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Conserved domains on  [gi|227499990|ref|NP_001128571|]
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transmembrane protease serine 2 isoform 1 [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 ...
293-524 1.44e-97

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: 1.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 293 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 370
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 371 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 450
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499990 451 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 524
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
190-283 1.96e-42

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: 146.71  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  190 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 266
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 227499990  267 ACSSKAVVSLRCIACGV 283
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
150-185 1.65e-05

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: 41.81  E-value: 1.65e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 227499990 150 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 185
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
293-524 1.44e-97

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: 1.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 293 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 370
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 371 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 450
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499990 451 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 524
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
292-521 2.45e-95

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: 289.19  E-value: 2.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   292 RIVGGESALPGAWPWQVSLHVQN-VHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGILRQSFMFYGAGYQVEKVIS 370
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   371 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQRCNS 449
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227499990   450 RYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTsKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 521
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
290-529 2.46e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 2.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 290 QSRIVGGESALPGAWPWQVSLHVQN---VHVCGGSIITPEWIVTAAHCVEKPlnNPWHWTAFAGILRQSfMFYGAGYQVE 366
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 367 KVISHPNYDSKTKNNDIALMKLQKPLTfndLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQ 445
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 446 RCNSryvYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQM 525
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ....
gi 227499990 526 RADG 529
Cdd:COG5640  259 GGLG 262
Trypsin pfam00089
Trypsin;
293-521 2.36e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 2.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  293 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEkplnNPWHWTAFAGI----LRQSFMFYGagyQVEK 367
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAhnivLREGGEQKF---DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  368 VISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGkTSEVLNAAKVLLIETQRC 447
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499990  448 NSRyvYDNLITPAMICAGFlqGNVDSCQGDSGGPLVTSKNniwWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 521
Cdd:pfam00089 153 RSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
190-283 1.96e-42

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: 146.71  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  190 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 266
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 227499990  267 ACSSKAVVSLRCIACGV 283
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
186-278 4.91e-09

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: 53.89  E-value: 4.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   186 VRLYGPNF----ILQVYSSQRksWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTS-AGN----V 256
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 227499990   257 DIYKKLYHSDACSSKAVVSLRC 278
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
150-185 1.65e-05

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: 41.81  E-value: 1.65e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 227499990 150 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 185
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
149-182 3.39e-05

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: 40.69  E-value: 3.39e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 227499990   149 KCSNSGIECDSsGTCINPSNWCDGVSHCPGGEDE 182
Cdd:smart00192   1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
293-524 1.44e-97

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: 1.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 293 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 370
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 371 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 450
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499990 451 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 524
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
292-521 2.45e-95

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: 289.19  E-value: 2.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   292 RIVGGESALPGAWPWQVSLHVQN-VHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGILRQSFMFYGAGYQVEKVIS 370
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   371 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQRCNS 449
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227499990   450 RYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTsKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 521
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
290-529 2.46e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 2.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 290 QSRIVGGESALPGAWPWQVSLHVQN---VHVCGGSIITPEWIVTAAHCVEKPlnNPWHWTAFAGILRQSfMFYGAGYQVE 366
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 367 KVISHPNYDSKTKNNDIALMKLQKPLTfndLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQ 445
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 446 RCNSryvYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQM 525
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ....
gi 227499990 526 RADG 529
Cdd:COG5640  259 GGLG 262
Trypsin pfam00089
Trypsin;
293-521 2.36e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 2.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  293 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEkplnNPWHWTAFAGI----LRQSFMFYGagyQVEK 367
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAhnivLREGGEQKF---DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  368 VISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGkTSEVLNAAKVLLIETQRC 447
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499990  448 NSRyvYDNLITPAMICAGFlqGNVDSCQGDSGGPLVTSKNniwWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 521
Cdd:pfam00089 153 RSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
190-283 1.96e-42

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: 146.71  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  190 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 266
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 227499990  267 ACSSKAVVSLRCIACGV 283
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
316-527 6.74e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 64.70  E-value: 6.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 316 HVCGGSIITPEWIVTAAHCVEKPLNNPWH--WTAFAGILRQSFmfygAGYQVEKVISHPNYDSKTK-NNDIALMKLQKPL 392
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWAtnIVFVPGYNGGPY----GTATATRFRVPPGWVASGDaGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990 393 TfnDLVKPVCLPNPGMMLQPEQLcWISGWGATEEKgktsevlnaakvllIETQRCNSRYVYDNlitpamicAGFLQGNVD 472
Cdd:COG3591   88 G--DTTGWLGLAFNDAPLAGEPV-TIIGYPGDRPK--------------DLSLDCSGRVTGVQ--------GNRLSYDCD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 227499990 473 SCQGDSGGPLVTSKNNIWWLIGDTSWGSgcAKAYRPGVYgnvmvFTDWIYRQMRA 527
Cdd:COG3591  143 TTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVR-----LTSAIVAALRA 190
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
186-278 4.91e-09

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: 53.89  E-value: 4.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990   186 VRLYGPNF----ILQVYSSQRksWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTS-AGN----V 256
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 227499990   257 DIYKKLYHSDACSSKAVVSLRC 278
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
150-185 1.65e-05

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: 41.81  E-value: 1.65e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 227499990 150 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 185
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
149-182 3.39e-05

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: 40.69  E-value: 3.39e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 227499990   149 KCSNSGIECDSsGTCINPSNWCDGVSHCPGGEDE 182
Cdd:smart00192   1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
304-416 5.76e-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: 36.76  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499990  304 WPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKV-ISHPNYDSKtknnd 382
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAKTLKSIEGPYEQIVRVdCRHDIPESE----- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 227499990  383 IALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLC 416
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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