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Conserved domains on  [gi|110347406|ref|NP_031712|]
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complement factor I isoform 1 preproprotein [Mus musculus]

Protein Classification

KAZAL_FS and Tryp_SPc domain-containing protein( domain architecture ID 12186019)

protein containing domains KAZAL_FS, SR, LDLa, and Tryp_SPc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 360-589 1.18e-80

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: 253.37  E-value: 1.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   360 RVIGGKPANVGDYPWQVAIK-DGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQtVKRVIVH 438
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   439 EKYNGATFQNDIALIEMKmhtgkKECELPNSV-PACVPWSPYLFQPNDRCIISGWGRGKDNQKVYS--LRWGEVDLIGN- 514
Cdd:smart00020  80 PNYNPSTYDNDIALLKLK-----EPVTLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347406   515 -CSQFYPDRYYEKE-MQCAGTRDGSIDACKGDSGGPLVCEDinNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWI 589
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
FIMAC smart00057
factor I membrane attack complex;
46-111 1.53e-28

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 108.40  E-value: 1.53e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347406    46 CNKVFCQPWQRCIEGTCICKLPYQCPRAGTPVCAMNGRSY--PTYCHQKSFECLHPEIKFSHNGTCAA 111
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSEktLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 117-220 1.24e-17

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: 78.54  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   117 VSLIYGRTKTEGLVQVKLvdQDERMFICKNSWSMAEANVACVDLGFPLGVRDIQGSFNISGNLHIndtECLHVHCRGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 110347406   197 SLAECAFT--KRRTELSNGLAGVVCY 220
Cdd:smart00202  76 SLSDCPHSgwGSHNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 232-261 2.42e-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: 2.42e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 110347406 232 FQCVNGKHIPQEKACNGVNDCGDQSDELCC 261
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 2.80e-06

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.16  E-value: 2.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110347406  264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRC 298
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 360-589 1.18e-80

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: 253.37  E-value: 1.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   360 RVIGGKPANVGDYPWQVAIK-DGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQtVKRVIVH 438
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   439 EKYNGATFQNDIALIEMKmhtgkKECELPNSV-PACVPWSPYLFQPNDRCIISGWGRGKDNQKVYS--LRWGEVDLIGN- 514
Cdd:smart00020  80 PNYNPSTYDNDIALLKLK-----EPVTLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347406   515 -CSQFYPDRYYEKE-MQCAGTRDGSIDACKGDSGGPLVCEDinNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWI 589
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 361-592 1.55e-78

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: 247.96  E-value: 1.55e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 361 VIGGKPANVGDYPWQVAIK-DGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQTVKRVIVHE 439
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 440 KYNGATFQNDIALIEMkmhtgKKECELPNSV-PACVPWSPYLFQPNDRCIISGWGR-GKDNQKVYSLRWGEVDLIGN--C 515
Cdd:cd00190   81 NYNPSTYDNDIALLKL-----KRPVTLSDNVrPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVPIVSNaeC 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347406 516 SQFYPDRYY-EKEMQCAGTRDGSIDACKGDSGGPLVCEDiNNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWISYH 592
Cdd:cd00190  156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
361-589 7.01e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 7.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  361 VIGGKPANVGDYPWQVAIKDGQ-RITCGGIYIGGCWILTAAHCVrpSRAHSYQVWTALLDWLKPNSQLGIQTVKRVIVHE 439
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  440 KYNGATFQNDIALIEMKmhtgkKECELPNSV-PACVPWSPYLFQPNDRCIISGWGRGKDNQKVYSLRWGEVDLIGN--CS 516
Cdd:pfam00089  79 NYNPDTLDNDIALLKLE-----SPVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347406  517 QFYPDRYYEkEMQCAGTrdGSIDACKGDSGGPLVCEDinnvTYVWGIVSWGENCGKPEFPGVYTRVANYFDWI 589
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 360-594 1.23e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.79  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 360 RVIGGKPANVGDYPWQVAI--KDG-QRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWlkpNSQLGIQ-TVKRV 435
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALqsSNGpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDL---STSGGTVvKVARI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 436 IVHEKYNGATFQNDIALIEMkmhtgkkECELPNSVPACVPWSPYLFQPNDRCIISGWGRGKDNQKVYS--LRWGEVDLIG 513
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 514 NCSQFYPDRYYEKEMQCAGTRDGSIDACKGDSGGPLVcEDINNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWISYHV 593
Cdd:COG5640  180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                 .
gi 110347406 594 G 594
Cdd:COG5640  259 G 259
FIMAC smart00057
factor I membrane attack complex;
46-111 1.53e-28

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 108.40  E-value: 1.53e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347406    46 CNKVFCQPWQRCIEGTCICKLPYQCPRAGTPVCAMNGRSY--PTYCHQKSFECLHPEIKFSHNGTCAA 111
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSEktLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 117-220 1.24e-17

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: 78.54  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   117 VSLIYGRTKTEGLVQVKLvdQDERMFICKNSWSMAEANVACVDLGFPLGVRDIQGSFNISGNLHIndtECLHVHCRGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 110347406   197 SLAECAFT--KRRTELSNGLAGVVCY 220
Cdd:smart00202  76 SLSDCPHSgwGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 122-219 7.19e-08

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 50.45  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  122 GRTKTEGLVQVKLVDQDERmfICKNSWSMAEANVACVDLGFPLGVRDIQGSFN----ISGNLHINDteclhVHCRGVETS 197
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGT--VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYfgpgSTGPIWLDD-----VRCSGNETS 73

                          90       100
                  ....*....|....*....|....
gi 110347406  198 LAECAF--TKRRTELSNGLAGVVC 219
Cdd:pfam00530  74 LWQCPHrpWGNHNCSHSEDAGVIC 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 232-261 2.42e-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: 2.42e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 110347406 232 FQCVNGKHIPQEKACNGVNDCGDQSDELCC 261
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 2.80e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.16  E-value: 2.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110347406  264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRC 298
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 232-258 3.70e-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: 43.78  E-value: 3.70e-06
                           10        20
                   ....*....|....*....|....*..
gi 110347406   232 FQCVNGKHIPQEKACNGVNDCGDQSDE 258
Cdd:smart00192   7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 264-298 3.04e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 41.04  E-value: 3.04e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 110347406 264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRC 298
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
232-261 5.02e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 5.02e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 110347406  232 FQCVNGKHIPQEKACNGVNDCGDQSDELCC 261
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 264-295 9.05e-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: 39.92  E-value: 9.05e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 110347406   264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDE 295
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 70-109 9.10e-03

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 34.55  E-value: 9.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 110347406  70 CPRAGTPVCAMNGRSYPTYCHQKSFECL-HPEIKFSHNGTC 109
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRsGRSITVAHNGPC 41
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 360-589 1.18e-80

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: 253.37  E-value: 1.18e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   360 RVIGGKPANVGDYPWQVAIK-DGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQtVKRVIVH 438
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   439 EKYNGATFQNDIALIEMKmhtgkKECELPNSV-PACVPWSPYLFQPNDRCIISGWGRGKDNQKVYS--LRWGEVDLIGN- 514
Cdd:smart00020  80 PNYNPSTYDNDIALLKLK-----EPVTLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347406   515 -CSQFYPDRYYEKE-MQCAGTRDGSIDACKGDSGGPLVCEDinNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWI 589
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 361-592 1.55e-78

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: 247.96  E-value: 1.55e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 361 VIGGKPANVGDYPWQVAIK-DGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQTVKRVIVHE 439
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 440 KYNGATFQNDIALIEMkmhtgKKECELPNSV-PACVPWSPYLFQPNDRCIISGWGR-GKDNQKVYSLRWGEVDLIGN--C 515
Cdd:cd00190   81 NYNPSTYDNDIALLKL-----KRPVTLSDNVrPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVPIVSNaeC 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347406 516 SQFYPDRYY-EKEMQCAGTRDGSIDACKGDSGGPLVCEDiNNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWISYH 592
Cdd:cd00190  156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
361-589 7.01e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 206.52  E-value: 7.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  361 VIGGKPANVGDYPWQVAIKDGQ-RITCGGIYIGGCWILTAAHCVrpSRAHSYQVWTALLDWLKPNSQLGIQTVKRVIVHE 439
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  440 KYNGATFQNDIALIEMKmhtgkKECELPNSV-PACVPWSPYLFQPNDRCIISGWGRGKDNQKVYSLRWGEVDLIGN--CS 516
Cdd:pfam00089  79 NYNPDTLDNDIALLKLE-----SPVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347406  517 QFYPDRYYEkEMQCAGTrdGSIDACKGDSGGPLVCEDinnvTYVWGIVSWGENCGKPEFPGVYTRVANYFDWI 589
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 360-594 1.23e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.79  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 360 RVIGGKPANVGDYPWQVAI--KDG-QRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWlkpNSQLGIQ-TVKRV 435
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALqsSNGpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDL---STSGGTVvKVARI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 436 IVHEKYNGATFQNDIALIEMkmhtgkkECELPNSVPACVPWSPYLFQPNDRCIISGWGRGKDNQKVYS--LRWGEVDLIG 513
Cdd:COG5640  107 VVHPDYDPATPGNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 514 NCSQFYPDRYYEKEMQCAGTRDGSIDACKGDSGGPLVcEDINNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWISYHV 593
Cdd:COG5640  180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                 .
gi 110347406 594 G 594
Cdd:COG5640  259 G 259
FIMAC smart00057
factor I membrane attack complex;
46-111 1.53e-28

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 108.40  E-value: 1.53e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347406    46 CNKVFCQPWQRCIEGTCICKLPYQCPRAGTPVCAMNGRSY--PTYCHQKSFECLHPEIKFSHNGTCAA 111
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSEktLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 117-220 1.24e-17

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: 78.54  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406   117 VSLIYGRTKTEGLVQVKLvdQDERMFICKNSWSMAEANVACVDLGFPLGVRDIQGSFNISGNLHIndtECLHVHCRGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 110347406   197 SLAECAFT--KRRTELSNGLAGVVCY 220
Cdd:smart00202  76 SLSDCPHSgwGSHNCSHGEDAGVVCS 101
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 380-567 4.42e-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: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 380 DGQRITCGGIYIGGCWILTAAHCV-RPSRAHSYQVWTALLDWLkpNSQLGIQTVKRVIVHEKY-NGATFQNDIALIEMkm 457
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVyDGAGGGWATNIVFVPGYN--GGPYGTATATRFRVPPGWvASGDAGYDYALLRL-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406 458 htgkkECELPNSVPACVPWSPYLFQPNDRCIISGWGRGKdnQKVYSLRWGevdliGNCSQFYPDRYYekeMQCagtrdgs 537
Cdd:COG3591   84 -----DEPLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDR--PKDLSLDCS-----GRVTGVQGNRLS---YDC------- 141

                        170       180       190
                 ....*....|....*....|....*....|...
gi 110347406 538 iDACKGDSGGPLvcedINNVTYVW---GIVSWG 567
Cdd:COG3591  142 -DTTGGSSGSPV----LDDSDGGGrvvGVHSAG 169
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 122-219 7.19e-08

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 50.45  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  122 GRTKTEGLVQVKLVDQDERmfICKNSWSMAEANVACVDLGFPLGVRDIQGSFN----ISGNLHINDteclhVHCRGVETS 197
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGT--VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYfgpgSTGPIWLDD-----VRCSGNETS 73

                          90       100
                  ....*....|....*....|....
gi 110347406  198 LAECAF--TKRRTELSNGLAGVVC 219
Cdd:pfam00530  74 LWQCPHrpWGNHNCSHSEDAGVIC 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 232-261 2.42e-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: 2.42e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 110347406 232 FQCVNGKHIPQEKACNGVNDCGDQSDELCC 261
Cdd:cd00112    6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 2.80e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.16  E-value: 2.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 110347406  264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRC 298
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 232-258 3.70e-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: 43.78  E-value: 3.70e-06
                           10        20
                   ....*....|....*....|....*..
gi 110347406   232 FQCVNGKHIPQEKACNGVNDCGDQSDE 258
Cdd:smart00192   7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 264-298 3.04e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 41.04  E-value: 3.04e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 110347406 264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRC 298
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
232-261 5.02e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.69  E-value: 5.02e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 110347406  232 FQCVNGKHIPQEKACNGVNDCGDQSDELCC 261
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 264-295 9.05e-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: 39.92  E-value: 9.05e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 110347406   264 CRGNASLCKSGVCIPDQYKCNGEVDCITGEDE 295
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 388-553 1.94e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.94  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  388 GIYIG-GCWILTAAHCVRPSRAHSYQVWTALLDwlkpnsqlGIQTVKRVIVHekyngATFQNDIALIEMKmhtgkkecEL 466
Cdd:pfam13365   3 GFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLA--------DGREYPATVVA-----RDPDLDLALLRVS--------GD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347406  467 PNSVPACVPWSPYLFQPNDRCIISGWGRGKDNQkvySLRWGEVDLIGNCSQFYPDRYYekeMQCagtrdgSIDACKGDSG 546
Cdd:pfam13365  62 GRGLPPLPLGDSEPLVGGERVYAVGYPLGGEKL---SLSEGIVSGVDEGRDGGDDGRV---IQT------DAALSPGSSG 129


                  ....*..
gi 110347406  547 GPLVCED 553
Cdd:pfam13365 130 GPVFDAD 136
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 67-109 6.20e-03

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 34.96  E-value: 6.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 110347406    67 PYQCPRAGTPVCAMNGRSYPTYCHQKSFECLH-PEIKFSHNGTC 109
Cdd:smart00280   3 PEACPREYDPVCGSDGVTYSNECHLCKAACESgKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 70-109 9.10e-03

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 34.55  E-value: 9.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 110347406  70 CPRAGTPVCAMNGRSYPTYCHQKSFECL-HPEIKFSHNGTC 109
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRsGRSITVAHNGPC 41
 
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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