NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|34328226|ref|NP_056590|]
View 

transmembrane protease serine 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
254-485 3.06e-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: 298.04  E-value: 3.06e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 254 IVGGLNASPGDWPWQVSLHV-QGVHVCGGSIITPEWIVTAAHCVEEplSSPRYWTAFAGIL-RQSLMFYGSRHQVEKVIS 331
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGKTSDVLNAAMVPLIEPSKCNSK 411
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328226 412 YIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQ 485
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
152-247 2.17e-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: 2.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   152 GQSFILQVYSSQRKAWYPVCQDDWSESYGRAACKDMGYKNN-FYSSQGIPDQSG--ATSFMKLNVSSGNVDLYKKLYHSD 228
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 34328226   229 SCSSRMVVSLRCIECGVRS 247
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
112-147 4.27e-08

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: 49.13  E-value: 4.27e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 34328226 112 CSTSEMECGSsGTCISSSLWCDGVAHCPNGEDENRC 147
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 ...
254-485 3.06e-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: 298.04  E-value: 3.06e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 254 IVGGLNASPGDWPWQVSLHV-QGVHVCGGSIITPEWIVTAAHCVEEplSSPRYWTAFAGIL-RQSLMFYGSRHQVEKVIS 331
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGKTSDVLNAAMVPLIEPSKCNSK 411
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328226 412 YIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQ 485
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
253-482 8.61e-97

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 291.50  E-value: 8.61e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    253 RIVGGLNASPGDWPWQVSLHVQG-VHVCGGSIITPEWIVTAAHCVEEplSSPRYWTAFAGILRQSLMFYGSRHQVEKVIS 331
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGAT-YEKGKTSDVLNAAMVPLIEPSKCNS 410
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328226    411 KYIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTlKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWI 482
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
251-490 7.24e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 7.24e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 251 QSRIVGGLNASPGDWPWQVSLHVQG---VHVCGGSIITPEWIVTAAHCVEEPlsSPRYWTAFAGILRQSlMFYGSRHQVE 327
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 328 KVISHPNYDSKTKNNDIALMKLQTPLafnDLVKPVCLPNPGMMLDLDQECWISGWGATYE-KGKTSDVLNAAMVPLIEPS 406
Cdd:COG5640 105 RIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 407 KCNSkyiYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQM 486
Cdd:COG5640 182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                ....
gi 34328226 487 RANS 490
Cdd:COG5640 259 GGLG 262
Trypsin pfam00089
Trypsin;
254-482 6.48e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 6.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   254 IVGGLNASPGDWPWQVSLHV-QGVHVCGGSIITPEWIVTAAHCVEEPLSspryWTAFAGILRQSLMFYGSRH-QVEKVIS 331
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKfDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGkTSDVLNAAMVPLIEPSKCNSK 411
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328226   412 yiYNNLITPAMICAGFlqGSVDSCQGDSGGPLVTLKNgiwWLIGDTSWGSGCAKALRPGVYGNVTVFTDWI 482
Cdd:pfam00089 156 --YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
152-247 2.17e-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: 2.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   152 GQSFILQVYSSQRKAWYPVCQDDWSESYGRAACKDMGYKNN-FYSSQGIPDQSG--ATSFMKLNVSSGNVDLYKKLYHSD 228
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 34328226   229 SCSSRMVVSLRCIECGVRS 247
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
148-240 9.49e-12

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: 61.20  E-value: 9.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    148 VRLYGQSF----ILQVYSSQRkaWYPVCQDDWSESYGRAACKDMGYKNNFYSSQGIPDQSGATSFMKLNVS-SGN----V 218
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 34328226    219 DLYKKLYHSDSCSSRMVVSLRC 240
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
112-147 4.27e-08

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: 49.13  E-value: 4.27e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 34328226 112 CSTSEMECGSsGTCISSSLWCDGVAHCPNGEDENRC 147
Cdd:cd00112   1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
112-144 1.20e-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: 44.93  E-value: 1.20e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 34328226    112 CSTSEMECGSsGTCISSSLWCDGVAHCPNGEDE 144
Cdd:smart00192   2 CPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
110-147 2.27e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 2.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 34328226   110 SNCSTSEMECGSsGTCISSSLWCDGVAHCPNGEDENRC 147
Cdd:pfam00057   1 STCSPNEFQCGS-GECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
254-485 3.06e-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: 298.04  E-value: 3.06e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 254 IVGGLNASPGDWPWQVSLHV-QGVHVCGGSIITPEWIVTAAHCVEEplSSPRYWTAFAGIL-RQSLMFYGSRHQVEKVIS 331
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHdLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGKTSDVLNAAMVPLIEPSKCNSK 411
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34328226 412 YIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQ 485
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
253-482 8.61e-97

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 291.50  E-value: 8.61e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    253 RIVGGLNASPGDWPWQVSLHVQG-VHVCGGSIITPEWIVTAAHCVEEplSSPRYWTAFAGILRQSLMFYGSRHQVEKVIS 331
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGAT-YEKGKTSDVLNAAMVPLIEPSKCNS 410
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34328226    411 KYIYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTlKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWI 482
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
251-490 7.24e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 7.24e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 251 QSRIVGGLNASPGDWPWQVSLHVQG---VHVCGGSIITPEWIVTAAHCVEEPlsSPRYWTAFAGILRQSlMFYGSRHQVE 327
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLS-TSGGTVVKVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 328 KVISHPNYDSKTKNNDIALMKLQTPLafnDLVKPVCLPNPGMMLDLDQECWISGWGATYE-KGKTSDVLNAAMVPLIEPS 406
Cdd:COG5640 105 RIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 407 KCNSkyiYNNLITPAMICAGFLQGSVDSCQGDSGGPLVTLKNGIWWLIGDTSWGSGCAKALRPGVYGNVTVFTDWIYQQM 486
Cdd:COG5640 182 TCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                ....
gi 34328226 487 RANS 490
Cdd:COG5640 259 GGLG 262
Trypsin pfam00089
Trypsin;
254-482 6.48e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 6.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   254 IVGGLNASPGDWPWQVSLHV-QGVHVCGGSIITPEWIVTAAHCVEEPLSspryWTAFAGILRQSLMFYGSRH-QVEKVIS 331
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKfDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   332 HPNYDSKTKNNDIALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQECWISGWGATYEKGkTSDVLNAAMVPLIEPSKCNSK 411
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34328226   412 yiYNNLITPAMICAGFlqGSVDSCQGDSGGPLVTLKNgiwWLIGDTSWGSGCAKALRPGVYGNVTVFTDWI 482
Cdd:pfam00089 156 --YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
152-247 2.17e-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: 2.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   152 GQSFILQVYSSQRKAWYPVCQDDWSESYGRAACKDMGYKNN-FYSSQGIPDQSG--ATSFMKLNVSSGNVDLYKKLYHSD 228
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLtHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 34328226   229 SCSSRMVVSLRCIECGVRS 247
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
148-240 9.49e-12

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: 61.20  E-value: 9.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226    148 VRLYGQSF----ILQVYSSQRkaWYPVCQDDWSESYGRAACKDMGYKNNFYSSQGIPDQSGATSFMKLNVS-SGN----V 218
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 34328226    219 DLYKKLYHSDSCSSRMVVSLRC 240
Cdd:smart00202  79 DCPHSGWGSHNCSHGEDAGVVC 100
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
275-488 2.75e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.61  E-value: 2.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 275 GVHVCGGSIITPEWIVTAAHCVEEPLS--SPRYWTAFAGILRQSlmfYGSrHQVEKVISHPNYDSKTK-NNDIALMKLQT 351
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYDGAGggWATNIVFVPGYNGGP---YGT-ATATRFRVPPGWVASGDaGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226 352 PLAfnDLVKPVCLPNPGMMLDlDQECWISGWGATYEKGKTSDvlnaamvpliepskCNSKYIYNNlitpamicAGFLQGS 431
Cdd:COG3591  86 PLG--DTTGWLGLAFNDAPLA-GEPVTIIGYPGDRPKDLSLD--------------CSGRVTGVQ--------GNRLSYD 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34328226 432 VDSCQGDSGGPLVTLKNGIWWLIGDTSWGSgcakalrPGVYGNVTVFTDWIYQQMRA 488
Cdd:COG3591 141 CDTTGGSSGSPVLDDSDGGGRVVGVHSAGG-------ADRANTGVRLTSAIVAALRA 190
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
112-147 4.27e-08

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: 49.13  E-value: 4.27e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 34328226 112 CSTSEMECGSsGTCISSSLWCDGVAHCPNGEDENRC 147
Cdd:cd00112   1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
265-377 6.70e-07

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: 47.93  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34328226   265 WPWQVSLHVQGVHVCGGSIITPEWIVTAAHCVEEPLSSPRYWTAFAGILRQSLMFYGSRHQVEKV-ISHPNYDSKtknnd 343
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAKTLKSIEGPYEQIVRVdCRHDIPESE----- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 34328226   344 IALMKLQTPLAFNDLVKPVCLPNPGMMLDLDQEC 377
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
112-144 1.20e-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: 44.93  E-value: 1.20e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 34328226    112 CSTSEMECGSsGTCISSSLWCDGVAHCPNGEDE 144
Cdd:smart00192   2 CPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
110-147 2.27e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 2.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 34328226   110 SNCSTSEMECGSsGTCISSSLWCDGVAHCPNGEDENRC 147
Cdd:pfam00057   1 STCSPNEFQCGS-GECIPRSWVCDGDPDCGDGSDEENC 37
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH