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Conserved domains on  [gi|205360943|ref|NP_005647|]
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transmembrane protease serine 2 isoform 2 [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 ...
256-487 1.23e-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: 293.80  E-value: 1.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 256 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 334 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205360943 414 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
153-246 1.80e-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: 145.94  E-value: 1.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  153 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 205360943  230 ACSSKAVVSLRCIACGV 246
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
113-148 1.69e-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: 1.69e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 205360943 113 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 148
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 ...
256-487 1.23e-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: 293.80  E-value: 1.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 256 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 334 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205360943 414 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
255-484 2.05e-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: 288.04  E-value: 2.05e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   255 RIVGGESALPGAWPWQVSLHVQN-VHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGILRQSFMFYGAGYQVEKVIS 333
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   334 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQRCNS 412
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205360943   413 RYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTsKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 484
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
253-492 8.56e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 8.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 253 QSRIVGGESALPGAWPWQVSLHVQN---VHVCGGSIITPEWIVTAAHCVEKPlnNPWHWTAFAGILRQSfMFYGAGYQVE 329
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 330 KVISHPNYDSKTKNNDIALMKLQKPLTfndLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQ 408
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 409 RCNSryvYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQM 488
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ....
gi 205360943 489 RADG 492
Cdd:COG5640  259 GGLG 262
Trypsin pfam00089
Trypsin;
256-484 2.18e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.07  E-value: 2.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  256 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEkplnNPWHWTAFAGI----LRQSFMFYGagyQVEK 330
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAhnivLREGGEQKF---DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  331 VISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGkTSEVLNAAKVLLIETQRC 410
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205360943  411 NSRyvYDNLITPAMICAGFlqGNVDSCQGDSGGPLVTSKNniwWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 484
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 ...
153-246 1.80e-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: 145.94  E-value: 1.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  153 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 205360943  230 ACSSKAVVSLRCIACGV 246
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
149-241 5.40e-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: 53.50  E-value: 5.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   149 VRLYGPNF----ILQVYSSQRksWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTS-AGN----V 219
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 205360943   220 DIYKKLYHSDACSSKAVVSLRC 241
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
113-148 1.69e-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: 1.69e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 205360943 113 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 148
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
112-145 3.41e-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: 3.41e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 205360943   112 KCSNSGIECDSsGTCINPSNWCDGVSHCPGGEDE 145
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 ...
256-487 1.23e-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: 293.80  E-value: 1.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 256 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGIL-RQSFMFYGAGYQVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 334 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSR 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205360943 414 YVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
255-484 2.05e-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: 288.04  E-value: 2.05e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   255 RIVGGESALPGAWPWQVSLHVQN-VHVCGGSIITPEWIVTAAHCVEKplNNPWHWTAFAGILRQSFMFYGAGYQVEKVIS 333
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   334 HPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQRCNS 412
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205360943   413 RYVYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTsKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 484
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
253-492 8.56e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 8.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 253 QSRIVGGESALPGAWPWQVSLHVQN---VHVCGGSIITPEWIVTAAHCVEKPlnNPWHWTAFAGILRQSfMFYGAGYQVE 329
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 330 KVISHPNYDSKTKNNDIALMKLQKPLTfndLVKPVCLPNPGMMLQPEQLCWISGWGATEE-KGKTSEVLNAAKVLLIETQ 408
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 409 RCNSryvYDNLITPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQM 488
Cdd:COG5640  182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                 ....
gi 205360943 489 RADG 492
Cdd:COG5640  259 GGLG 262
Trypsin pfam00089
Trypsin;
256-484 2.18e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.07  E-value: 2.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  256 IVGGESALPGAWPWQVSLHV-QNVHVCGGSIITPEWIVTAAHCVEkplnNPWHWTAFAGI----LRQSFMFYGagyQVEK 330
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAhnivLREGGEQKF---DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  331 VISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGkTSEVLNAAKVLLIETQRC 410
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205360943  411 NSRyvYDNLITPAMICAGFlqGNVDSCQGDSGGPLVTSKNniwWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWI 484
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 ...
153-246 1.80e-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: 145.94  E-value: 1.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  153 GPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNN-FYSSQGIVDDSG--STSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*..
gi 205360943  230 ACSSKAVVSLRCIACGV 246
Cdd:pfam15494  81 SCSSGSVVSLRCSECGL 97
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
279-490 6.12e-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: 6.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 279 HVCGGSIITPEWIVTAAHCVEKPLNNPWH--WTAFAGILRQSFmfygAGYQVEKVISHPNYDSKTK-NNDIALMKLQKPL 355
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWAtnIVFVPGYNGGPY----GTATATRFRVPPGWVASGDaGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943 356 TfnDLVKPVCLPNPGMMLQPEQLcWISGWGATEEKgktsevlnaakvllIETQRCNSRYVYDNlitpamicAGFLQGNVD 435
Cdd:COG3591   88 G--DTTGWLGLAFNDAPLAGEPV-TIIGYPGDRPK--------------DLSLDCSGRVTGVQ--------GNRLSYDCD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 205360943 436 SCQGDSGGPLVTSKNNIWWLIGDTSWGSgcAKAYRPGVYgnvmvFTDWIYRQMRA 490
Cdd:COG3591  143 TTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVR-----LTSAIVAALRA 190
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
149-241 5.40e-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: 53.50  E-value: 5.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943   149 VRLYGPNF----ILQVYSSQRksWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFMKLNTS-AGN----V 219
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 205360943   220 DIYKKLYHSDACSSKAVVSLRC 241
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
113-148 1.69e-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: 1.69e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 205360943 113 CSNSGIECDSsGTCINPSNWCDGVSHCPGGEDENRC 148
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
112-145 3.41e-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: 3.41e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 205360943   112 KCSNSGIECDSsGTCINPSNWCDGVSHCPGGEDE 145
Cdd:smart00192   1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
267-379 5.47e-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: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205360943  267 WPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKV-ISHPNYDSKtknnd 345
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAKTLKSIEGPYEQIVRVdCRHDIPESE----- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 205360943  346 IALMKLQKPLTFNDLVKPVCLPNPGMMLQPEQLC 379
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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