam01390  87 LIEEILRQTLNNTT 100
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-386 1.70e-99

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: 294.95  E-value: 1.70e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 158 IVSGNPAAKGAWPWQVSLQRSNI-HQCGGTLIGNMWVVTAAHCFRtNSNPRQWTLSFGTT----INPPLMKRDVRRIIMH 232
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQNELREARVQIISNDICKKRH 312
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794609 313 VYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkDTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWIASK 386
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-383 2.63e-96

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: 286.88  E-value: 2.63e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    157 RIVSGNPAAKGAWPWQVSLQRSNI-HQCGGTLIGNMWVVTAAHCFRtNSNPRQWTLSFGTT---INPPLMKRDVRRIIMH 232
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHdlsSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQ-NELREARVQIISNDICKKR 311
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794609    312 HVYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkdTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWI 383
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG--RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
158-383 5.60e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 5.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   158 IVSGNPAAKGAWPWQVSLQ-RSNIHQCGGTLIGNMWVVTAAHCFrtnSNPRQWTLSFGTTI----NPPLMKRDVRRIIMH 232
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNivlrEGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQNeLREARVQIISNDICKKRh 312
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84794609   313 vYGNEIKRGMFCAGFleGNYDACRGDSGGPLVIRDNkdtwYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWI 383
Cdd:pfam00089 156 -YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
154-388 1.42e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.22  E-value: 1.42e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 154 IANRIVSGNPAAKGAWPWQVSLQRSNI---HQCGGTLIGNMWVVTAAHCFrTNSNPRQWTLSFGTT--INPPLMKRDVRR 228
Cdd:COG5640  27 AAPAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTdlSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 229 IIMHERYRPPARDHDIALVQFSPRVTfsdEVRRICLPEPSASFPPNSTVYITGFGALY-YGGESQNELREARVQIISNDI 307
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 308 CKkrhVYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkDTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWIASKT 387
Cdd:COG5640 183 CA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG-GGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                .
gi 84794609 388 G 388
Cdd:COG5640 259 G 259
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
39-132 1.41e-24

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: 96.54  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    39 FLVFDIQVNSNSGQKSSNQLKDLQETNENLVDEIFIDSALNNRYIKNHVVGLTPEEDDTKADIVMVFQPPATGRRTVGKK 118
Cdd:pfam01390   7 FKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEPALDREK 86
                          90
                  ....*....|....
gi 84794609   119 THHSILDQKTRNAR 132
Cdd:pfam01390  87 LIEEILRQTLNNTT 100
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-386 1.70e-99

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: 294.95  E-value: 1.70e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 158 IVSGNPAAKGAWPWQVSLQRSNI-HQCGGTLIGNMWVVTAAHCFRtNSNPRQWTLSFGTT----INPPLMKRDVRRIIMH 232
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHdlssNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQNELREARVQIISNDICKKRH 312
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794609 313 VYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkDTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWIASK 386
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-383 2.63e-96

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: 286.88  E-value: 2.63e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    157 RIVSGNPAAKGAWPWQVSLQRSNI-HQCGGTLIGNMWVVTAAHCFRtNSNPRQWTLSFGTT---INPPLMKRDVRRIIMH 232
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHdlsSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQ-NELREARVQIISNDICKKR 311
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794609    312 HVYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkdTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWI 383
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG--RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
158-383 5.60e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 5.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   158 IVSGNPAAKGAWPWQVSLQ-RSNIHQCGGTLIGNMWVVTAAHCFrtnSNPRQWTLSFGTTI----NPPLMKRDVRRIIMH 232
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNivlrEGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   233 ERYRPPARDHDIALVQFSPRVTFSDEVRRICLPEPSASFPPNSTVYITGFGALYYGGESQNeLREARVQIISNDICKKRh 312
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84794609   313 vYGNEIKRGMFCAGFleGNYDACRGDSGGPLVIRDNkdtwYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWI 383
Cdd:pfam00089 156 -YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
154-388 1.42e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.22  E-value: 1.42e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 154 IANRIVSGNPAAKGAWPWQVSLQRSNI---HQCGGTLIGNMWVVTAAHCFrTNSNPRQWTLSFGTT--INPPLMKRDVRR 228
Cdd:COG5640  27 AAPAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTdlSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 229 IIMHERYRPPARDHDIALVQFSPRVTfsdEVRRICLPEPSASFPPNSTVYITGFGALY-YGGESQNELREARVQIISNDI 307
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 308 CKkrhVYGNEIKRGMFCAGFLEGNYDACRGDSGGPLVIRDNkDTWYLIGIVSWGDNCGQKNKPGVYTQVTYYRHWIASKT 387
Cdd:COG5640 183 CA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDG-GGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                .
gi 84794609 388 G 388
Cdd:COG5640 259 G 259
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
39-132 1.41e-24

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: 96.54  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609    39 FLVFDIQVNSNSGQKSSNQLKDLQETNENLVDEIFIDSALNNRYIKNHVVGLTPEEDDTKADIVMVFQPPATGRRTVGKK 118
Cdd:pfam01390   7 FKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEPALDREK 86
                          90
                  ....*....|....
gi 84794609   119 THHSILDQKTRNAR 132
Cdd:pfam01390  87 LIEEILRQTLNNTT 100
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
183-363 8.73e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 69.32  E-value: 8.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 183 CGGTLIGNMWVVTAAHCF---RTNSNPRQWTLSFGTTiNPPLMKRDVRRIIMHERYRP-PARDHDIALVQFSPRVTfsdE 258
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYN-GGPYGTATATRFRVPPGWVAsGDAGYDYALLRLDEPLG---D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609 259 VRRICLPEPSASFPPNSTVYITGFGAlyyGGESQNELREArvqiisndiCKKRHVYGNEIkrGMFCagflegnyDACRGD 338
Cdd:COG3591  90 TTGWLGLAFNDAPLAGEPVTIIGYPG---DRPKDLSLDCS---------GRVTGVQGNRL--SYDC--------DTTGGS 147
                       170       180
                ....*....|....*....|....*
gi 84794609 339 SGGPlVIRDNKDTWYLIGIVSWGDN 363
Cdd:COG3591 148 SGSP-VLDDSDGGGRVVGVHSAGGA 171
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
185-357 6.90e-04

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.71  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   185 GTLIG-NMWVVTAAHCFRtnsNPRQWTLSFGTTINPPLMKRDVRRIimherYRPParDHDIALVQFSPRVTFSDEVRric 263
Cdd:pfam13365   3 GFVVSsDGLVLTNAHVVD---DAEEAAVELVSVVLADGREYPATVV-----ARDP--DLDLALLRVSGDGRGLPPLP--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794609   264 lPEPSASFPPNSTVYITGFGalyyggesqneLREARVQIISNDICKKRHVYGNEIKRGMF-CAGFLEGnydacrGDSGGP 342
Cdd:pfam13365  70 -LGDSEPLVGGERVYAVGYP-----------LGGEKLSLSEGIVSGVDEGRDGGDDGRVIqTDAALSP------GSSGGP 131
                         170
                  ....*....|....*
gi 84794609   343 LVirDnkDTWYLIGI 357
Cdd:pfam13365 132 VF--D--ADGRVVGI 142
 
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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