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Conserved domains on  [gi|1890341535|ref|NP_001265473|]
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complement component C8 beta chain isoform 3 [Homo sapiens]

Protein Classification

LDLa and MACPF domain-containing protein( domain architecture ID 11081371)

protein containing domains LDLa, MACPF, and TSP1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
230-436 7.77e-58

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 190.72  E-value: 7.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  230 FLHARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIYEYTLVMNKEAMERGDYT 309
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  310 LNNVHACakndfkigGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDtmVEDLVVLVRGGaseHITTLAYQELPTAD---L 386
Cdd:smart00457  81 SEDISKC--------LAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG---HVTVLCDLLRGPSSnslD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1890341535  387 MQEWGDAVQYNPAIIKVKVEPLYELVTATDFAysSTVRQNMKQALEEFQK 436
Cdd:smart00457 148 FSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYLK 195
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 486-529 1.69e-12

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: 62.22  E-value: 1.69e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1890341535  486 WNCWSNWSSCS----GRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS 529
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
58-93 1.70e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.32  E-value: 1.70e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1890341535  58 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 93
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
230-436 7.77e-58

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 190.72  E-value: 7.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  230 FLHARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIYEYTLVMNKEAMERGDYT 309
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  310 LNNVHACakndfkigGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDtmVEDLVVLVRGGaseHITTLAYQELPTAD---L 386
Cdd:smart00457  81 SEDISKC--------LAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG---HVTVLCDLLRGPSSnslD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1890341535  387 MQEWGDAVQYNPAIIKVKVEPLYELVTATDFAysSTVRQNMKQALEEFQK 436
Cdd:smart00457 148 FSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 224-434 1.85e-34

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: 129.06  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 224 SHTKSVFLHARSDLEVAHYKLKPRS-LMLHYEFLQRVKRLPLEYSYG---EYRDLFRDFGTHYITEAVLGGIYEYTLVMN 299
Cdd:pfam01823  17 KQKKKSLIISKSTCSLYQFTLKRSNkLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITSVTLGGKIVYVLKLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 300 KEAMERGDYTLNNVHACAKNDFKIggaieevyVSLGVSVGKCRGILNEIKDRNKRDTMVEDLVVLVRGGASEHITtlayq 379
Cdd:pfam01823  97 KSQLEDLKLKGEDVKICLSASAGA--------SIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTPESID----- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890341535 380 elPTADLMQEWGDAVQYNPAIIKVKVEPLYELVTAtdfaySSTVRQNMKQALEEF 434
Cdd:pfam01823 164 --DDSKTYSDWAESVKDNPMPIDFELTPISELLKG-----VPLKKENLRKALEEY 211
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 486-529 1.69e-12

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: 62.22  E-value: 1.69e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1890341535  486 WNCWSNWSSCS----GRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS 529
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
58-93 1.70e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.32  E-value: 1.70e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1890341535  58 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 93
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 63-93 6.12e-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: 48.74  E-value: 6.12e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1890341535  63 FVCAqTGRCVNRRLLCNGDNDCGDQSDEANC 93
Cdd:cd00112     6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 63-90 2.22e-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: 2.22e-06
                           10        20
                   ....*....|....*....|....*...
gi 1890341535   63 FVCAqTGRCVNRRLLCNGDNDCGDQSDE 90
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 275-431 5.63e-04

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 42.93  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 275 FRDFGTHYITEAVLGGIYEYTLVMNK---EAMERgdytlNNVHACAKNDFKIGGAieEVYVSLGVSVGKcrgilNEIKDR 351
Cdd:PTZ00482  433 FEQYGTHIIMELQLGGKITKQVTVKNssvEQMKK-----DGVSVKAQVKAQFGFA--SAGGSTNVSSDN-----SSASNE 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 352 NKRDtMVEDLVVLvrGGAsehittlayqelPTADL-----MQEWGDAVQYNPAIIKVKVEPLYELVTATDfaysstVRQN 426
Cdd:PTZ00482  501 YSYN-MSEQLLVI--GGN------------PIKDVtkeenLAEWSKTVSTLPMPINIELLPISTLFPSDD------LKES 559


                  ....*
gi 1890341535 427 MKQAL 431
Cdd:PTZ00482  560 YEKAV 564
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
230-436 7.77e-58

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 190.72  E-value: 7.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  230 FLHARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIYEYTLVMNKEAMERGDYT 309
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535  310 LNNVHACakndfkigGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDtmVEDLVVLVRGGaseHITTLAYQELPTAD---L 386
Cdd:smart00457  81 SEDISKC--------LAGSSNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG---HVTVLCDLLRGPSSnslD 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1890341535  387 MQEWGDAVQYNPAIIKVKVEPLYELVTATDFAysSTVRQNMKQALEEFQK 436
Cdd:smart00457 148 FSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 224-434 1.85e-34

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: 129.06  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 224 SHTKSVFLHARSDLEVAHYKLKPRS-LMLHYEFLQRVKRLPLEYSYG---EYRDLFRDFGTHYITEAVLGGIYEYTLVMN 299
Cdd:pfam01823  17 KQKKKSLIISKSTCSLYQFTLKRSNkLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITSVTLGGKIVYVLKLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 300 KEAMERGDYTLNNVHACAKNDFKIggaieevyVSLGVSVGKCRGILNEIKDRNKRDTMVEDLVVLVRGGASEHITtlayq 379
Cdd:pfam01823  97 KSQLEDLKLKGEDVKICLSASAGA--------SIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTPESID----- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890341535 380 elPTADLMQEWGDAVQYNPAIIKVKVEPLYELVTAtdfaySSTVRQNMKQALEEF 434
Cdd:pfam01823 164 --DDSKTYSDWAESVKDNPMPIDFELTPISELLKG-----VPLKKENLRKALEEY 211
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 486-529 1.69e-12

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: 62.22  E-value: 1.69e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1890341535  486 WNCWSNWSSCS----GRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS 529
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
58-93 1.70e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.32  E-value: 1.70e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1890341535  58 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 93
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 63-93 6.12e-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: 48.74  E-value: 6.12e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1890341535  63 FVCAqTGRCVNRRLLCNGDNDCGDQSDEANC 93
Cdd:cd00112     6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 63-90 2.22e-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: 2.22e-06
                           10        20
                   ....*....|....*....|....*...
gi 1890341535   63 FVCAqTGRCVNRRLLCNGDNDCGDQSDE 90
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 275-431 5.63e-04

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 42.93  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 275 FRDFGTHYITEAVLGGIYEYTLVMNK---EAMERgdytlNNVHACAKNDFKIGGAieEVYVSLGVSVGKcrgilNEIKDR 351
Cdd:PTZ00482  433 FEQYGTHIIMELQLGGKITKQVTVKNssvEQMKK-----DGVSVKAQVKAQFGFA--SAGGSTNVSSDN-----SSASNE 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890341535 352 NKRDtMVEDLVVLvrGGAsehittlayqelPTADL-----MQEWGDAVQYNPAIIKVKVEPLYELVTATDfaysstVRQN 426
Cdd:PTZ00482  501 YSYN-MSEQLLVI--GGN------------PIKDVtkeenLAEWSKTVSTLPMPINIELLPISTLFPSDD------LKES 559


                  ....*
gi 1890341535 427 MKQAL 431
Cdd:PTZ00482  560 YEKAV 564
 
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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