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Conserved domains on  [gi|966931275|ref|XP_014988331|]
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transmembrane protease serine 2 isoform X3 [Macaca mulatta]

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 1.86e-100

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: 301.12  E-value: 1.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 256 IVGGQNALLGAWPWQVSLHVQNI-HVCGGSIITPEWIVTAAHCVEKplNSPWQWTAFVGTLRQSSM-FYEKGHRVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNeGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQEKGKTSDVLNAAMVPLIEPRRCNNK 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966931275 414 YVYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTLKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
153-248 6.70e-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: 144.78  E-value: 6.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  153 GPNFILQVYSSQRKSWHPVCRDDWNENYARAACRDMGY-KNSFYSSQGIVDNSG--ATSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYlRLTHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 966931275  230 ACSSKAVVSLRCIACGVRS 248
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
113-148 1.24e-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: 44.89  E-value: 1.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966931275 113 CSDSGIECDSsGTCISSSNWCDGVSHCPNGEDENRC 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 1.86e-100

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: 301.12  E-value: 1.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 256 IVGGQNALLGAWPWQVSLHVQNI-HVCGGSIITPEWIVTAAHCVEKplNSPWQWTAFVGTLRQSSM-FYEKGHRVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNeGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQEKGKTSDVLNAAMVPLIEPRRCNNK 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966931275 414 YVYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTLKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
255-484 3.61e-99

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: 297.67  E-value: 3.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   255 RIVGGQNALLGAWPWQVSLHVQNI-HVCGGSIITPEWIVTAAHCVEKPLNSpwQWTAFVGTLRQSSMFYEKGHRVEKVIS 333
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPS--NIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQE-KGKTSDVLNAAMVPLIEPRRCNN 412
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966931275   413 KYVYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTlKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWI 484
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
253-490 3.65e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 232.23  E-value: 3.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 253 QSRIVGGQNALLGAWPWQVSLHVQNI---HVCGGSIITPEWIVTAAHCVEKPlnSPWQWTAFVGTLRQSSmfyEKG--HR 327
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLST---SGGtvVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 328 VEKVISHPNYDSKTKNNDIALMKLHTPLTFnevVKPVCLPNPGMMLEPEQHCWISGWGATQE-KGKTSDVLNAAMVPLIE 406
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 407 PRRCNNkyvYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTLKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWIYR 486
Cdd:COG5640  180 DATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256

                 ....
gi 966931275 487 QMRA 490
Cdd:COG5640  257 TAGG 260
Trypsin pfam00089
Trypsin;
256-484 8.72e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 8.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  256 IVGGQNALLGAWPWQVSLHV-QNIHVCGGSIITPEWIVTAAHCVEkplnSPWQWTAFVGTLRQSSMFYEKGHR-VEKVIS 333
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAHNIVLREGGEQKFdVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQEKGkTSDVLNAAMVPLIEPRRCNNk 413
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966931275  414 yVYDGLITPAMICAGFlqGTVDSCQGDSGGPLVTLKNDvwwLIGDTSWGSGCAQANRPGVYGNVTVFTDWI 484
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
153-248 6.70e-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: 144.78  E-value: 6.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  153 GPNFILQVYSSQRKSWHPVCRDDWNENYARAACRDMGY-KNSFYSSQGIVDNSG--ATSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYlRLTHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 966931275  230 ACSSKAVVSLRCIACGVRS 248
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
149-241 6.62e-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: 53.11  E-value: 6.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   149 VRLYGPNF----ILQVYSSQRksWHPVCRDDWNENYARAACRDMGYKNSFYSSQGIVDNSGATSFMKLNTS-AGN----V 219
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 966931275   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 1.24e-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: 44.89  E-value: 1.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966931275 113 CSDSGIECDSsGTCISSSNWCDGVSHCPNGEDENRC 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 1.07e-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: 42.24  E-value: 1.07e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 966931275   112 KCSDSGIECDSsGTCISSSNWCDGVSHCPNGEDE 145
Cdd:smart00192   1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
111-148 5.50e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 5.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966931275  111 SKCSDSGIECdSSGTCISSSNWCDGVSHCPNGEDENRC 148
Cdd:pfam00057   1 STCSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
256-487 1.86e-100

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: 301.12  E-value: 1.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 256 IVGGQNALLGAWPWQVSLHVQNI-HVCGGSIITPEWIVTAAHCVEKplNSPWQWTAFVGTLRQSSM-FYEKGHRVEKVIS 333
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNeGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQEKGKTSDVLNAAMVPLIEPRRCNNK 413
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966931275 414 YVYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTLKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWIYRQ 487
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
255-484 3.61e-99

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: 297.67  E-value: 3.61e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   255 RIVGGQNALLGAWPWQVSLHVQNI-HVCGGSIITPEWIVTAAHCVEKPLNSpwQWTAFVGTLRQSSMFYEKGHRVEKVIS 333
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPS--NIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQE-KGKTSDVLNAAMVPLIEPRRCNN 412
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966931275   413 KYVYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTlKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWI 484
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
253-490 3.65e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 232.23  E-value: 3.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 253 QSRIVGGQNALLGAWPWQVSLHVQNI---HVCGGSIITPEWIVTAAHCVEKPlnSPWQWTAFVGTLRQSSmfyEKG--HR 327
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDLST---SGGtvVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 328 VEKVISHPNYDSKTKNNDIALMKLHTPLTFnevVKPVCLPNPGMMLEPEQHCWISGWGATQE-KGKTSDVLNAAMVPLIE 406
Cdd:COG5640  103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 407 PRRCNNkyvYDGLITPAMICAGFLQGTVDSCQGDSGGPLVTLKNDVWWLIGDTSWGSGCAQANRPGVYGNVTVFTDWIYR 486
Cdd:COG5640  180 DATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256

                 ....
gi 966931275 487 QMRA 490
Cdd:COG5640  257 TAGG 260
Trypsin pfam00089
Trypsin;
256-484 8.72e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.24  E-value: 8.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  256 IVGGQNALLGAWPWQVSLHV-QNIHVCGGSIITPEWIVTAAHCVEkplnSPWQWTAFVGTLRQSSMFYEKGHR-VEKVIS 333
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAHNIVLREGGEQKFdVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  334 HPNYDSKTKNNDIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHCWISGWGATQEKGkTSDVLNAAMVPLIEPRRCNNk 413
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966931275  414 yVYDGLITPAMICAGFlqGTVDSCQGDSGGPLVTLKNDvwwLIGDTSWGSGCAQANRPGVYGNVTVFTDWI 484
Cdd:pfam00089 155 -AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
153-248 6.70e-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: 144.78  E-value: 6.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  153 GPNFILQVYSSQRKSWHPVCRDDWNENYARAACRDMGY-KNSFYSSQGIVDNSG--ATSFMKLNTSAGNVDIYKKLYHSD 229
Cdd:pfam15494   1 GENFLLQVYSSARPSWLPVCSDDWNPAYGRAACQQLGYlRLTHHKSVNLTDISSnsSQSFMKLNSSSLNTDLYEALQPRD 80
                          90
                  ....*....|....*....
gi 966931275  230 ACSSKAVVSLRCIACGVRS 248
Cdd:pfam15494  81 SCSSGSVVSLRCSECGLRS 99
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
279-490 8.07e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.15  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 279 HVCGGSIITPEWIVTAAHCVEKPLNSPWQWTAFVGTLRQSSMFyeKGHRVEKVISHPNYDSKTK-NNDIALMKLHTPLTf 357
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPY--GTATATRFRVPPGWVASGDaGYDYALLRLDEPLG- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275 358 nEVVKPVCLpNPGMMLEPEQHCWISGWGATQekgktsdvlnaamvPLIEPRRCNNKYVYDGlitpamicAGFLQGTVDSC 437
Cdd:COG3591   89 -DTTGWLGL-AFNDAPLAGEPVTIIGYPGDR--------------PKDLSLDCSGRVTGVQ--------GNRLSYDCDTT 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966931275 438 QGDSGGPLVTLKNDVWWLIGDTSWGsGCAQANRpGVYgnvtvFTDWIYRQMRA 490
Cdd:COG3591  145 GGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVR-----LTSAIVAALRA 190
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
149-241 6.62e-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: 53.11  E-value: 6.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275   149 VRLYGPNF----ILQVYSSQRksWHPVCRDDWNENYARAACRDMGYKNSFYSSQGIVDNSGATSFMKLNTS-AGN----V 219
Cdd:smart00202   1 VRLVGGGSpcegRVEVYHNGQ--WGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRcSGTeaslS 78
                           90       100
                   ....*....|....*....|..
gi 966931275   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 1.24e-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: 44.89  E-value: 1.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966931275 113 CSDSGIECDSsGTCISSSNWCDGVSHCPNGEDENRC 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 1.07e-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: 42.24  E-value: 1.07e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 966931275   112 KCSDSGIECDSsGTCISSSNWCDGVSHCPNGEDE 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 3.91e-04

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: 40.22  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966931275  267 WPWQVSLHVQNIHVCGGSIITPEWIVTAAHCVeKPLNSPWQWTAFV----GTLRQSSMFYEKGHRVEkvISHPNYDSKtk 342
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCL-RDTNLRHQYISVVlggaKTLKSIEGPYEQIVRVD--CRHDIPESE-- 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 966931275  343 nndIALMKLHTPLTFNEVVKPVCLPNPGMMLEPEQHC 379
Cdd:pfam09342  76 ---ISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
111-148 5.50e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 5.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966931275  111 SKCSDSGIECdSSGTCISSSNWCDGVSHCPNGEDENRC 148
Cdd:pfam00057   1 STCSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 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.
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