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Conserved domains on  [gi|33563297|ref|NP_598643|]
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complement component C8 beta chain isoform 1 preproprotein [Mus musculus]

Protein Classification

thrombospondin type-1 domain-containing protein; MACPF domain-containing protein( domain architecture ID 11259063)

thrombospondin type-1 (TSP1) domain-containing protein similar to Mus musculus thrombospondin type-1 domain-containing protein 1, which is a positive regulator of nascent focal adhesion assembly, involved in the modulation of endothelial cell attachment to the extracellular matrix| MACPF (MAC/Perforin) domain-containing protein may facilitate membrane insertion and pore formation; similar to Plasmodium perforin-like protein 4 that plays an essential role in ookinete midgut passage

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
291-496 9.94e-47

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 162.60  E-value: 9.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    291 FLHARSVLEVAHYKLKSRSLMLHYEFLQRVKSLPLEYSYGEYRDLLRDFGTHFITEAVLGGIYEYTLIMNKDAMEQGDYT 370
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    371 LSHVTACAGGS---FGIGGmvykvyvkvgvSAKKCSDIMKEINERNKRStmVEDLVVLVRGGTsedITALAYKELPT--- 444
Cdd:smart00457  81 SEDISKCLAGSsnsFAGSV-----------SAEHCLQSSSYIKYLSTSL--RRESHTQVLGGH---VTVLCDLLRGPssn 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 33563297    445 PELMEAWGDAVKYNPAIIKIKAEPLYELVTATDFAysSTVKQNLKKALEEFQ 496
Cdd:smart00457 145 SLDFSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYL 194
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 547-589 1.62e-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: 1.62e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 33563297    547 WSCWSDWSACS----GGHKTRHRQCNNPAPHKGGSPCSGPASETLNC 589
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
119-154 4.34e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 4.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 33563297   119 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 154
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 67-115 1.59e-03

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: 36.80  E-value: 1.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 33563297     67 STWSSWTACD----PCQKKRYRhTYLLRPSQFYGELCDLSDKEVEDCVTnQPC 115
Cdd:smart00209   2 SEWSEWSPCSvtcgGGVQTRTR-SCCSPPPQNGGGPCTGEDVETRACNE-QPC 52
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
291-496 9.94e-47

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 162.60  E-value: 9.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    291 FLHARSVLEVAHYKLKSRSLMLHYEFLQRVKSLPLEYSYGEYRDLLRDFGTHFITEAVLGGIYEYTLIMNKDAMEQGDYT 370
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    371 LSHVTACAGGS---FGIGGmvykvyvkvgvSAKKCSDIMKEINERNKRStmVEDLVVLVRGGTsedITALAYKELPT--- 444
Cdd:smart00457  81 SEDISKCLAGSsnsFAGSV-----------SAEHCLQSSSYIKYLSTSL--RRESHTQVLGGH---VTVLCDLLRGPssn 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 33563297    445 PELMEAWGDAVKYNPAIIKIKAEPLYELVTATDFAysSTVKQNLKKALEEFQ 496
Cdd:smart00457 145 SLDFSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYL 194
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 271-495 2.39e-33

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: 126.75  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297   271 SNEGKNYVTRTKrfaHTQSKFLHARSVLEVAHYKLK-SRSLMLHYEFLQRVKSLPLEYSYG---EYRDLLRDFGTHFITE 346
Cdd:pfam01823   6 SSEFKKMSDKSK---QKKKSLIISKSTCSLYQFTLKrSNKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297   347 AVLGGIYEYTLIMNKDAMEQGDYTLSHVTACAGGSFGIggmvykvyVKVGVSAKKCSDIMKEINERNKRSTMVEDLVVLV 426
Cdd:pfam01823  83 VTLGGKIVYVLKLDKSQLEDLKLKGEDVKICLSASAGA--------SIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33563297   427 RGGTSEDITalaykelPTPELMEAWGDAVKYNPAIIKIKAEPLYELVTAtdfaySSTVKQNLKKALEEF 495
Cdd:pfam01823 155 IGGTPESID-------DDSKTYSDWAESVKDNPMPIDFELTPISELLKG-----VPLKKENLRKALEEY 211
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 547-589 1.62e-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: 1.62e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 33563297    547 WSCWSDWSACS----GGHKTRHRQCNNPAPHKGGSPCSGPASETLNC 589
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
119-154 4.34e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 4.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 33563297   119 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 154
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 124-154 1.30e-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: 47.97  E-value: 1.30e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 33563297 124 FVCAqTGRCVNRRLLCNGDNDCGDQSDEANC 154
Cdd:cd00112   6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
548-589 6.43e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 6.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 33563297   548 SCWSDWSACS----GGHKTRHRQCNNPAPhkGGSPCSGPASETLNC 589
Cdd:pfam00090   1 SPWSPWSPCSvtcgKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 124-151 4.39e-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: 43.39  E-value: 4.39e-06
                           10        20
                   ....*....|....*....|....*...
gi 33563297    124 FVCAqTGRCVNRRLLCNGDNDCGDQSDE 151
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 339-492 1.21e-04

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 45.24  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297  339 FGTHFITEAVLGGIYEYTLIMNKDAMEQ----GDYTLSHVTACAGGsFGIGGmvykvyvkvgvSAKKCSDIMKEINERNk 414
Cdd:PTZ00482 436 YGTHIIMELQLGGKITKQVTVKNSSVEQmkkdGVSVKAQVKAQFGF-ASAGG-----------STNVSSDNSSASNEYS- 502

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33563297  415 rSTMVEDLVVLvrGGTSeditalaYKELPTPELMEAWGDAVKYNPAIIKIKAEPLYELVTATDfaysstVKQNLKKAL 492
Cdd:PTZ00482 503 -YNMSEQLLVI--GGNP-------IKDVTKEENLAEWSKTVSTLPMPINIELLPISTLFPSDD------LKESYEKAV 564
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 67-115 1.59e-03

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: 36.80  E-value: 1.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 33563297     67 STWSSWTACD----PCQKKRYRhTYLLRPSQFYGELCDLSDKEVEDCVTnQPC 115
Cdd:smart00209   2 SEWSEWSPCSvtcgGGVQTRTR-SCCSPPPQNGGGPCTGEDVETRACNE-QPC 52
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
291-496 9.94e-47

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 162.60  E-value: 9.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    291 FLHARSVLEVAHYKLKSRSLMLHYEFLQRVKSLPLEYSYGEYRDLLRDFGTHFITEAVLGGIYEYTLIMNKDAMEQGDYT 370
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297    371 LSHVTACAGGS---FGIGGmvykvyvkvgvSAKKCSDIMKEINERNKRStmVEDLVVLVRGGTsedITALAYKELPT--- 444
Cdd:smart00457  81 SEDISKCLAGSsnsFAGSV-----------SAEHCLQSSSYIKYLSTSL--RRESHTQVLGGH---VTVLCDLLRGPssn 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 33563297    445 PELMEAWGDAVKYNPAIIKIKAEPLYELVTATDFAysSTVKQNLKKALEEFQ 496
Cdd:smart00457 145 SLDFSDWAESVPNEPVLIDVSLAPIYELLPPNPEL--SQKREALRQALRSYL 194
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 271-495 2.39e-33

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: 126.75  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297   271 SNEGKNYVTRTKrfaHTQSKFLHARSVLEVAHYKLK-SRSLMLHYEFLQRVKSLPLEYSYG---EYRDLLRDFGTHFITE 346
Cdd:pfam01823   6 SSEFKKMSDKSK---QKKKSLIISKSTCSLYQFTLKrSNKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297   347 AVLGGIYEYTLIMNKDAMEQGDYTLSHVTACAGGSFGIggmvykvyVKVGVSAKKCSDIMKEINERNKRSTMVEDLVVLV 426
Cdd:pfam01823  83 VTLGGKIVYVLKLDKSQLEDLKLKGEDVKICLSASAGA--------SIGSVNLKGCSKNSSSTKEKKSFNQEIESSITLV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33563297   427 RGGTSEDITalaykelPTPELMEAWGDAVKYNPAIIKIKAEPLYELVTAtdfaySSTVKQNLKKALEEF 495
Cdd:pfam01823 155 IGGTPESID-------DDSKTYSDWAESVKDNPMPIDFELTPISELLKG-----VPLKKENLRKALEEY 211
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 547-589 1.62e-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: 1.62e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 33563297    547 WSCWSDWSACS----GGHKTRHRQCNNPAPHKGGSPCSGPASETLNC 589
Cdd:smart00209   1 WSEWSEWSPCSvtcgGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
119-154 4.34e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.17  E-value: 4.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 33563297   119 VRCE--GFVCaQTGRCVNRRLLCNGDNDCGDQSDEANC 154
Cdd:pfam00057   1 STCSpnEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 124-154 1.30e-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: 47.97  E-value: 1.30e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 33563297 124 FVCAqTGRCVNRRLLCNGDNDCGDQSDEANC 154
Cdd:cd00112   6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP_1 pfam00090
Thrombospondin type 1 domain;
548-589 6.43e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 6.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 33563297   548 SCWSDWSACS----GGHKTRHRQCNNPAPhkGGSPCSGPASETLNC 589
Cdd:pfam00090   1 SPWSPWSPCSvtcgKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 124-151 4.39e-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: 43.39  E-value: 4.39e-06
                           10        20
                   ....*....|....*....|....*...
gi 33563297    124 FVCAqTGRCVNRRLLCNGDNDCGDQSDE 151
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 339-492 1.21e-04

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 45.24  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563297  339 FGTHFITEAVLGGIYEYTLIMNKDAMEQ----GDYTLSHVTACAGGsFGIGGmvykvyvkvgvSAKKCSDIMKEINERNk 414
Cdd:PTZ00482 436 YGTHIIMELQLGGKITKQVTVKNSSVEQmkkdGVSVKAQVKAQFGF-ASAGG-----------STNVSSDNSSASNEYS- 502

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33563297  415 rSTMVEDLVVLvrGGTSeditalaYKELPTPELMEAWGDAVKYNPAIIKIKAEPLYELVTATDfaysstVKQNLKKAL 492
Cdd:PTZ00482 503 -YNMSEQLLVI--GGNP-------IKDVTKEENLAEWSKTVSTLPMPINIELLPISTLFPSDD------LKESYEKAV 564
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 67-115 1.59e-03

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: 36.80  E-value: 1.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 33563297     67 STWSSWTACD----PCQKKRYRhTYLLRPSQFYGELCDLSDKEVEDCVTnQPC 115
Cdd:smart00209   2 SEWSEWSPCSvtcgGGVQTRTR-SCCSPPPQNGGGPCTGEDVETRACNE-QPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 550-579 3.00e-03

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: 36.10  E-value: 3.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 33563297   550 WSDWSACS----GGHKTRHRQCNNPAPHkGGSPC 579
Cdd:pfam19028   6 WSEWSECSvtcgGGVQTRTRTVIVEPQN-GGRPC 38
 
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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