NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1572616317|ref|NP_038513|]
View 

complement component C9 isoform 1 precursor [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
292-506 1.70e-46

membrane-attack complex / perforin;


:

Pssm-ID: 214671  Cd Length: 195  Bit Score: 161.45  E-value: 1.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  292 FVHLRGVVQLGRFVMRNRDVVLRSTFLDDVKALPTSYEKGEYFGFLETYGTHYSTSGSLGGQYEIVYVLDKASMKEKGVD 371
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  372 LNDVKHCLGFNmdlriplqddlkDASVTASVNADGCIKTDNGKTVNITRDniIDDVISFIRGGtreqAILLKEKILRGDK 451
Cdd:smart00457  81 SEDISKCLAGS------------SNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG----HVTVLCDLLRGPS 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1572616317  452 TfDKTDFANWASSLANAPALISQRMSPIYNLIPlKIKDAYIKKQNLEKAVEDYID 506
Cdd:smart00457 143 S-NSLDFSDWAESVPNEPVLIDVSLAPIYELLP-PNPELSQKREALRQALRSYLK 195
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
101-132 2.06e-11

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.41  E-value: 2.06e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1572616317 101 NDFQCETGRCIKRRLLCNGDNDCGDYSDENDC 132
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 41-92 1.55e-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: 50.74  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1572616317  41 CRMSPWSNWSECD-PCLK-QRFRSRSILAFGQFNGKSCVDVLgDRQGCEpTQEC 92
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELL-ERRPCN-LPPC 52
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
292-506 1.70e-46

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 161.45  E-value: 1.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  292 FVHLRGVVQLGRFVMRNRDVVLRSTFLDDVKALPTSYEKGEYFGFLETYGTHYSTSGSLGGQYEIVYVLDKASMKEKGVD 371
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  372 LNDVKHCLGFNmdlriplqddlkDASVTASVNADGCIKTDNGKTVNITRDniIDDVISFIRGGtreqAILLKEKILRGDK 451
Cdd:smart00457  81 SEDISKCLAGS------------SNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG----HVTVLCDLLRGPS 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1572616317  452 TfDKTDFANWASSLANAPALISQRMSPIYNLIPlKIKDAYIKKQNLEKAVEDYID 506
Cdd:smart00457 143 S-NSLDFSDWAESVPNEPVLIDVSLAPIYELLP-PNPELSQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 267-504 7.08e-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: 124.83  E-value: 7.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 267 KFKFSyfmgKNFRRLSSYFSQSKKMFVHLRGVVQLGRFVM-RNRDVVLRSTFLDDVKALPTSYEKG---EYFGFLETYGT 342
Cdd:pfam01823   2 SFSAS----SEFKKMSDKSKQKKKSLIISKSTCSLYQFTLkRSNKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 343 HYSTSGSLGGQYEIVYVLDKASMKEKGVDLNDVKHCLgfnmdlriplqdDLKDASVTASVNADGCIKTDNGKTVNITRDN 422
Cdd:pfam01823  78 HYITSVTLGGKIVYVLKLDKSQLEDLKLKGEDVKICL------------SASAGASIGSVNLKGCSKNSSSTKEKKSFNQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 423 IIDDVISFIRGGTREQAILlkekilrgdktfDKTDFANWASSLANAPALISQRMSPIYNLIPlkikDAYIKKQNLEKAVE 502
Cdd:pfam01823 146 EIESSITLVIGGTPESIDD------------DSKTYSDWAESVKDNPMPIDFELTPISELLK----GVPLKKENLRKALE 209


                  ..
gi 1572616317 503 DY 504
Cdd:pfam01823 210 EY 211
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
101-132 2.06e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.41  E-value: 2.06e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1572616317 101 NDFQCETGRCIKRRLLCNGDNDCGDYSDENDC 132
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 101-132 3.10e-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: 55.29  E-value: 3.10e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1572616317 101 NDFQCETGRCIKRRLLCNGDNDCGDYSDENDC 132
Cdd:cd00112     4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 101-129 7.54e-09

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: 51.09  E-value: 7.54e-09
                           10        20
                   ....*....|....*....|....*....
gi 1572616317  101 NDFQCETGRCIKRRLLCNGDNDCGDYSDE 129
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 41-92 1.55e-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: 50.74  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1572616317  41 CRMSPWSNWSECD-PCLK-QRFRSRSILAFGQFNGKSCVDVLgDRQGCEpTQEC 92
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELL-ERRPCN-LPPC 52
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 336-504 5.49e-06

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 49.48  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 336 FLETYGTHYSTSGSLGGQyeIVYVL-----DKASMKEKGVDLN-DVKHCLGFnmdlriplqddlkdASVTASVNadgcIK 409
Cdd:PTZ00482  432 FFEQYGTHIIMELQLGGK--ITKQVtvknsSVEQMKKDGVSVKaQVKAQFGF--------------ASAGGSTN----VS 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 410 TDNGKTVNITRDNIiddvisfirggtREQAILLKEKILrGDKTfDKTDFANWASSLANAPALISQRMSPIYNLIPL-KIK 488
Cdd:PTZ00482  492 SDNSSASNEYSYNM------------SEQLLVIGGNPI-KDVT-KEENLAEWSKTVSTLPMPINIELLPISTLFPSdDLK 557

                         170
                  ....*....|....*.
gi 1572616317 489 DAYikkqnlEKAVEDY 504
Cdd:PTZ00482  558 ESY------EKAVIYY 567
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 43-93 1.10e-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: 37.18  E-value: 1.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1572616317   43 MSPWSNWSECD-PCLK-QRFRSRS-ILAFGQFNGKSCVDVLGDRQGCEpTQECE 93
Cdd:smart00209   1 WSEWSEWSPCSvTCGGgVQTRTRScCSPPPQNGGGPCTGEDVETRACN-EQPCP 53
 
Name Accession Description Interval E-value
MACPF smart00457
membrane-attack complex / perforin;
292-506 1.70e-46

membrane-attack complex / perforin;


Pssm-ID: 214671  Cd Length: 195  Bit Score: 161.45  E-value: 1.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  292 FVHLRGVVQLGRFVMRNRDVVLRSTFLDDVKALPTSYEKGEYFGFLETYGTHYSTSGSLGGQYEIVYVLDKASMKEKGVD 371
Cdd:smart00457   1 FLVARDTVRNRLYSVKLDELPLALEFLKALRDLPDTYNRGAYARFIDDYGTHYITSATLGGEYSLLLVLDKESLERKGLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317  372 LNDVKHCLGFNmdlriplqddlkDASVTASVNADGCIKTDNGKTVNITRDniIDDVISFIRGGtreqAILLKEKILRGDK 451
Cdd:smart00457  81 SEDISKCLAGS------------SNSFAGSVSAEHCLQSSSYIKYLSTSL--RRESHTQVLGG----HVTVLCDLLRGPS 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1572616317  452 TfDKTDFANWASSLANAPALISQRMSPIYNLIPlKIKDAYIKKQNLEKAVEDYID 506
Cdd:smart00457 143 S-NSLDFSDWAESVPNEPVLIDVSLAPIYELLP-PNPELSQKREALRQALRSYLK 195
MACPF pfam01823
MAC/Perforin domain; The membrane-attack complex (MAC) of the complement system forms ...
 267-504 7.08e-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: 124.83  E-value: 7.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 267 KFKFSyfmgKNFRRLSSYFSQSKKMFVHLRGVVQLGRFVM-RNRDVVLRSTFLDDVKALPTSYEKG---EYFGFLETYGT 342
Cdd:pfam01823   2 SFSAS----SEFKKMSDKSKQKKKSLIISKSTCSLYQFTLkRSNKLQLSDEFLQALSDLPDNYDYAakaTYIQFFDKYGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 343 HYSTSGSLGGQYEIVYVLDKASMKEKGVDLNDVKHCLgfnmdlriplqdDLKDASVTASVNADGCIKTDNGKTVNITRDN 422
Cdd:pfam01823  78 HYITSVTLGGKIVYVLKLDKSQLEDLKLKGEDVKICL------------SASAGASIGSVNLKGCSKNSSSTKEKKSFNQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 423 IIDDVISFIRGGTREQAILlkekilrgdktfDKTDFANWASSLANAPALISQRMSPIYNLIPlkikDAYIKKQNLEKAVE 502
Cdd:pfam01823 146 EIESSITLVIGGTPESIDD------------DSKTYSDWAESVKDNPMPIDFELTPISELLK----GVPLKKENLRKALE 209


                  ..
gi 1572616317 503 DY 504
Cdd:pfam01823 210 EY 211
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
101-132 2.06e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.41  E-value: 2.06e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1572616317 101 NDFQCETGRCIKRRLLCNGDNDCGDYSDENDC 132
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 101-132 3.10e-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: 55.29  E-value: 3.10e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1572616317 101 NDFQCETGRCIKRRLLCNGDNDCGDYSDENDC 132
Cdd:cd00112     4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 101-129 7.54e-09

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: 51.09  E-value: 7.54e-09
                           10        20
                   ....*....|....*....|....*....
gi 1572616317  101 NDFQCETGRCIKRRLLCNGDNDCGDYSDE 129
Cdd:smart00192   5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 41-92 1.55e-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: 50.74  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1572616317  41 CRMSPWSNWSECD-PCLK-QRFRSRSILAFGQFNGKSCVDVLgDRQGCEpTQEC 92
Cdd:pfam19028   1 CVVSEWSEWSECSvTCGGgVQTRTRTVIVEPQNGGRPCPELL-ERRPCN-LPPC 52
PTZ00482 PTZ00482
membrane-attack complex/perforin (MACPF) Superfamily; Provisional
 336-504 5.49e-06

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


Pssm-ID: 240433 [Multi-domain]  Cd Length: 844  Bit Score: 49.48  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 336 FLETYGTHYSTSGSLGGQyeIVYVL-----DKASMKEKGVDLN-DVKHCLGFnmdlriplqddlkdASVTASVNadgcIK 409
Cdd:PTZ00482  432 FFEQYGTHIIMELQLGGK--ITKQVtvknsSVEQMKKDGVSVKaQVKAQFGF--------------ASAGGSTN----VS 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616317 410 TDNGKTVNITRDNIiddvisfirggtREQAILLKEKILrGDKTfDKTDFANWASSLANAPALISQRMSPIYNLIPL-KIK 488
Cdd:PTZ00482  492 SDNSSASNEYSYNM------------SEQLLVIGGNPI-KDVT-KEENLAEWSKTVSTLPMPINIELLPISTLFPSdDLK 557

                         170
                  ....*....|....*.
gi 1572616317 489 DAYikkqnlEKAVEDY 504
Cdd:PTZ00482  558 ESY------EKAVIYY 567
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 43-93 1.10e-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: 37.18  E-value: 1.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1572616317   43 MSPWSNWSECD-PCLK-QRFRSRS-ILAFGQFNGKSCVDVLGDRQGCEpTQECE 93
Cdd:smart00209   1 WSEWSEWSPCSvTCGGgVQTRTRScCSPPPQNGGGPCTGEDVETRACN-EQPCP 53
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH