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Conserved domains on  [gi|161086891|ref|NP_057913|]
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complement component C6 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 296-514 1.37e-53

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: 184.15  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  296 SSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKAT-DLQLSDVFLKALVHLPLEYNSA---VYSRIFDDFGTHYFTSGSL 371
Cdd:pfam01823   6 SSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITSVTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  372 GGKYDLIYQFSRQELQNSGLTEEEAQNCVQyetKKLKFLYMEIHkEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSqq 451
Cdd:pfam01823  86 GGKIVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIGSVN-LKGCSKNSSSTKEKKSFNQEIESSITLVIGGTP-- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161086891  452 aaalawekGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLvrnIPCAVTKRNNLRRALQEY 514
Cdd:pfam01823 160 --------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 1.64e-10

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: 56.45  E-value: 1.64e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 161086891 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 1.73e-09

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 54.01  E-value: 1.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-614 3.01e-09

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: 53.36  E-value: 3.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 161086891   568 WGCWSSWSACNAA---YRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVS 614
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 8.95e-09

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: 51.90  E-value: 8.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161086891   28 PWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLcikQETRECNLQTC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
PHA02831 super family cl31511
EEV host range protein; Provisional
 641-755 2.83e-06

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02831:

Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.61  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 641 ESGCSQPPLPENAFTWNEKKLYSVGEEVEISC----LTGFTAVGFQYLRCLpDRTWSQGDVECQRTSCLKPVVQDVLtIS 716
Cdd:PHA02831  75 KRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LN 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161086891 717 PFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDS-WTPPI 755
Cdd:PHA02831 153 VFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGI 192
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.35e-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: 39.57  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161086891   82 CVLGDYGTWSDCD-PCTE-KQVKVKSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 296-514 1.37e-53

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: 184.15  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  296 SSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKAT-DLQLSDVFLKALVHLPLEYNSA---VYSRIFDDFGTHYFTSGSL 371
Cdd:pfam01823   6 SSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITSVTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  372 GGKYDLIYQFSRQELQNSGLTEEEAQNCVQyetKKLKFLYMEIHkEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSqq 451
Cdd:pfam01823  86 GGKIVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIGSVN-LKGCSKNSSSTKEKKSFNQEIESSITLVIGGTP-- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161086891  452 aaalawekGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLvrnIPCAVTKRNNLRRALQEY 514
Cdd:pfam01823 160 --------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
313-514 3.19e-50

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.54  E-value: 3.19e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891   313 FIRIHKLIKVLNFTMKATDLQLSDVFLKALVHLPLEYNSAVYSRIFDDFGTHYFTSGSLGGKYDLIYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891   393 EEEAQNCVQYETKKLKFLYmeihKEDTCTKNKLSEKYGGSFLqgSEKSISLVQGGRSQQAAALAWEKGTSGPEenvYSEW 472
Cdd:smart00457  81 SEDISKCLAGSSNSFAGSV----SAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 161086891   473 LESVKENPAVVDYKLAPITDLVRNIPCAVTKRNNLRRALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 1.64e-10

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: 56.45  E-value: 1.64e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 161086891 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 1.41e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.79  E-value: 1.41e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 161086891  138 TNCK-NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 1.73e-09

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 54.01  E-value: 1.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-614 3.01e-09

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: 53.36  E-value: 3.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 161086891   568 WGCWSSWSACNAA---YRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVS 614
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 8.95e-09

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: 51.90  E-value: 8.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161086891   28 PWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLcikQETRECNLQTC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 26-79 1.21e-08

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: 51.82  E-value: 1.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891    26 HYPWTHWSSCSKSCNSGTQSRQRQVVVNDyywKNLCDKLCIKQ--ETRECNLQTCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPP---PQNGGGPCTGEdvETRACNEQPCP 53
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 142-170 1.75e-08

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: 50.71  E-value: 1.75e-08
                           10        20
                   ....*....|....*....|....*....
gi 161086891   142 NKFLCDSGRCIPSKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 3.38e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 3.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891  644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 644-699 4.67e-08

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 50.22  E-value: 4.67e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891   644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 644-755 3.64e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 52.35  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRClPDRTWSQGDVeCQRTSCLKPVVQDVLTISPFQRVYQ 723
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225

                         90       100       110
                 ....*....|....*....|....*....|...
gi 161086891 724 IGESIELTCPRGFVVAGPSRYTCK-EDSWTPPI 755
Cdd:PHA02927 226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPEL 258
PHA02831 PHA02831
EEV host range protein; Provisional
 641-755 2.83e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.61  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 641 ESGCSQPPLPENAFTWNEKKLYSVGEEVEISC----LTGFTAVGFQYLRCLpDRTWSQGDVECQRTSCLKPVVQDVLtIS 716
Cdd:PHA02831  75 KRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LN 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161086891 717 PFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDS-WTPPI 755
Cdd:PHA02831 153 VFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGI 192
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 704-762 1.09e-04

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 40.52  E-value: 1.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 704 CLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDS-WTPPIsnsLTCE 762
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPP---PTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 704-755 1.19e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 40.59  E-value: 1.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161086891   704 CLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKED-SWTPPI 755
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.35e-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: 39.57  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161086891   82 CVLGDYGTWSDCD-PCTE-KQVKVKSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
Sushi pfam00084
Sushi repeat (SCR repeat);
722-754 7.78e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.25  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 161086891  722 YQIGESIELTCPRGFVVAGPSRYTCKED-SWTPP 754
Cdd:pfam00084  19 YNYGASVSYECDPGYRLVGSPTITCQEDgTWSPP 52
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 296-514 1.37e-53

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: 184.15  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  296 SSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKAT-DLQLSDVFLKALVHLPLEYNSA---VYSRIFDDFGTHYFTSGSL 371
Cdd:pfam01823   6 SSEFKKMSDKSKQKKKSLIISKSTCSLYQFTLKRSnKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGTHYITSVTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891  372 GGKYDLIYQFSRQELQNSGLTEEEAQNCVQyetKKLKFLYMEIHkEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSqq 451
Cdd:pfam01823  86 GGKIVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIGSVN-LKGCSKNSSSTKEKKSFNQEIESSITLVIGGTP-- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161086891  452 aaalawekGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLvrnIPCAVTKRNNLRRALQEY 514
Cdd:pfam01823 160 --------ESIDDDSKTYSDWAESVKDNPMPIDFELTPISEL---LKGVPLKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
313-514 3.19e-50

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 174.54  E-value: 3.19e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891   313 FIRIHKLIKVLNFTMKATDLQLSDVFLKALVHLPLEYNSAVYSRIFDDFGTHYFTSGSLGGKYDLIYQFSRQELQNSGLT 392
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891   393 EEEAQNCVQYETKKLKFLYmeihKEDTCTKNKLSEKYGGSFLqgSEKSISLVQGGRSQQAAALAWEKGTSGPEenvYSEW 472
Cdd:smart00457  81 SEDISKCLAGSSNSFAGSV----SAEHCLQSSSYIKYLSTSL--RRESHTQVLGGHVTVLCDLLRGPSSNSLD---FSDW 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 161086891   473 LESVKENPAVVDYKLAPITDLVRNIPCAVTKRNNLRRALQEY 514
Cdd:smart00457 152 AESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSY 193
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 142-173 1.64e-10

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: 56.45  E-value: 1.64e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 161086891 142 NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:cd00112    4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
138-173 1.41e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.79  E-value: 1.41e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 161086891  138 TNCK-NKFLCDSGRCIPSKLECNGENDCGDNSDERNC 173
Cdd:pfam00057   1 STCSpNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 644-700 1.73e-09

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 54.01  E-value: 1.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQ 700
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 568-614 3.01e-09

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: 53.36  E-value: 3.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 161086891   568 WGCWSSWSACNAA---YRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVS 614
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 28-78 8.95e-09

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: 51.90  E-value: 8.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161086891   28 PWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLcikQETRECNLQTC 78
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPEL---LERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 26-79 1.21e-08

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: 51.82  E-value: 1.21e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891    26 HYPWTHWSSCSKSCNSGTQSRQRQVVVNDyywKNLCDKLCIKQ--ETRECNLQTCP 79
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPP---PQNGGGPCTGEdvETRACNEQPCP 53
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 142-170 1.75e-08

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: 50.71  E-value: 1.75e-08
                           10        20
                   ....*....|....*....|....*....
gi 161086891   142 NKFLCDSGRCIPSKLECNGENDCGDNSDE 170
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Sushi pfam00084
Sushi repeat (SCR repeat);
644-699 3.38e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 3.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891  644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVEC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 644-699 4.67e-08

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 50.22  E-value: 4.67e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 161086891   644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVEC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 644-755 3.64e-07

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 52.35  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRClPDRTWSQGDVeCQRTSCLKPVVQDVLTISPFQRVYQ 723
Cdd:PHA02927 148 CQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVKCPHPTISNGYLSSGFKRSYS 225

                         90       100       110
                 ....*....|....*....|....*....|...
gi 161086891 724 IGESIELTCPRGFVVAGPSRYTCK-EDSWTPPI 755
Cdd:PHA02927 226 YNDNVDFKCKYGYKLSGSSSSTCSpGNTWQPEL 258
PHA02831 PHA02831
EEV host range protein; Provisional
 641-755 2.83e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 49.61  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 641 ESGCSQPPLPENAFTWNEKKLYSVGEEVEISC----LTGFTAVGFQYLRCLpDRTWSQGDVECQRTSCLKPVVQDVLtIS 716
Cdd:PHA02831  75 KRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-LN 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161086891 717 PFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDS-WTPPI 755
Cdd:PHA02831 153 VFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSiWYPGI 192
TSP_1 pfam00090
Thrombospondin type 1 domain;
28-78 5.05e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.25  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 161086891   28 PWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLcikQETRECNLQTC 78
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDD---IETQACKMDKC 49
PHA02639 PHA02639
EEV host range protein; Provisional
 644-761 1.06e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.04  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDR---TWSQGDVECQRTSCLKPVVQDVLTISPFQR 720
Cdd:PHA02639  22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKnnaIWSNKAPFCMLKECNDPPSIINGKIYNKRE 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 161086891 721 VYQIGESIELTCPR----GFVVAGPSRYTCKED-SWT--PPISNSLTC 761
Cdd:PHA02639 102 MYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKpdPPICKMINC 149
PHA02817 PHA02817
EEV Host range protein; Provisional
 644-755 1.08e-04

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 44.16  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 644 CSQPPLPENAFTWNEKKLYSVGEEVEISCLTG-----FTAVGFQYLRCLPDRTWSQGDVECQRTSCLKPVVQD-VLTISP 717
Cdd:PHA02817  24 CCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQNgFVNGIP 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 161086891 718 FQRVYQIGESIELTCPRGFVVAGPSRYTCK-EDSWTPPI 755
Cdd:PHA02817 104 DSKKFYYESEVSFSCKPGFVLIGTKYSVCGiNSSWIPKV 142
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 659-753 1.08e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 45.08  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 659 KKLYSVGEEVEISCLTGFTAVGFQYLRCLPDrTWSQGDvECQRTSCLKPVVQDVLTISPFQrvyqIGESIELTCPRGFVV 738
Cdd:PHA02954 144 KEKYSFGEHITINCDVGYEVIGASYISCTAN-SWNVIP-SCQQKCDIPSLSNGLISGSTFS----IGGVIHLSCKSGFTL 217

                         90
                 ....*....|....*
gi 161086891 739 AGPSRYTCKEDSWTP 753
Cdd:PHA02954 218 TGSPSSTCIDGKWNP 232
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 704-762 1.09e-04

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 40.52  E-value: 1.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161086891 704 CLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDS-WTPPIsnsLTCE 762
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPP---PTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 704-755 1.19e-04

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 40.59  E-value: 1.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161086891   704 CLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKED-SWTPPI 755
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENgTWSPPP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 82-127 2.35e-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: 39.57  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 161086891   82 CVLGDYGTWSDCD-PCTE-KQVKVKSVLRPSQFGGQPCTEPLVTfQPC 127
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELLER-RPC 47
Sushi pfam00084
Sushi repeat (SCR repeat);
722-754 7.78e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 38.25  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 161086891  722 YQIGESIELTCPRGFVVAGPSRYTCKED-SWTPP 754
Cdd:pfam00084  19 YNYGASVSYECDPGYRLVGSPTITCQEDgTWSPP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
85-133 4.59e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.86  E-value: 4.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 161086891   85 GDYGTWSDCDPCTEKQVKVKSVLRPSQF-GGQPCTEPLVTFQPCvPSKLC 133
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFpGGEPCTGDDIETQAC-KMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 32-78 7.86e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 35.12  E-value: 7.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 161086891   32 WSSCSKSCNSGTQSRQ---RQVVVNDYYWKNLCDKLCIKQETRECNLQTC 78
Cdd:pfam19030   6 WGECSVTCGGGVQTRLvqcVQKGGGSIVPDSECSAQKKPPETQSCNLKPC 55
 
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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