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Conserved domains on  [gi|1812653237|ref|NP_000195|]
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complement factor I isoform 2 preproprotein [Homo sapiens]

Protein Classification

FIMAC and Tryp_SPc domain-containing protein( domain architecture ID 11249539)

protein containing domains FIMAC, SR, LDLa, and Tryp_SPc

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 ...
340-572 3.11e-80

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: 251.81  E-value: 3.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 340 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 418
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 419 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 495
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237 496 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 572
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
FIMAC smart00057
factor I membrane attack complex;
43-108 1.59e-27

factor I membrane attack complex;


:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 105.32  E-value: 1.59e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237   43 CDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRS--FPTYCQQKSLECLHPGTKFLNNGTCTA 108
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSekTLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
114-215 4.11e-19

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: 82.77  E-value: 4.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  114 VSLKHGNTDSEGIVEVKLvdQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSiNSTECLHVHCRGLETSL 193
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGS-GPIWLDNVRCSGTEASL 77
                           90       100
                   ....*....|....*....|....
gi 1812653237  194 AECTFT--KRRTMGYQDFADVVCY 215
Cdd:smart00202  78 SDCPHSgwGSHNCSHGEDAGVVCS 101
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
257-293 4.54e-10

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.95  E-value: 4.54e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1812653237 257 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 293
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
224-256 6.41e-07

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 6.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1812653237 224 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 256
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 ...
340-572 3.11e-80

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: 251.81  E-value: 3.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 340 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 418
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 419 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 495
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237 496 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 572
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
339-569 9.93e-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: 250.67  E-value: 9.93e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  339 RIVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieYVDRIIF 417
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVI--KVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  418 HENYNAGTYQNDIALIEMKKDGNkkdceLPRSI-PACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLISN 494
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237  495 --CSKFYGNRFYEKE-MECAGTYDGSIDACKGDSGGPLVCMDanNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 569
Cdd:smart00020 154 atCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
340-569 8.64e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.55  E-value: 8.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 340 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASktHRYQIWTTVvDWIHPDLKRIVIEYVDRIIFH 418
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGA-HNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 419 ENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPAcvpwSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISN--CS 496
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPD----ASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812653237 497 KFYGNRFYEkEMECAGTydGSIDACKGDSGGPLVCMDannvTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 569
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
339-576 2.44e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 185.24  E-value: 2.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 339 RIVGGKRAQLGDLPWQVAIKDASGI---TCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieyVDRI 415
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK---VARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 416 IFHENYNAGTYQNDIALIEMKKDgnkkdceLPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLIS 493
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 494 NCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVcMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHV 573
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                  ...
gi 1812653237 574 GRP 576
Cdd:COG5640   259 GGL 261
FIMAC smart00057
factor I membrane attack complex;
43-108 1.59e-27

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 105.32  E-value: 1.59e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237   43 CDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRS--FPTYCQQKSLECLHPGTKFLNNGTCTA 108
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSekTLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
114-215 4.11e-19

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: 82.77  E-value: 4.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  114 VSLKHGNTDSEGIVEVKLvdQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSiNSTECLHVHCRGLETSL 193
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGS-GPIWLDNVRCSGTEASL 77
                           90       100
                   ....*....|....*....|....
gi 1812653237  194 AECTFT--KRRTMGYQDFADVVCY 215
Cdd:smart00202  78 SDCPHSgwGSHNCSHGEDAGVVCS 101
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
257-293 4.54e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.95  E-value: 4.54e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1812653237 257 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 293
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
119-214 4.98e-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: 50.84  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 119 GNTDSEGIVEVKLVDQDKTmfICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLH-VHCRGLETSLAECT 197
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGT--VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFGPGSTGPIWLDdVRCSGNETSLWQCP 78
                          90
                  ....*....|....*....
gi 1812653237 198 F--TKRRTMGYQDFADVVC 214
Cdd:pfam00530  79 HrpWGNHNCSHSEDAGVIC 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
259-293 1.90e-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: 1.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1812653237 259 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 293
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
224-256 6.41e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 6.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1812653237 224 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 256
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
225-253 1.32e-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: 44.93  E-value: 1.32e-06
                           10        20
                   ....*....|....*....|....*....
gi 1812653237  225 DFFQCVNGKYISQMKACDGINDCGDQSDE 253
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
259-290 3.90e-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: 3.90e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1812653237  259 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDE 290
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
227-256 1.44e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1812653237 227 FQCVNGKYISQMKACDGINDCGDQSDELCC 256
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 ...
340-572 3.11e-80

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: 251.81  E-value: 3.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 340 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEyVDRIIFH 418
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIK-VKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 419 ENYNAGTYQNDIALIEMKKDGNKKDcelpRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERV-FSLQWGEVKLISN--C 495
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSD----NVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLpDVLQEVNVPIVSNaeC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237 496 SKFYGNRFY-EKEMECAGTYDGSIDACKGDSGGPLVCMDaNNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYH 572
Cdd:cd00190   156 KRAYSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
339-569 9.93e-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: 250.67  E-value: 9.93e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  339 RIVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieYVDRIIF 417
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVI--KVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  418 HENYNAGTYQNDIALIEMKKDGNkkdceLPRSI-PACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLISN 494
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVrPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPdtLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237  495 --CSKFYGNRFYEKE-MECAGTYDGSIDACKGDSGGPLVCMDanNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 569
Cdd:smart00020 154 atCRRAYSGGGAITDnMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
340-569 8.64e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.55  E-value: 8.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 340 IVGGKRAQLGDLPWQVAIKDASG-ITCGGIYIGGCWILTAAHCLRASktHRYQIWTTVvDWIHPDLKRIVIEYVDRIIFH 418
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGA-HNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 419 ENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPAcvpwSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISN--CS 496
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPD----ASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRetCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812653237 497 KFYGNRFYEkEMECAGTydGSIDACKGDSGGPLVCMDannvTYVWGVVSWGENCGKPEFPGVYTKVANYFDWI 569
Cdd:pfam00089 154 SAYGGTVTD-TMICAGA--GGKDACQGDSGGPLVCSD----GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
339-576 2.44e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 185.24  E-value: 2.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 339 RIVGGKRAQLGDLPWQVAIKDASGI---TCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVieyVDRI 415
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK---VARI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 416 IFHENYNAGTYQNDIALIEMKKDgnkkdceLPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFS--LQWGEVKLIS 493
Cdd:COG5640   107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSgtLRKADVPVVS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 494 NCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVcMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHV 573
Cdd:COG5640   180 DATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258

                  ...
gi 1812653237 574 GRP 576
Cdd:COG5640   259 GGL 261
FIMAC smart00057
factor I membrane attack complex;
43-108 1.59e-27

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 105.32  E-value: 1.59e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812653237   43 CDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRS--FPTYCQQKSLECLHPGTKFLNNGTCTA 108
Cdd:smart00057   1 CAKGFCQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSekTLTYCKQGALRCLNQKYKFLHIGSCTA 68
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
114-215 4.11e-19

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: 82.77  E-value: 4.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237  114 VSLKHGNTDSEGIVEVKLvdQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSiNSTECLHVHCRGLETSL 193
Cdd:smart00202   1 VRLVGGGSPCEGRVEVYH--NGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYFGPGS-GPIWLDNVRCSGTEASL 77
                           90       100
                   ....*....|....*....|....
gi 1812653237  194 AECTFT--KRRTMGYQDFADVVCY 215
Cdd:smart00202  78 SDCPHSgwGSHNCSHGEDAGVVCS 101
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
257-293 4.54e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.95  E-value: 4.54e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1812653237 257 KACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 293
Cdd:pfam00057   1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
119-214 4.98e-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: 50.84  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 119 GNTDSEGIVEVKLVDQDKTmfICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLH-VHCRGLETSLAECT 197
Cdd:pfam00530   1 GSSPCEGRVEVYHNGSWGT--VCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFGPGSTGPIWLDdVRCSGNETSLWQCP 78
                          90
                  ....*....|....*....
gi 1812653237 198 F--TKRRTMGYQDFADVVC 214
Cdd:pfam00530  79 HrpWGNHNCSHSEDAGVIC 97
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
259-293 1.90e-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: 1.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1812653237 259 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGC 293
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
224-256 6.41e-07

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 46.05  E-value: 6.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1812653237 224 DDFFQCVNGKYISQMKACDGINDCGDQSDELCC 256
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
225-253 1.32e-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: 44.93  E-value: 1.32e-06
                           10        20
                   ....*....|....*....|....*....
gi 1812653237  225 DFFQCVNGKYISQMKACDGINDCGDQSDE 253
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
259-290 3.90e-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: 3.90e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1812653237  259 CQGKGFHCKSGVCIPSQYQCNGEVDCITGEDE 290
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
359-547 1.34e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.21  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 359 DASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVV-DWihpDLKRIVIEYVDRIIFHENY-NAGTYQNDIALIemk 436
Cdd:COG3591     8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVpGY---NGGPYGTATATRFRVPPGWvASGDAGYDYALL--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812653237 437 kdgnkkdcELPRSIPACVPWSPYLFQPndtcivsgwgREKDNERVFSLQWGevklisncskfyGNRFYEKEMECAGTYDG 516
Cdd:COG3591    82 --------RLDEPLGDTTGWLGLAFND----------APLAGEPVTIIGYP------------GDRPKDLSLDCSGRVTG 131
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1812653237 517 --------SIDACKGDSGGPlVCMDANNVTYVWGVVSWG 547
Cdd:COG3591   132 vqgnrlsyDCDTTGGSSGSP-VLDDSDGGGRVVGVHSAG 169
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
227-256 1.44e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 42.24  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1812653237 227 FQCVNGKYISQMKACDGINDCGDQSDELCC 256
Cdd:pfam00057   8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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