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Conserved domains on  [gi|149065992|gb|EDM15865|]
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transmembrane serine protease 6 (predicted), isoform CRA_a [Rattus norvegicus]

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 ...
 577-771 1.94e-84

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: 267.61  E-value: 1.94e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 577 IVGGAMSSEGEWPWQASLQIR-GRHICGGALIADRWVITAAHCFQEdsmASPRLWTVFLGKMRQNSRWPGEVSFKVSRLF 655
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 656 LHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPGSSTLQKVDVQLIPQDLCNE 735
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 149065992 736 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKEP 771
Cdd:cd00190  158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN 195
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
529-566 6.07e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 6.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149065992  529 VPCGTFTFQCEDRSCVKKpNPECDGQADCRDGSDEEHC 566
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 495-525 3.91e-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: 44.12  E-value: 3.91e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 149065992 495 FQCQeDSTCISLPRVCDRQPDCLNGSDEEQC 525
Cdd:cd00112    6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 459-489 4.99e-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: 43.73  E-value: 4.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 149065992 459 PGEFLCSvNGLCVPA---CDGIKDCPNGLDERNC 489
Cdd:cd00112    3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-182 1.01e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.92  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   88 QVYSGSLRVLNRHFSQDLARRESIAFRTETAKAQKMFQELVASTRLGTYYNSSSIYAF--GEGPLICFFWFILDIPeyqr 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76

                          90
                  ....*....|....*..
gi 149065992  166 lTLSPEVVRELLVGELL 182
Cdd:pfam01390  77 -STEPALDREKLIEEIL 92
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 577-771 1.94e-84

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: 267.61  E-value: 1.94e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 577 IVGGAMSSEGEWPWQASLQIR-GRHICGGALIADRWVITAAHCFQEdsmASPRLWTVFLGKMRQNSRWPGEVSFKVSRLF 655
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 656 LHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPGSSTLQKVDVQLIPQDLCNE 735
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 149065992 736 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKEP 771
Cdd:cd00190  158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN 195
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 576-772 4.33e-78

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: 250.67  E-value: 4.33e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   576 RIVGGAMSSEGEWPWQASLQIRG-RHICGGALIADRWVITAAHCFQEDSmasPRLWTVFLGKMRQNSRWPGEVsFKVSRL 654
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD---PSNIRVRLGSHDLSSGEEGQV-IKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   655 FLHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREG-GPGSSTLQKVDVQLIPQDLC 733
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 149065992   734 NEAYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKEPR 772
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR 197
Trypsin pfam00089
Trypsin;
577-769 1.20e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992  577 IVGGAMSSEGEWPWQASLQIR-GRHICGGALIADRWVITAAHCFqedsmASPRLWTVFLGKMRQNSRWPGEVSFKVSRLF 655
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992  656 LHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPgSSTLQKVDVQLIPQDLCNE 735
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 149065992  736 AYRYQVTPRMLCAGYrkGKKDACQGDSGGPLVCK 769
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCS 186
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 568-767 9.28e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 9.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 568 CGLQGPSSRIVGGAMSSEGEWPWQASLQIRG---RHICGGALIADRWVITAAHCFQEDSMASprlWTVFLGKMRQNSRwP 644
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLSTS-G 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 645 GEVSfKVSRLFLHPYHEEDSHDYDVALLQLDHPVvysATVRPVCLPARSHFFEPGQHCWITGWGAQREG-GPGSSTLQKV 723
Cdd:COG5640   98 GTVV-KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 149065992 724 DVQLIPQDLCNeAYRYQVTPRMLCAGYRKGKKDACQGDSGGPLV 767
Cdd:COG5640  174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV 216
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
529-566 6.07e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 6.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149065992  529 VPCGTFTFQCEDRSCVKKpNPECDGQADCRDGSDEEHC 566
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 531-566 7.60e-07

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: 46.05  E-value: 7.60e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 149065992 531 CGTFTFQCEDRSCVKKpNPECDGQADCRDGSDEEHC 566
Cdd:cd00112    1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 495-525 3.91e-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: 44.12  E-value: 3.91e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 149065992 495 FQCQeDSTCISLPRVCDRQPDCLNGSDEEQC 525
Cdd:cd00112    6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 459-489 4.99e-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: 43.73  E-value: 4.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 149065992 459 PGEFLCSvNGLCVPA---CDGIKDCPNGLDERNC 489
Cdd:cd00112    3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
495-525 7.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.39  E-value: 7.05e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 149065992  495 FQCQeDSTCISLPRVCDRQPDCLNGSDEEQC 525
Cdd:pfam00057   8 FQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-182 1.01e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.92  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   88 QVYSGSLRVLNRHFSQDLARRESIAFRTETAKAQKMFQELVASTRLGTYYNSSSIYAF--GEGPLICFFWFILDIPeyqr 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76

                          90
                  ....*....|....*..
gi 149065992  166 lTLSPEVVRELLVGELL 182
Cdd:pfam01390  77 -STEPALDREKLIEEIL 92
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 495-522 2.50e-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: 41.85  E-value: 2.50e-05
                           10        20
                   ....*....|....*....|....*...
gi 149065992   495 FQCQeDSTCISLPRVCDRQPDCLNGSDE 522
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 531-563 2.76e-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: 41.46  E-value: 2.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 149065992   531 CGTFTFQCEDRSCVkkpnPE---CDGQADCRDGSDE 563
Cdd:smart00192   2 CPPGEFQCDNGRCI----PSswvCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 459-486 3.95e-04

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: 38.38  E-value: 3.95e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 149065992   459 PGEFLCSvNGLCVPA---CDGIKDCPNGLDE 486
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
459-489 2.44e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 2.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 149065992  459 PGEFLCSvNGLCVP---ACDGIKDCPNGLDERNC 489
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 577-771 1.94e-84

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: 267.61  E-value: 1.94e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 577 IVGGAMSSEGEWPWQASLQIR-GRHICGGALIADRWVITAAHCFQEdsmASPRLWTVFLGKMRQNSRWPGEVSFKVSRLF 655
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 656 LHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPGSSTLQKVDVQLIPQDLCNE 735
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 149065992 736 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKEP 771
Cdd:cd00190  158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN 195
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 576-772 4.33e-78

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: 250.67  E-value: 4.33e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   576 RIVGGAMSSEGEWPWQASLQIRG-RHICGGALIADRWVITAAHCFQEDSmasPRLWTVFLGKMRQNSRWPGEVsFKVSRL 654
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD---PSNIRVRLGSHDLSSGEEGQV-IKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   655 FLHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREG-GPGSSTLQKVDVQLIPQDLC 733
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 149065992   734 NEAYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKEPR 772
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR 197
Trypsin pfam00089
Trypsin;
577-769 1.20e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992  577 IVGGAMSSEGEWPWQASLQIR-GRHICGGALIADRWVITAAHCFqedsmASPRLWTVFLGKMRQNSRWPGEVSFKVSRLF 655
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992  656 LHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPgSSTLQKVDVQLIPQDLCNE 735
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 149065992  736 AYRYQVTPRMLCAGYrkGKKDACQGDSGGPLVCK 769
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCS 186
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 568-767 9.28e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 9.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 568 CGLQGPSSRIVGGAMSSEGEWPWQASLQIRG---RHICGGALIADRWVITAAHCFQEDSMASprlWTVFLGKMRQNSRwP 644
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLSTS-G 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 645 GEVSfKVSRLFLHPYHEEDSHDYDVALLQLDHPVvysATVRPVCLPARSHFFEPGQHCWITGWGAQREG-GPGSSTLQKV 723
Cdd:COG5640   98 GTVV-KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 149065992 724 DVQLIPQDLCNeAYRYQVTPRMLCAGYRKGKKDACQGDSGGPLV 767
Cdd:COG5640  174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV 216
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 597-766 1.11e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.39  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 597 RGRHICGGALIADRWVITAAHCFQEDSMAS-PRLWTVFLGkmRQNSRWpgeVSFKVSRLFLHP-YHEEDSHDYDVALLQL 674
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGwATNIVFVPG--YNGGPY---GTATATRFRVPPgWVASGDAGYDYALLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992 675 DHPVvySATVRPVCLpARSHFFEPGQHCWITGWGAqreGGPGSSTLQkvdvqlipqDLCNEAYRYQVTPRMLCagyrkgk 754
Cdd:COG3591   84 DEPL--GDTTGWLGL-AFNDAPLAGEPVTIIGYPG---DRPKDLSLD---------CSGRVTGVQGNRLSYDC------- 141

                        170
                 ....*....|..
gi 149065992 755 kDACQGDSGGPL 766
Cdd:COG3591  142 -DTTGGSSGSPV 152
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
529-566 6.07e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 6.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149065992  529 VPCGTFTFQCEDRSCVKKpNPECDGQADCRDGSDEEHC 566
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 531-566 7.60e-07

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: 46.05  E-value: 7.60e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 149065992 531 CGTFTFQCEDRSCVKKpNPECDGQADCRDGSDEEHC 566
Cdd:cd00112    1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 588-702 1.96e-06

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: 47.16  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992  588 WPWQASLQIRGRHICGGALIADRWVITAAHCFQEDSMASPRLwTVFLG--KMRQNSRWPGEVSFKVSRLflhpyheEDSH 665
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYI-SVVLGgaKTLKSIEGPYEQIVRVDCR-------HDIP 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 149065992  666 DYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHC 702
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 495-525 3.91e-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: 44.12  E-value: 3.91e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 149065992 495 FQCQeDSTCISLPRVCDRQPDCLNGSDEEQC 525
Cdd:cd00112    6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 459-489 4.99e-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: 43.73  E-value: 4.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 149065992 459 PGEFLCSvNGLCVPA---CDGIKDCPNGLDERNC 489
Cdd:cd00112    3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
495-525 7.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.39  E-value: 7.05e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 149065992  495 FQCQeDSTCISLPRVCDRQPDCLNGSDEEQC 525
Cdd:pfam00057   8 FQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-182 1.01e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.92  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149065992   88 QVYSGSLRVLNRHFSQDLARRESIAFRTETAKAQKMFQELVASTRLGTYYNSSSIYAF--GEGPLICFFWFILDIPeyqr 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76

                          90
                  ....*....|....*..
gi 149065992  166 lTLSPEVVRELLVGELL 182
Cdd:pfam01390  77 -STEPALDREKLIEEIL 92
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 495-522 2.50e-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: 41.85  E-value: 2.50e-05
                           10        20
                   ....*....|....*....|....*...
gi 149065992   495 FQCQeDSTCISLPRVCDRQPDCLNGSDE 522
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 531-563 2.76e-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: 41.46  E-value: 2.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 149065992   531 CGTFTFQCEDRSCVkkpnPE---CDGQADCRDGSDE 563
Cdd:smart00192   2 CPPGEFQCDNGRCI----PSswvCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 459-486 3.95e-04

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: 38.38  E-value: 3.95e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 149065992   459 PGEFLCSvNGLCVPA---CDGIKDCPNGLDE 486
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
459-489 2.44e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.07  E-value: 2.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 149065992  459 PGEFLCSvNGLCVP---ACDGIKDCPNGLDERNC 489
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 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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