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Conserved domains on  [gi|1767344729|ref|NP_001362213|]
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complement factor I isoform 10 [Homo sapiens]

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 ...
 137-369 1.37e-81

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: 1.37e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 137 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 215
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 216 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 292
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767344729 293 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 369
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
54-90 1.63e-10

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.72  E-value: 1.63e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1767344729  54 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 90
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 21-53 2.87e-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: 46.43  E-value: 2.87e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1767344729  21 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 53
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 137-369 1.37e-81

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: 1.37e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 137 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 215
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 216 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 292
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767344729 293 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 369
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 136-366 5.04e-81

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: 247.59  E-value: 5.04e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729  136 RIVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieYVDRIIF 214
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVI--KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729  215 HENYNAGTYQNDIALIEMKKDGNkkdceLPRSI-PACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLISN 291
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767344729  292 --CSKFYGNRFYEKE-MECAGTYDGSIDACKGDSGGPLVCMDanNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 366
Cdd:smart00020 154 atCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
137-366 3.43e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 216.92  E-value: 3.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 137 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASktHRYQIWTTVvDWIHPDLKRIVIEYVDRIIFH 215
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGA-HNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 216 ENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPAcvpwSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISN--CS 293
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPD----ASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767344729 294 KFYGNRFYEkEMECAGTydGSIDACKGDSGGPLVCMDannvTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 366
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 136-373 4.44e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.77  E-value: 4.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 136 RIVGGKRAQLGDLPWQVAIKDASGI---TCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieyVDRI 212
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK---VARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 213 IFHENYNAGTYQNDIALIEMKKDgnkkdceLPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLIS 290
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 291 NCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVcMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHV 370
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ...
gi 1767344729 371 GRP 373
Cdd:COG5640   259 GGL 261
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
54-90 1.63e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.72  E-value: 1.63e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1767344729  54 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 90
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 56-90 8.27e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 47.97  E-value: 8.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1767344729  56 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 90
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 21-53 2.87e-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: 46.43  E-value: 2.87e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1767344729  21 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 53
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 22-50 6.07e-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: 45.32  E-value: 6.07e-07
                           10        20
                   ....*....|....*....|....*....
gi 1767344729   22 DFFQCVNGKYISQMKACDGINDCGDQSDE 50
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 56-87 1.80e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.16  E-value: 1.80e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1767344729   56 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDE 87
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
24-53 6.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.62  E-value: 6.05e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1767344729  24 FQCVNGKYISQMKACDGINDCGDQSDELCC 53
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 137-369 1.37e-81

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: 1.37e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 137 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 215
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 216 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 292
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767344729 293 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 369
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 136-366 5.04e-81

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: 247.59  E-value: 5.04e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729  136 RIVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieYVDRIIF 214
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVI--KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729  215 HENYNAGTYQNDIALIEMKKDGNkkdceLPRSI-PACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLISN 291
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767344729  292 --CSKFYGNRFYEKE-MECAGTYDGSIDACKGDSGGPLVCMDanNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 366
Cdd:smart00020 154 atCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
137-366 3.43e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 216.92  E-value: 3.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 137 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASktHRYQIWTTVvDWIHPDLKRIVIEYVDRIIFH 215
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGA-HNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 216 ENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPAcvpwSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISN--CS 293
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPD----ASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767344729 294 KFYGNRFYEkEMECAGTydGSIDACKGDSGGPLVCMDannvTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 366
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 136-373 4.44e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.77  E-value: 4.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 136 RIVGGKRAQLGDLPWQVAIKDASGI---TCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieyVDRI 212
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK---VARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 213 IFHENYNAGTYQNDIALIEMKKDgnkkdceLPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLIS 290
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 291 NCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVcMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHV 370
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ...
gi 1767344729 371 GRP 373
Cdd:COG5640   259 GGL 261
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
54-90 1.63e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.72  E-value: 1.63e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1767344729  54 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 90
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 56-90 8.27e-08

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 47.97  E-value: 8.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1767344729  56 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 90
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 21-53 2.87e-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: 46.43  E-value: 2.87e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1767344729  21 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 53
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 22-50 6.07e-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: 45.32  E-value: 6.07e-07
                           10        20
                   ....*....|....*....|....*....
gi 1767344729   22 DFFQCVNGKYISQMKACDGINDCGDQSDE 50
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 56-87 1.80e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.16  E-value: 1.80e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1767344729   56 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDE 87
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
24-53 6.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.62  E-value: 6.05e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1767344729  24 FQCVNGKYISQMKACDGINDCGDQSDELCC 53
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 156-344 3.44e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.28  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 156 DASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVV-DWihpDLKRIVIEYVDRIIFHENY-NAGTYQNDIALIemk 233
Cdd:COG3591     8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVpGY---NGGPYGTATATRFRVPPGWvASGDAGYDYALL--- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767344729 234 kdgnkkdcELPRSIPACVPWSPYLFQPndtcivsgwgREKDNERVFSLQWGevklisncskfyGNRFYEKEMECAGTYDG 313
Cdd:COG3591    82 --------RLDEPLGDTTGWLGLAFND----------APLAGEPVTIIGYP------------GDRPKDLSLDCSGRVTG 131

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1767344729 314 --------SIDACKGDSGGPlVCMDANNVTYVWGVVSWG 344
Cdd:COG3591   132 vqgnrlsyDCDTTGGSSGSP-VLDDSDGGGRVVGVHSAG 169
 
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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