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Conserved domains on  [gi|41055345|ref|NP_956932|]
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complement component C6 [Danio rerio]

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 ...
 248-463 1.35e-51

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: 179.91  E-value: 1.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   248 YREAVKASQQKDSVFYRVHQVIATSTFKVK-SSDLYLSDPFLQFLNSLPLEYNYAL---YRHIFQLFGTHYFSSGTLGGK 323
Cdd:pfam01823   9 FKKMSDKSKQKKKSLIISKSTCSLYQFTLKrSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   324 YDLLFQFDREELKTFGLKESDSEYCLSdddTLVTFFYNrHKQRNTCGNISMKTKYEGSMVKASERCITSVQGGRTEFAaa 403
Cdd:pfam01823  89 IVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIG-SVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTPESI-- 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   404 lawekkgvSPQSTVYTDWIKSTIENPVVINYELLPLVNLVRGIScavTKRRHFHRALEEY 463
Cdd:pfam01823 163 --------DDDSKTYSDWAESVKDNPMPIDFELTPISELLKGVP---LKKENLRKALEEY 211
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 517-561 8.64e-10

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: 54.90  E-value: 8.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41055345    517 WSCWSSWSPCDAT---LKKHRSRTCSNPAPQRGGKPCPGLEKQVEECT 561
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
FIMAC super family cl42952
factor I membrane attack complex;
813-883 8.52e-08

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 49.85  E-value: 8.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055345    813 CGSDTCYEWETCSVSkTCECKMPRECPKDGKKiYCLKIVRTQTTrsMNLCFMAAMKCSSIEFELQHEGPCA 883
Cdd:smart00057   1 CAKGFCQLWQKCSAS-TCVCKLPYECPKAGTD-VCVEDGRSEKT--LTYCKQGALRCLNQKYKFLHIGSCT 67
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 123-154 9.89e-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: 9.89e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 41055345 123 DKFTCDTGRCIHADLQCNDQNDCGDNSDERDC 154
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 63-108 9.91e-08

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: 49.20  E-value: 9.91e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 41055345    63 CQLTEFGPWSECS-SCAK-KSFRIRSVLRPSQFGGADCSqSLMEERAC 108
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCP-ELLERRPC 47
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 594-650 5.34e-07

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: 47.46  E-value: 5.34e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345 594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQCI 650
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
FIMAC super family cl42952
factor I membrane attack complex;
725-787 1.51e-05

factor I membrane attack complex;


The actual alignment was detected with superfamily member smart00057:

Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 43.69  E-value: 1.51e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055345    725 CKPGEINDGTKCVCMTKERCRGYREDLCVYDAGKEtaIMMSLCAFHADRCHGDRLYFMNNGPC 787
Cdd:smart00057   6 CQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSC 66
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 7-60 3.71e-05

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: 41.80  E-value: 3.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345      7 HYPWSTWSQCTKTCDSGTQSRLRdvQYDDHWFKNSCSQlCQIHD--NRVCNVEACP 60
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTR--SCCSPPPQNGGGP-CTGEDveTRACNEQPCP 53
PHA02831 super family cl31511
EEV host range protein; Provisional
 590-722 3.72e-05

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02831:

Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.52  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345  590 GTSGCAKPLPPANSHLRINKRQYDYGDHEEIIC----FTGFELQGFQLIHCLqDGTWEKPKAQCIKKVCSKPSVPDGMtI 665
Cdd:PHA02831  74 GKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-L 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345  666 NPDRMEYKVGSDIMLVClESGTSPSGRLSYSCGKSLIWEPSIPKDIYCKIDKPYVPD 722
Cdd:PHA02831 152 NVFEKKFYYGDIVNFKC-KKGFILLGSSVSTCDINSIWYPGIPKCVKDKVHNEIQPN 207
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 248-463 1.35e-51

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: 179.91  E-value: 1.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   248 YREAVKASQQKDSVFYRVHQVIATSTFKVK-SSDLYLSDPFLQFLNSLPLEYNYAL---YRHIFQLFGTHYFSSGTLGGK 323
Cdd:pfam01823   9 FKKMSDKSKQKKKSLIISKSTCSLYQFTLKrSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   324 YDLLFQFDREELKTFGLKESDSEYCLSdddTLVTFFYNrHKQRNTCGNISMKTKYEGSMVKASERCITSVQGGRTEFAaa 403
Cdd:pfam01823  89 IVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIG-SVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTPESI-- 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   404 lawekkgvSPQSTVYTDWIKSTIENPVVINYELLPLVNLVRGIScavTKRRHFHRALEEY 463
Cdd:pfam01823 163 --------DDDSKTYSDWAESVKDNPMPIDFELTPISELLKGVP---LKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
262-465 1.14e-38

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 142.57  E-value: 1.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345    262 FYRVHQVIATSTFKVKSSDLYLSDPFLQFLNSLPLEYNYALYRHIFQLFGTHYFSSGTLGGKYDLLFQFDREELKTFGLK 341
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345    342 ESDSEYCLSDDDTLVTF-FYNRHkqrntCGNISMKTKYEGSMvkASERCITSVQGGRTEFAAALAWekkGVSPQSTVYTD 420
Cdd:smart00457  81 SEDISKCLAGSSNSFAGsVSAEH-----CLQSSSYIKYLSTS--LRRESHTQVLGGHVTVLCDLLR---GPSSNSLDFSD 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 41055345    421 WIKSTIENPVVINYELLPLVNLVRGISCAVTKRRHFHRALEEYQT 465
Cdd:smart00457 151 WAESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSYLK 195
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 517-561 8.64e-10

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: 54.90  E-value: 8.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41055345    517 WSCWSSWSPCDAT---LKKHRSRTCSNPAPQRGGKPCPGLEKQVEECT 561
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
FIMAC smart00057
factor I membrane attack complex;
813-883 8.52e-08

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 49.85  E-value: 8.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055345    813 CGSDTCYEWETCSVSkTCECKMPRECPKDGKKiYCLKIVRTQTTrsMNLCFMAAMKCSSIEFELQHEGPCA 883
Cdd:smart00057   1 CAKGFCQLWQKCSAS-TCVCKLPYECPKAGTD-VCVEDGRSEKT--LTYCKQGALRCLNQKYKFLHIGSCT 67
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 123-154 9.89e-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: 9.89e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 41055345 123 DKFTCDTGRCIHADLQCNDQNDCGDNSDERDC 154
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 63-108 9.91e-08

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: 49.20  E-value: 9.91e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 41055345    63 CQLTEFGPWSECS-SCAK-KSFRIRSVLRPSQFGGADCSqSLMEERAC 108
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCP-ELLERRPC 47
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
123-154 1.80e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.01  E-value: 1.80e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 41055345   123 DKFTCDTGRCIHADLQCNDQNDCGDNSDERDC 154
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 594-650 5.34e-07

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: 47.46  E-value: 5.34e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345 594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQCI 650
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 123-151 2.64e-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: 44.55  E-value: 2.64e-06
                           10        20
                   ....*....|....*....|....*....
gi 41055345    123 DKFTCDTGRCIHADLQCNDQNDCGDNSDE 151
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FIMAC smart00057
factor I membrane attack complex;
725-787 1.51e-05

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 43.69  E-value: 1.51e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055345    725 CKPGEINDGTKCVCMTKERCRGYREDLCVYDAGKEtaIMMSLCAFHADRCHGDRLYFMNNGPC 787
Cdd:smart00057   6 CQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSC 66
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 594-649 1.94e-05

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: 42.90  E-value: 1.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345    594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQC 649
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 7-60 3.71e-05

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: 41.80  E-value: 3.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345      7 HYPWSTWSQCTKTCDSGTQSRLRdvQYDDHWFKNSCSQlCQIHD--NRVCNVEACP 60
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTR--SCCSPPPQNGGGP-CTGEDveTRACNEQPCP 53
PHA02831 PHA02831
EEV host range protein; Provisional
 590-722 3.72e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.52  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345  590 GTSGCAKPLPPANSHLRINKRQYDYGDHEEIIC----FTGFELQGFQLIHCLqDGTWEKPKAQCIKKVCSKPSVPDGMtI 665
Cdd:PHA02831  74 GKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-L 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345  666 NPDRMEYKVGSDIMLVClESGTSPSGRLSYSCGKSLIWEPSIPKDIYCKIDKPYVPD 722
Cdd:PHA02831 152 NVFEKKFYYGDIVNFKC-KKGFILLGSSVSTCDINSIWYPGIPKCVKDKVHNEIQPN 207
Sushi pfam00084
Sushi repeat (SCR repeat);
594-649 4.38e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 41.72  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345   594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQC 649
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 520-560 1.23e-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: 40.34  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 41055345   520 WSSWSPCDATL---KKHRSRTCSNPaPQRGGKPCPGLEkQVEEC 560
Cdd:pfam19028   6 WSEWSECSVTCgggVQTRTRTVIVE-PQNGGRPCPELL-ERRPC 47
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 9-31 2.76e-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: 2.76e-04
                          10        20
                  ....*....|....*....|...
gi 41055345     9 PWSTWSQCTKTCDSGTQSRLRDV 31
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTV 27
 
Name Accession Description Interval E-value
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 248-463 1.35e-51

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: 179.91  E-value: 1.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   248 YREAVKASQQKDSVFYRVHQVIATSTFKVK-SSDLYLSDPFLQFLNSLPLEYNYAL---YRHIFQLFGTHYFSSGTLGGK 323
Cdd:pfam01823   9 FKKMSDKSKQKKKSLIISKSTCSLYQFTLKrSNKLQLSDEFLQALSDLPDNYDYAAkatYIQFFDKYGTHYITSVTLGGK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   324 YDLLFQFDREELKTFGLKESDSEYCLSdddTLVTFFYNrHKQRNTCGNISMKTKYEGSMVKASERCITSVQGGRTEFAaa 403
Cdd:pfam01823  89 IVYVLKLDKSQLEDLKLKGEDVKICLS---ASAGASIG-SVNLKGCSKNSSSTKEKKSFNQEIESSITLVIGGTPESI-- 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345   404 lawekkgvSPQSTVYTDWIKSTIENPVVINYELLPLVNLVRGIScavTKRRHFHRALEEY 463
Cdd:pfam01823 163 --------DDDSKTYSDWAESVKDNPMPIDFELTPISELLKGVP---LKKENLRKALEEY 211
MACPF smart00457
membrane-attack complex / perforin;
262-465 1.14e-38

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 142.57  E-value: 1.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345    262 FYRVHQVIATSTFKVKSSDLYLSDPFLQFLNSLPLEYNYALYRHIFQLFGTHYFSSGTLGGKYDLLFQFDREELKTFGLK 341
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345    342 ESDSEYCLSDDDTLVTF-FYNRHkqrntCGNISMKTKYEGSMvkASERCITSVQGGRTEFAAALAWekkGVSPQSTVYTD 420
Cdd:smart00457  81 SEDISKCLAGSSNSFAGsVSAEH-----CLQSSSYIKYLSTS--LRRESHTQVLGGHVTVLCDLLR---GPSSNSLDFSD 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 41055345    421 WIKSTIENPVVINYELLPLVNLVRGISCAVTKRRHFHRALEEYQT 465
Cdd:smart00457 151 WAESVPNEPVLIDVSLAPIYELLPPNPELSQKREALRQALRSYLK 195
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 517-561 8.64e-10

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: 54.90  E-value: 8.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 41055345    517 WSCWSSWSPCDAT---LKKHRSRTCSNPAPQRGGKPCPGLEKQVEECT 561
Cdd:smart00209   1 WSEWSEWSPCSVTcggGVQTRTRSCCSPPPQNGGGPCTGEDVETRACN 48
FIMAC smart00057
factor I membrane attack complex;
813-883 8.52e-08

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 49.85  E-value: 8.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41055345    813 CGSDTCYEWETCSVSkTCECKMPRECPKDGKKiYCLKIVRTQTTrsMNLCFMAAMKCSSIEFELQHEGPCA 883
Cdd:smart00057   1 CAKGFCQLWQKCSAS-TCVCKLPYECPKAGTD-VCVEDGRSEKT--LTYCKQGALRCLNQKYKFLHIGSCT 67
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 123-154 9.89e-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: 9.89e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 41055345 123 DKFTCDTGRCIHADLQCNDQNDCGDNSDERDC 154
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 63-108 9.91e-08

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: 49.20  E-value: 9.91e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 41055345    63 CQLTEFGPWSECS-SCAK-KSFRIRSVLRPSQFGGADCSqSLMEERAC 108
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCP-ELLERRPC 47
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
123-154 1.80e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.01  E-value: 1.80e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 41055345   123 DKFTCDTGRCIHADLQCNDQNDCGDNSDERDC 154
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 594-650 5.34e-07

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: 47.46  E-value: 5.34e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345 594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQCI 650
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 123-151 2.64e-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: 44.55  E-value: 2.64e-06
                           10        20
                   ....*....|....*....|....*....
gi 41055345    123 DKFTCDTGRCIHADLQCNDQNDCGDNSDE 151
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FIMAC smart00057
factor I membrane attack complex;
725-787 1.51e-05

factor I membrane attack complex;


Pssm-ID: 214493 [Multi-domain]  Cd Length: 68  Bit Score: 43.69  E-value: 1.51e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055345    725 CKPGEINDGTKCVCMTKERCRGYREDLCVYDAGKEtaIMMSLCAFHADRCHGDRLYFMNNGPC 787
Cdd:smart00057   6 CQLWQKCSASTCVCKLPYECPKAGTDVCVEDGRSE--KTLTYCKQGALRCLNQKYKFLHIGSC 66
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 594-649 1.94e-05

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: 42.90  E-value: 1.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345    594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQC 649
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 7-60 3.71e-05

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: 41.80  E-value: 3.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345      7 HYPWSTWSQCTKTCDSGTQSRLRdvQYDDHWFKNSCSQlCQIHD--NRVCNVEACP 60
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTR--SCCSPPPQNGGGP-CTGEDveTRACNEQPCP 53
PHA02831 PHA02831
EEV host range protein; Provisional
 590-722 3.72e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.52  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345  590 GTSGCAKPLPPANSHLRINKRQYDYGDHEEIIC----FTGFELQGFQLIHCLqDGTWEKPKAQCIKKVCSKPSVPDGMtI 665
Cdd:PHA02831  74 GKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKYPALQNGF-L 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055345  666 NPDRMEYKVGSDIMLVClESGTSPSGRLSYSCGKSLIWEPSIPKDIYCKIDKPYVPD 722
Cdd:PHA02831 152 NVFEKKFYYGDIVNFKC-KKGFILLGSSVSTCDINSIWYPGIPKCVKDKVHNEIQPN 207
Sushi pfam00084
Sushi repeat (SCR repeat);
594-649 4.38e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 41.72  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41055345   594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQDGTWEKPKAQC 649
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 520-560 1.23e-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: 40.34  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 41055345   520 WSSWSPCDATL---KKHRSRTCSNPaPQRGGKPCPGLEkQVEEC 560
Cdd:pfam19028   6 WSEWSECSVTCgggVQTRTRTVIVE-PQNGGRPCPELL-ERRPC 47
PHA02639 PHA02639
EEV host range protein; Provisional
 594-714 2.03e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 44.27  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345  594 CAKPLPPANSHLRINKRQYDYGDHEEIICFTGFELQGFQLIHCLQD---GTWEKPKAQCIKKVCSKP-SVPDGMTINPDR 669
Cdd:PHA02639  22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDknnAIWSNKAPFCMLKECNDPpSIINGKIYNKRE 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 41055345  670 MeYKVGSDIMLVCLESGT---SPSGRLSYSCGKSLIWEPSIP--KDIYCK 714
Cdd:PHA02639 102 M-YKVGDEIYYVCNEHKGvqySLVGNEKITCIQDKSWKPDPPicKMINCR 150
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 9-31 2.76e-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: 2.76e-04
                          10        20
                  ....*....|....*....|...
gi 41055345     9 PWSTWSQCTKTCDSGTQSRLRDV 31
Cdd:pfam19028   5 EWSEWSECSVTCGGGVQTRTRTV 27
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 597-709 1.64e-03

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 41.18  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055345  597 PLPPANSHLRINKRQYDYGDHEEII--CFTGFELQGFQLIHClQDGTWEKPKAQCIKKvCSKPSVPDGMTINPDRMEYKV 674
Cdd:PHA02927 149 QSPPSISNGRHNGYEDFYTDGSVVTysCNSGYSLIGNSGVLC-SGGEWSDPPTCQIVK-CPHPTISNGYLSSGFKRSYSY 226

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41055345  675 GSDIMLVClESGTSPSGRLSYSCGKSLIWEPSIPK 709
Cdd:PHA02927 227 NDNVDFKC-KYGYKLSGSSSSTCSPGNTWQPELPK 260
TSP_1 pfam00090
Thrombospondin type 1 domain;
518-561 3.71e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 3.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 41055345   518 SCWSSWSPCDATL---KKHRSRTCSNPAPqrGGKPCPGLEKQVEECT 561
Cdd:pfam00090   1 SPWSPWSPCSVTCgkgIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
 
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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