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Conserved domains on  [gi|59809147|gb|AAH89798|]
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Complement factor I [Rattus norvegicus]

Protein Classification

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 ...
 361-590 1.25e-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: 1.25e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    361 RVVGGKPAEMGDYPWQVAIK-DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQgVSRVVVH 439
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    440 EKYNGATYQNDIALVEMKKHPgkkecELINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKVYS--LRWGEVDLIGN- 515
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPV-----TLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59809147    516 -CSRFYPGRYYEKE-MQCAGTSDGSIDACKGDSGGPLVCKDvnNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWI 590
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
FIMAC smart00057
factor I membrane attack complex;
46-111 1.28e-26

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 103.01  E-value: 1.28e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59809147     46 CDKVFCQPWQKCIEGTCACKLPYQCPKAGTPVCATNGRGY--PTYCHLKSFECLHPEIKFSNNGTCTA 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 1.12e-15

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: 72.76  E-value: 1.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    117 VSLIYGSTDTEGIVQVKLvdQDEKMFICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKInstECLHVRCQGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 59809147    197 SLAECTF-TKKSSKAPHG-LAGVVCY 220
Cdd:smart00202  76 SLSDCPHsGWGSHNCSHGeDAGVVCS 101
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-258 2.20e-07

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: 47.24  E-value: 2.20e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 59809147    228 TSQSFQCVNGKRIPQEKACDGVNDCGDQSDE 258
Cdd:smart00192   3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 4.49e-07

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.47  E-value: 4.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 59809147   264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGC 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 ...
 361-590 1.25e-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: 1.25e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    361 RVVGGKPAEMGDYPWQVAIK-DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQgVSRVVVH 439
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    440 EKYNGATYQNDIALVEMKKHPgkkecELINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKVYS--LRWGEVDLIGN- 515
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPV-----TLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59809147    516 -CSRFYPGRYYEKE-MQCAGTSDGSIDACKGDSGGPLVCKDvnNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWI 590
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 362-591 6.02e-79

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: 249.12  E-value: 6.02e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 362 VVGGKPAEMGDYPWQVAIK-DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQGVSRVVVHE 440
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 441 KYNGATYQNDIALVEMKKhPGKkeceLINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKV-YSLRWGEVDLIGN--C 516
Cdd:cd00190  81 NYNPSTYDNDIALLKLKR-PVT----LSDNVrPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59809147 517 SRFYPGRYY-EKEMQCAGTSDGSIDACKGDSGGPLVCKDvNNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWIS 591
Cdd:cd00190 156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Trypsin pfam00089
Trypsin;
362-590 1.45e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 205.75  E-value: 1.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   362 VVGGKPAEMGDYPWQVAIKD-GDRITCGGIYIGGCWILTAAHCVrpSRYRNYQVWTSLLDWLKPNSQLAVQGVSRVVVHE 440
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   441 KYNGATYQNDIALVEMKKhpgkkECELINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKVYSLRWGEVDLIGN--CS 517
Cdd:pfam00089  79 NYNPDTLDNDIALLKLES-----PVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59809147   518 RFYPGRYYEkEMQCAGTsdGSIDACKGDSGGPLVCKDVnnvtYVWGIVSWGENCGKPEFPGVYTRVASYFDWI 590
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 361-591 8.27e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 192.17  E-value: 8.27e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 361 RVVGGKPAEMGDYPWQVAIKDGD---RITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAvqGVSRVV 437
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVV--KVARIV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 438 VHEKYNGATYQNDIALVEMKKhpgkkecELINSVPACVPWSPYLFQPNDRCIISGWGREKDNQKVYS--LRWGEVDLIGN 515
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLAT-------PVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVSD 180

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59809147 516 CSRFYPGRYYEKEMQCAGTSDGSIDACKGDSGGPLVcKDVNNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWIS 591
Cdd:COG5640 181 ATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255
FIMAC smart00057
factor I membrane attack complex;
46-111 1.28e-26

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 103.01  E-value: 1.28e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59809147     46 CDKVFCQPWQKCIEGTCACKLPYQCPKAGTPVCATNGRGY--PTYCHLKSFECLHPEIKFSNNGTCTA 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 1.12e-15

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: 72.76  E-value: 1.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    117 VSLIYGSTDTEGIVQVKLvdQDEKMFICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKInstECLHVRCQGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 59809147    197 SLAECTF-TKKSSKAPHG-LAGVVCY 220
Cdd:smart00202  76 SLSDCPHsGWGSHNCSHGeDAGVVCS 101
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-258 2.20e-07

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: 47.24  E-value: 2.20e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 59809147    228 TSQSFQCVNGKRIPQEKACDGVNDCGDQSDE 258
Cdd:smart00192   3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 232-261 2.49e-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: 47.20  E-value: 2.49e-07
                        10        20        30
                ....*....|....*....|....*....|
gi 59809147 232 FQCVNGKRIPQEKACDGVNDCGDQSDELCC 261
Cdd:cd00112   6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 4.49e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.47  E-value: 4.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 59809147   264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGC 298
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 264-298 1.32e-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: 1.32e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 59809147 264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGC 298
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 143-219 1.39e-06

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: 46.99  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   143 ICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKINSteCLH-VRCQGVETSLAECTFTK-KSSKAPHG-LAGVVC 219
Cdd:pfam00530  20 VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFGPGSTGPI--WLDdVRCSGNETSLWQCPHRPwGNHNCSHSeDAGVIC 97
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 264-295 4.04e-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: 4.04e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 59809147    264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDE 295
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
232-261 3.50e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.08  E-value: 3.50e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 59809147   232 FQCVNGKRIPQEKACDGVNDCGDQSDELCC 261
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 67-109 1.96e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.70  E-value: 1.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 59809147    67 PYQCPKA-GTPVCATNGRGYPTYCHLKSFEC-LHPEIK---FSNNGTC 109
Cdd:pfam07648   3 NCQCPKTeYEPVCGSDGVTYPSPCALCAAGCkLGKEVKeekVKYDGSC 50
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 70-109 4.62e-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: 35.32  E-value: 4.62e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 59809147  70 CPKAGTPVCATNGRGYPTYCHLKSFECL-HPEIKFSNNGTC 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 ...
 361-590 1.25e-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: 1.25e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    361 RVVGGKPAEMGDYPWQVAIK-DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQgVSRVVVH 439
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK-VSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    440 EKYNGATYQNDIALVEMKKHPgkkecELINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKVYS--LRWGEVDLIGN- 515
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPV-----TLSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSNa 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 59809147    516 -CSRFYPGRYYEKE-MQCAGTSDGSIDACKGDSGGPLVCKDvnNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWI 590
Cdd:smart00020 155 tCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 362-591 6.02e-79

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: 249.12  E-value: 6.02e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 362 VVGGKPAEMGDYPWQVAIK-DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAVQGVSRVVVHE 440
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 441 KYNGATYQNDIALVEMKKhPGKkeceLINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKV-YSLRWGEVDLIGN--C 516
Cdd:cd00190  81 NYNPSTYDNDIALLKLKR-PVT----LSDNVrPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59809147 517 SRFYPGRYY-EKEMQCAGTSDGSIDACKGDSGGPLVCKDvNNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWIS 591
Cdd:cd00190 156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Trypsin pfam00089
Trypsin;
362-590 1.45e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 205.75  E-value: 1.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   362 VVGGKPAEMGDYPWQVAIKD-GDRITCGGIYIGGCWILTAAHCVrpSRYRNYQVWTSLLDWLKPNSQLAVQGVSRVVVHE 440
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   441 KYNGATYQNDIALVEMKKhpgkkECELINSV-PACVPWSPYLFQPNDRCIISGWGREKDNQKVYSLRWGEVDLIGN--CS 517
Cdd:pfam00089  79 NYNPDTLDNDIALLKLES-----PVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59809147   518 RFYPGRYYEkEMQCAGTsdGSIDACKGDSGGPLVCKDVnnvtYVWGIVSWGENCGKPEFPGVYTRVASYFDWI 590
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 361-591 8.27e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 192.17  E-value: 8.27e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 361 RVVGGKPAEMGDYPWQVAIKDGD---RITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTSLLDWLKPNSQLAvqGVSRVV 437
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVV--KVARIV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 438 VHEKYNGATYQNDIALVEMKKhpgkkecELINSVPACVPWSPYLFQPNDRCIISGWGREKDNQKVYS--LRWGEVDLIGN 515
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLAT-------PVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVSD 180

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 59809147 516 CSRFYPGRYYEKEMQCAGTSDGSIDACKGDSGGPLVcKDVNNVTYVWGIVSWGENCGKPEFPGVYTRVASYFDWIS 591
Cdd:COG5640 181 ATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255
FIMAC smart00057
factor I membrane attack complex;
46-111 1.28e-26

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 103.01  E-value: 1.28e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 59809147     46 CDKVFCQPWQKCIEGTCACKLPYQCPKAGTPVCATNGRGY--PTYCHLKSFECLHPEIKFSNNGTCTA 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 1.12e-15

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: 72.76  E-value: 1.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147    117 VSLIYGSTDTEGIVQVKLvdQDEKMFICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKInstECLHVRCQGVET 196
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPI---WLDNVRCSGTEA 75

                           90       100
                   ....*....|....*....|....*.
gi 59809147    197 SLAECTF-TKKSSKAPHG-LAGVVCY 220
Cdd:smart00202  76 SLSDCPHsGWGSHNCSHGeDAGVVCS 101
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-258 2.20e-07

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: 47.24  E-value: 2.20e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 59809147    228 TSQSFQCVNGKRIPQEKACDGVNDCGDQSDE 258
Cdd:smart00192   3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 232-261 2.49e-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: 47.20  E-value: 2.49e-07
                        10        20        30
                ....*....|....*....|....*....|
gi 59809147 232 FQCVNGKRIPQEKACDGVNDCGDQSDELCC 261
Cdd:cd00112   6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
264-298 4.49e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.47  E-value: 4.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 59809147   264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGC 298
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 381-568 6.29e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.06  E-value: 6.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 381 DGDRITCGGIYIGGCWILTAAHCVRPSRYRNYQVWTslldWLKPNSQLAVQG---VSRVVVHEKY-NGATYQNDIALVEM 456
Cdd:COG3591   8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNI----VFVPGYNGGPYGtatATRFRVPPGWvASGDAGYDYALLRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147 457 KKHPGkkeceliNSVPACVPWSPYLFQPNDRCIISGWGRekDNQKVYSLRWGevdliGNCSRFYPGRYYekeMQCagtsd 536
Cdd:COG3591  84 DEPLG-------DTTGWLGLAFNDAPLAGEPVTIIGYPG--DRPKDLSLDCS-----GRVTGVQGNRLS---YDC----- 141

                       170       180       190
                ....*....|....*....|....*....|..
gi 59809147 537 gsiDACKGDSGGPLVCKDvNNVTYVWGIVSWG 568
Cdd:COG3591 142 ---DTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 264-298 1.32e-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: 1.32e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 59809147 264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDESGC 298
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 143-219 1.39e-06

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: 46.99  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59809147   143 ICKNSWSTVEANVACFDLGFPLGVRDIQGRFNIPVNHKINSteCLH-VRCQGVETSLAECTFTK-KSSKAPHG-LAGVVC 219
Cdd:pfam00530  20 VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFGPGSTGPI--WLDdVRCSGNETSLWQCPHRPwGNHNCSHSeDAGVIC 97
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 264-295 4.04e-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: 4.04e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 59809147    264 CRGQAFLCKSGVCIPNQRKCNGEVDCITGEDE 295
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
232-261 3.50e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.08  E-value: 3.50e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 59809147   232 FQCVNGKRIPQEKACDGVNDCGDQSDELCC 261
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 67-109 1.96e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.70  E-value: 1.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 59809147    67 PYQCPKA-GTPVCATNGRGYPTYCHLKSFEC-LHPEIK---FSNNGTC 109
Cdd:pfam07648   3 NCQCPKTeYEPVCGSDGVTYPSPCALCAAGCkLGKEVKeekVKYDGSC 50
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 67-109 3.37e-03

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 35.73  E-value: 3.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 59809147     67 PYQCPKAGTPVCATNGRGYPTYCHLKSFECLH-PEIKFSNNGTC 109
Cdd:smart00280   3 PEACPREYDPVCGSDGVTYSNECHLCKAACESgKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 70-109 4.62e-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: 35.32  E-value: 4.62e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 59809147  70 CPKAGTPVCATNGRGYPTYCHLKSFECL-HPEIKFSNNGTC 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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