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Conserved domains on  [gi|373251166|ref|NP_001243246|]
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transmembrane protease serine 3 isoform 4 [Homo sapiens]

Protein Classification

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 ...
217-446 1.04e-105

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: 313.06  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASPVLNHAAVPLISNKICNHRD 373
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373251166 374 VYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQ 446
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 8.11e-31

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


:

Pssm-ID: 464747  Cd Length: 99  Bit Score: 114.35  E-value: 8.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 373251166  190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 4.67e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.96  E-value: 4.67e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 373251166  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112    3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
217-446 1.04e-105

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: 313.06  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASPVLNHAAVPLISNKICNHRD 373
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373251166 374 VYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQ 446
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
216-443 7.34e-103

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: 305.76  E-value: 7.34e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166   216 RIVGGNMSLLSQWPWQASLQFQG-YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLL-DNPAPSHLVEKIVYH 293
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSsGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166   294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASP-VLNHAAVPLISNKICNHR 372
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373251166   373 DVYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRlWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWI 443
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
214-447 2.60e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.47  E-value: 2.60e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 214 SSRIVGGNMSLLSQWPWQASLQFQG---YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPSHLVEKI 290
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVVKVARI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 291 VYHSKYKPKRLGNDIALMKLAGPLTFnemIQPVCLPNSEENFPDGKVCWTSGWGAT-EDGGDASPVLNHAAVPLISNKIC 369
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373251166 370 NhrdVYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQM 447
Cdd:COG5640  184 A---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
217-443 4.59e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 229.25  E-value: 4.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlylPKSWTIQVG--LVSLLDNPAPSHLVEKIVYH 293
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGahNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGdASPVLNHAAVPLISNKICNHRd 373
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  374 vYGGIISPSMLCAGYltGGVDSCQGDSGGPLVCQERrlwKLVGATSFGIGCAEVNKPGVYTRVTSFLDWI 443
Cdd:pfam00089 156 -YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 8.11e-31

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 114.35  E-value: 8.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 373251166  190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 4.67e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.96  E-value: 4.67e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 373251166  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112    3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
74-104 5.93e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.62  E-value: 5.93e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 373251166    74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDE 104
Cdd:smart00192   4 PGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
108-149 8.55e-06

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 44.26  E-value: 8.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 373251166   108 VR-VGGQNA---VLQVFTAASWKTMCSDDWKGHYANVACAQLGFPS 149
Cdd:smart00202   1 VRlVGGGSPcegRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGG 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
74-107 4.08e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 4.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 373251166   74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:pfam00057   5 PNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
217-446 1.04e-105

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: 313.06  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPS--HLVEKIVYH 293
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGqvIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASPVLNHAAVPLISNKICNHRD 373
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373251166 374 VYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQ 446
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
216-443 7.34e-103

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: 305.76  E-value: 7.34e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166   216 RIVGGNMSLLSQWPWQASLQFQG-YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLL-DNPAPSHLVEKIVYH 293
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSsGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166   294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGDASP-VLNHAAVPLISNKICNHR 372
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373251166   373 DVYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRlWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWI 443
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
214-447 2.60e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.47  E-value: 2.60e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 214 SSRIVGGNMSLLSQWPWQASLQFQG---YHLCGGSVITPLWIITAAHCVYDlYLPKSWTIQVGLVSLLDNPAPSHLVEKI 290
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGTVVKVARI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 291 VYHSKYKPKRLGNDIALMKLAGPLTFnemIQPVCLPNSEENFPDGKVCWTSGWGAT-EDGGDASPVLNHAAVPLISNKIC 369
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373251166 370 NhrdVYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQM 447
Cdd:COG5640  184 A---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
217-443 4.59e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 229.25  E-value: 4.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  217 IVGGNMSLLSQWPWQASLQF-QGYHLCGGSVITPLWIITAAHCVYDlylPKSWTIQVG--LVSLLDNPAPSHLVEKIVYH 293
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSG---ASDVKVVLGahNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  294 SKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGGdASPVLNHAAVPLISNKICNHRd 373
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  374 vYGGIISPSMLCAGYltGGVDSCQGDSGGPLVCQERrlwKLVGATSFGIGCAEVNKPGVYTRVTSFLDWI 443
Cdd:pfam00089 156 -YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
112-210 8.11e-31

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 114.35  E-value: 8.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  112 GQNAVLQVFTAA--SWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSidhLLPDDKVTALHHSVY 189
Cdd:pfam15494   1 GENFLLQVYSSArpSWLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSNSSQSFMK---LNSSSLNTDLYEALQ 77
                          90       100
                  ....*....|....*....|.
gi 373251166  190 VREGCASGHVVTLQCTACGHR 210
Cdd:pfam15494  78 PRDSCSSGSVVSLRCSECGLR 98
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
238-449 1.36e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 238 GYHLCGGSVITPLWIITAAHCVYDLY---LPKSWTIQVGlvsLLDNPAPSHLVEKIVYHSKYKPK-RLGNDIALMKLAGP 313
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggWATNIVFVPG---YNGGPYGTATATRFRVPPGWVASgDAGYDYALLRLDEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166 314 LTFNEMIQPvcLPNSEENFPDGKVcWTSGWGAtedGGDASPVLNHAavplisnkiCNHRDVYGGIIspSMLCagyltggv 393
Cdd:COG3591   87 LGDTTGWLG--LAFNDAPLAGEPV-TIIGYPG---DRPKDLSLDCS---------GRVTGVQGNRL--SYDC-------- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 373251166 394 DSCQGDSGGPLVCQERRLWKLVGATSFGIgcAEVNKPGVYTRvTSFLDWIHEQMER 449
Cdd:COG3591  142 DTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVRLT-SAIVAALRAWASA 194
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
74-107 4.67e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 42.96  E-value: 4.67e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 373251166  74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:cd00112    3 PNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
74-104 5.93e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.62  E-value: 5.93e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 373251166    74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDE 104
Cdd:smart00192   4 PGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
108-149 8.55e-06

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 44.26  E-value: 8.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 373251166   108 VR-VGGQNA---VLQVFTAASWKTMCSDDWKGHYANVACAQLGFPS 149
Cdd:smart00202   1 VRlVGGGSPcegRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGG 46
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
228-342 1.44e-05

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: 44.08  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373251166  228 WPWQASLQFQGYHLCGGSVITPLWIITAAHCVYDLYLPKSWTIQV--GLVSLLDNPAPSHLVEKI-VYHSKYKPKrlgnd 304
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlgGAKTLKSIEGPYEQIVRVdCRHDIPESE----- 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 373251166  305 IALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSG 342
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
74-107 4.08e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 4.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 373251166   74 SGKYRCRSSfKCIELIARCDGVSDCKDGEDEYRC 107
Cdd:pfam00057   5 PNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
117-153 5.30e-03

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 36.20  E-value: 5.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 373251166  117 LQVFTAASWKTMCSDDWKGHYANVACAQLGFPSYVSS 153
Cdd:pfam00530   9 VEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSA 45
 
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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