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Conserved domains on  [gi|1033015281|ref|NP_001314855|]
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complement component C9 precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF super family cl46582
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 354-576 2.62e-27

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


The actual alignment was detected with superfamily member pfam01823:

Pssm-ID: 460349  Cd Length: 211  Bit Score: 109.80  E-value: 2.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 354 KQLSELTTTKRKTFMRVKGRVELATYRM-RQRGLEVSSTFLDDVDALPLQYEKGQ---YFSFLEEYGTHFTKNGKSGGEY 429
Cdd:pfam01823  10 KKMSDKSKQKKKSLIISKSTCSLYQFTLkRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGKI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 430 QLVYVMNEDIRKQKHVTEATVKKCFELGLKADFqltpaaeGGGEVKPLNDCNSLTNTDTDEKNNkgvIDKVLIEVKGGSA 509
Cdd:pfam01823  90 VYVLKLDKSQLEDLKLKGEDVKICLSASAGASI-------GSVNLKGCSKNSSSTKEKKSFNQE---IESSITLVIGGTP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033015281 510 ASAVamksqltkDGILDYNqyvEWAKTITILPALIQSEPEPIYNAIplsfPDAQPRRDNLKRALDEY 576
Cdd:pfam01823 160 ESID--------DDSKTYS---DWAESVKDNPMPIDFELTPISELL----KGVPLKKENLRKALEEY 211
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 103-140 8.90e-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: 45.66  E-value: 8.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281 103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDEEDC 140
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCG--DGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 633-673 2.10e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.27  E-value: 2.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1033015281  633 WGCWSAWSHCS----GGRRTRSRSCNNRGLTNG--ICKGDKTSEDYC 673
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGggPCTGEDVETRAC 47
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 44-79 6.18e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 38.03  E-value: 6.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281  44 CKMSAWSQWSPCD-PCTN-TTYRSRSIEVFGQFKGTVC 79
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPC 38
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 354-576 2.62e-27

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 109.80  E-value: 2.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 354 KQLSELTTTKRKTFMRVKGRVELATYRM-RQRGLEVSSTFLDDVDALPLQYEKGQ---YFSFLEEYGTHFTKNGKSGGEY 429
Cdd:pfam01823  10 KKMSDKSKQKKKSLIISKSTCSLYQFTLkRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGKI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 430 QLVYVMNEDIRKQKHVTEATVKKCFELGLKADFqltpaaeGGGEVKPLNDCNSLTNTDTDEKNNkgvIDKVLIEVKGGSA 509
Cdd:pfam01823  90 VYVLKLDKSQLEDLKLKGEDVKICLSASAGASI-------GSVNLKGCSKNSSSTKEKKSFNQE---IESSITLVIGGTP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033015281 510 ASAVamksqltkDGILDYNqyvEWAKTITILPALIQSEPEPIYNAIplsfPDAQPRRDNLKRALDEY 576
Cdd:pfam01823 160 ESID--------DDSKTYS---DWAESVKDNPMPIDFELTPISELL----KGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
367-577 2.07e-24

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 100.97  E-value: 2.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281  367 FMRVKGRVELATYRMRQRGLEVSSTFLDDVDALPLQYEKGQYFSFLEEYGTHFTKNGKSGGEYQLVYVMNEDIRKQKHVT 446
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281  447 EATVKKCFElGLKADFQLTPAAEGGGEVKplndcNSLTNTDTDEknnkgvIDKVLIEVKGGsaasAVAMKSQLTKDGILD 526
Cdd:smart00457  81 SEDISKCLA-GSSNSFAGSVSAEHCLQSS-----SYIKYLSTSL------RRESHTQVLGG----HVTVLCDLLRGPSSN 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1033015281  527 YNQYVEWAKTITILPALIQSEPEPIYNAIPlSFPDAQPRRDNLKRALDEYV 577
Cdd:smart00457 145 SLDFSDWAESVPNEPVLIDVSLAPIYELLP-PNPELSQKREALRQALRSYL 194
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 334-581 6.10e-07

membrane-attack complex/perforin (MACPF) Superfamily; Provisional


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 52.95  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 334 GFGiSGSAGANYKqtttniiKQLSELTTTKRKTFMrvkgrveLATYRMR-QRGL------EVSSTFLDDVDALPL----- 401
Cdd:PTZ00482  339 GIN-SFSASTGYK-------KFLQEVSKRTTKTYL-------LKSNCVKyTAGLppyfkwNQTTAFKNAVNGLPPvfdgl 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 402 ---------QYEKGQ----------YFSFLEEYGTHFTKNGKSGGEyqlvyvmnedIRKQKHVTEATVKKCFELGLKADF 462
Cdd:PTZ00482  404 eaesecssdVYEQDKtaeecenvpiWISFFEQYGTHIIMELQLGGK----------ITKQVTVKNSSVEQMKKDGVSVKA 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 463 QLTpAAEGGGEVKPLNDCNSLTNTDTDEKNNKgvIDKVLIeVKGGSAASAVAMKSQLtkdgildynqyVEWAKTITILPA 542
Cdd:PTZ00482  474 QVK-AQFGFASAGGSTNVSSDNSSASNEYSYN--MSEQLL-VIGGNPIKDVTKEENL-----------AEWSKTVSTLPM 538

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1033015281 543 LIQSEPEPIYNAIPlsfpdaqprRDNLKRALDEYVAEYS 581
Cdd:PTZ00482  539 PINIELLPISTLFP---------SDDLKESYEKAVIYYS 568
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 103-140 8.90e-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: 45.66  E-value: 8.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281 103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDEEDC 140
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCG--DGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 633-673 2.10e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.27  E-value: 2.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1033015281  633 WGCWSAWSHCS----GGRRTRSRSCNNRGLTNG--ICKGDKTSEDYC 673
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGggPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 103-137 4.50e-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: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1033015281  103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDE 137
Cdd:smart00192   2 CPPGEFQCD-NGRCIPSSWVCDGVDDCG--DGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
103-140 2.14e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.85  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281 103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDEEDC 140
Cdd:pfam00057   3 CSPNEFQCG-SGECIPRSWVCDGDPDCG--DGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 44-79 6.18e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 38.03  E-value: 6.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281  44 CKMSAWSQWSPCD-PCTN-TTYRSRSIEVFGQFKGTVC 79
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPC 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
636-673 7.77e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.09  E-value: 7.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1033015281 636 WSAWSHCS----GGRRTRSRSCNNRGLTNGICKGDKTSEDYC 673
Cdd:pfam00090   3 WSPWSPCSvtcgKGIQVRQRTCKSPFPGGEPCTGDDIETQAC 44
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 354-576 2.62e-27

MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerizes into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold.


Pssm-ID: 460349  Cd Length: 211  Bit Score: 109.80  E-value: 2.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 354 KQLSELTTTKRKTFMRVKGRVELATYRM-RQRGLEVSSTFLDDVDALPLQYEKGQ---YFSFLEEYGTHFTKNGKSGGEY 429
Cdd:pfam01823  10 KKMSDKSKQKKKSLIISKSTCSLYQFTLkRSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGKI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 430 QLVYVMNEDIRKQKHVTEATVKKCFELGLKADFqltpaaeGGGEVKPLNDCNSLTNTDTDEKNNkgvIDKVLIEVKGGSA 509
Cdd:pfam01823  90 VYVLKLDKSQLEDLKLKGEDVKICLSASAGASI-------GSVNLKGCSKNSSSTKEKKSFNQE---IESSITLVIGGTP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033015281 510 ASAVamksqltkDGILDYNqyvEWAKTITILPALIQSEPEPIYNAIplsfPDAQPRRDNLKRALDEY 576
Cdd:pfam01823 160 ESID--------DDSKTYS---DWAESVKDNPMPIDFELTPISELL----KGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
367-577 2.07e-24

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 100.97  E-value: 2.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281  367 FMRVKGRVELATYRMRQRGLEVSSTFLDDVDALPLQYEKGQYFSFLEEYGTHFTKNGKSGGEYQLVYVMNEDIRKQKHVT 446
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281  447 EATVKKCFElGLKADFQLTPAAEGGGEVKplndcNSLTNTDTDEknnkgvIDKVLIEVKGGsaasAVAMKSQLTKDGILD 526
Cdd:smart00457  81 SEDISKCLA-GSSNSFAGSVSAEHCLQSS-----SYIKYLSTSL------RRESHTQVLGG----HVTVLCDLLRGPSSN 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1033015281  527 YNQYVEWAKTITILPALIQSEPEPIYNAIPlSFPDAQPRRDNLKRALDEYV 577
Cdd:smart00457 145 SLDFSDWAESVPNEPVLIDVSLAPIYELLP-PNPELSQKREALRQALRSYL 194
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 334-581 6.10e-07

membrane-attack complex/perforin (MACPF) Superfamily; Provisional


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 52.95  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 334 GFGiSGSAGANYKqtttniiKQLSELTTTKRKTFMrvkgrveLATYRMR-QRGL------EVSSTFLDDVDALPL----- 401
Cdd:PTZ00482  339 GIN-SFSASTGYK-------KFLQEVSKRTTKTYL-------LKSNCVKyTAGLppyfkwNQTTAFKNAVNGLPPvfdgl 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 402 ---------QYEKGQ----------YFSFLEEYGTHFTKNGKSGGEyqlvyvmnedIRKQKHVTEATVKKCFELGLKADF 462
Cdd:PTZ00482  404 eaesecssdVYEQDKtaeecenvpiWISFFEQYGTHIIMELQLGGK----------ITKQVTVKNSSVEQMKKDGVSVKA 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033015281 463 QLTpAAEGGGEVKPLNDCNSLTNTDTDEKNNKgvIDKVLIeVKGGSAASAVAMKSQLtkdgildynqyVEWAKTITILPA 542
Cdd:PTZ00482  474 QVK-AQFGFASAGGSTNVSSDNSSASNEYSYN--MSEQLL-VIGGNPIKDVTKEENL-----------AEWSKTVSTLPM 538

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1033015281 543 LIQSEPEPIYNAIPlsfpdaqprRDNLKRALDEYVAEYS 581
Cdd:PTZ00482  539 PINIELLPISTLFP---------SDDLKESYEKAVIYYS 568
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 103-140 8.90e-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: 45.66  E-value: 8.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281 103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDEEDC 140
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCG--DGSDEENC 35
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 633-673 2.10e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.27  E-value: 2.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1033015281  633 WGCWSAWSHCS----GGRRTRSRSCNNRGLTNG--ICKGDKTSEDYC 673
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGggPCTGEDVETRAC 47
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 103-137 4.50e-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: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1033015281  103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDE 137
Cdd:smart00192   2 CPPGEFQCD-NGRCIPSSWVCDGVDDCG--DGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
103-140 2.14e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.85  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281 103 CKSSQWQCTfTRMCINKNLRCNGDNDCGptDESDEEDC 140
Cdd:pfam00057   3 CSPNEFQCG-SGECIPRSWVCDGDPDCG--DGSDEENC 37
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 44-79 6.18e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 38.03  E-value: 6.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1033015281  44 CKMSAWSQWSPCD-PCTN-TTYRSRSIEVFGQFKGTVC 79
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPC 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
636-673 7.77e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.09  E-value: 7.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1033015281 636 WSAWSHCS----GGRRTRSRSCNNRGLTNGICKGDKTSEDYC 673
Cdd:pfam00090   3 WSPWSPCSvtcgKGIQVRQRTCKSPFPGGEPCTGDDIETQAC 44
 
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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