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Conserved domains on  [gi|320543806|ref|NP_001188908|]
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scavenger receptor class C, type II, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 136-311 2.10e-50

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 171.39  E-value: 2.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  136 CDFESEDQCGWSAEETIWLPWKRISAvtdfHHPRTGPRYDHTFgNTSGGHYMRMETQIEAYG-SYHFVSPVYPRSLClnv 214
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHTQ-GTGSGHFMYVDTSSGAPGqTARLLSPLLPPSRS--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  215 ACCFRFHYFMFGAGVDRLVLSVKPaslqiddmwNSFRSNSSKFEITGSQGTHWLENTITIDKMHEDFQVVFTATDARSQF 294
Cdd:pfam00629  73 PQCLRFWYHMSGSGVGTLRVYVRE---------NGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSR 143

                         170
                  ....*....|....*..
gi 320543806  295 GDIAIDDVKLmTGSECG 311
Cdd:pfam00629 144 GGIALDDISL-SSGPCP 159
Somatomedin_B pfam01033
Somatomedin B domain;
340-388 5.77e-07

Somatomedin B domain;


:

Pssm-ID: 460034  Cd Length: 40  Bit Score: 46.14  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 320543806  340 MSCTFRCG-SISPGSPlfsdegivmsCGCDDSCILNNNCCPNYFEKCVKE 388
Cdd:pfam01033   1 ESCKGRCGeSFDRGRL----------CQCDDDCVKYGDCCPDYESLCLGE 40
Sushi pfam00084
Sushi repeat (SCR repeat);
27-72 3.09e-04

Sushi repeat (SCR repeat);


:

Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.02  E-value: 3.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320543806   27 DLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:pfam00084   6 DIPNGKVSATKNEYnygasVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 22-127 1.48e-03

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.79  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  22 CEGSLDLENGR------FFTrSNNLVIFQCNRGFVLQGNSIHTCdrDGRLREKKPFCARKGCDKPEdPTNGYVLDNPVKA 95
Cdd:PHA02927 148 CQSPPSISNGRhngyedFYT-DGSVVTYSCNSGYSLIGNSGVLC--SGGEWSDPPTCQIVKCPHPT-ISNGYLSSGFKRS 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 320543806  96 -------EIVCLDGFVLYGSRTAFCD-GEKWSTQLGACRR 127
Cdd:PHA02927 224 ysyndnvDFKCKYGYKLSGSSSSTCSpGNTWQPELPKCVR 263
 
Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 136-311 2.10e-50

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 171.39  E-value: 2.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  136 CDFESEDQCGWSAEETIWLPWKRISAvtdfHHPRTGPRYDHTFgNTSGGHYMRMETQIEAYG-SYHFVSPVYPRSLClnv 214
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHTQ-GTGSGHFMYVDTSSGAPGqTARLLSPLLPPSRS--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  215 ACCFRFHYFMFGAGVDRLVLSVKPaslqiddmwNSFRSNSSKFEITGSQGTHWLENTITIDKMHEDFQVVFTATDARSQF 294
Cdd:pfam00629  73 PQCLRFWYHMSGSGVGTLRVYVRE---------NGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSR 143

                         170
                  ....*....|....*..
gi 320543806  295 GDIAIDDVKLmTGSECG 311
Cdd:pfam00629 144 GGIALDDISL-SSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 131-308 2.89e-46

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 160.20  E-value: 2.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806   131 TMDHSCDFESEDQCGWSAEETIWLPWKRISAVTdfhhPRTGPRYDHTFGNtsgGHYMRMETQIEAYGsyHFVSPVYPRSL 210
Cdd:smart00137   1 TSPGNCDFEEGSTCGWHQDSNDDGHWERVSSAT----GIPGPNRDHTTGN---GHFMFFETSSGAEG--QTARLLSPPLY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806   211 CLNVACCFRFHYFMFGAGVDRLVLSVKPASLQIDdmwnsfrsnSSKFEITGSQGTHWLENTITIDKMHEDFQVVFTATDA 290
Cdd:smart00137  72 ENRSTHCLTFWYYMYGSGSGTLNVYVRENNGSQD---------TLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRG 142

                          170
                   ....*....|....*...
gi 320543806   291 RSQFGDIAIDDVKLMTGS 308
Cdd:smart00137 143 KGHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 136-308 3.97e-37

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 135.20  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806 136 CDFEsEDQCGWSAEETIWLPWKRISAVTDFHHPRTgpryDHTFGnTSGGHYMRMETQIEAYG-SYHFVSPVYPRSlclNV 214
Cdd:cd06263    1 CDFE-DGLCGWTQDSTDDFDWTRVSGSTPSPGTPP----DHTHG-TGSGHYLYVESSSGREGqKARLLSPLLPPP---RS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806 215 ACCFRFHYFMFGAGVDRLVLSVKPASLQIDDMWnsfrsnsskFEITGSQGTHWLENTITIDKMHEDFQVVFTATDARSQF 294
Cdd:cd06263   72 SHCLSFWYHMYGSGVGTLNVYVREEGGGLGTLL---------WSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSR 142

                        170
                 ....*....|....
gi 320543806 295 GDIAIDDVKLMTGS 308
Cdd:cd06263  143 GDIALDDISLSPGP 156
Somatomedin_B pfam01033
Somatomedin B domain;
340-388 5.77e-07

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 46.14  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 320543806  340 MSCTFRCG-SISPGSPlfsdegivmsCGCDDSCILNNNCCPNYFEKCVKE 388
Cdd:pfam01033   1 ESCKGRCGeSFDRGRL----------CQCDDDCVKYGDCCPDYESLCLGE 40
Sushi pfam00084
Sushi repeat (SCR repeat);
27-72 3.09e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.02  E-value: 3.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320543806   27 DLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:pfam00084   6 DIPNGKVSATKNEYnygasVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 22-72 3.41e-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: 38.98  E-value: 3.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320543806  22 CEGSLDLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYsygstVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 22-72 4.24e-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: 38.66  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 320543806    22 CEGSLDLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYsygdtVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 338-389 4.58e-04

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 38.12  E-value: 4.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 320543806   338 DMMSCTFRCGSISPGSPLfsdegivmsCGCDDSCILNNNCCPNYFEKCVKEL 389
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA---------CRCDALCLSYGDCCTDYESVCKKEV 43
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 22-127 1.48e-03

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.79  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  22 CEGSLDLENGR------FFTrSNNLVIFQCNRGFVLQGNSIHTCdrDGRLREKKPFCARKGCDKPEdPTNGYVLDNPVKA 95
Cdd:PHA02927 148 CQSPPSISNGRhngyedFYT-DGSVVTYSCNSGYSLIGNSGVLC--SGGEWSDPPTCQIVKCPHPT-ISNGYLSSGFKRS 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 320543806  96 -------EIVCLDGFVLYGSRTAFCD-GEKWSTQLGACRR 127
Cdd:PHA02927 224 ysyndnvDFKCKYGYKLSGSSSSTCSpGNTWQPELPKCVR 263
 
Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 136-311 2.10e-50

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 171.39  E-value: 2.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  136 CDFESEDQCGWSAEETIWLPWKRISAvtdfHHPRTGPRYDHTFgNTSGGHYMRMETQIEAYG-SYHFVSPVYPRSLClnv 214
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHTQ-GTGSGHFMYVDTSSGAPGqTARLLSPLLPPSRS--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  215 ACCFRFHYFMFGAGVDRLVLSVKPaslqiddmwNSFRSNSSKFEITGSQGTHWLENTITIDKMHEDFQVVFTATDARSQF 294
Cdd:pfam00629  73 PQCLRFWYHMSGSGVGTLRVYVRE---------NGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSR 143

                         170
                  ....*....|....*..
gi 320543806  295 GDIAIDDVKLmTGSECG 311
Cdd:pfam00629 144 GGIALDDISL-SSGPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 131-308 2.89e-46

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 160.20  E-value: 2.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806   131 TMDHSCDFESEDQCGWSAEETIWLPWKRISAVTdfhhPRTGPRYDHTFGNtsgGHYMRMETQIEAYGsyHFVSPVYPRSL 210
Cdd:smart00137   1 TSPGNCDFEEGSTCGWHQDSNDDGHWERVSSAT----GIPGPNRDHTTGN---GHFMFFETSSGAEG--QTARLLSPPLY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806   211 CLNVACCFRFHYFMFGAGVDRLVLSVKPASLQIDdmwnsfrsnSSKFEITGSQGTHWLENTITIDKMHEDFQVVFTATDA 290
Cdd:smart00137  72 ENRSTHCLTFWYYMYGSGSGTLNVYVRENNGSQD---------TLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRG 142

                          170
                   ....*....|....*...
gi 320543806   291 RSQFGDIAIDDVKLMTGS 308
Cdd:smart00137 143 KGHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 136-308 3.97e-37

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 135.20  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806 136 CDFEsEDQCGWSAEETIWLPWKRISAVTDFHHPRTgpryDHTFGnTSGGHYMRMETQIEAYG-SYHFVSPVYPRSlclNV 214
Cdd:cd06263    1 CDFE-DGLCGWTQDSTDDFDWTRVSGSTPSPGTPP----DHTHG-TGSGHYLYVESSSGREGqKARLLSPLLPPP---RS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806 215 ACCFRFHYFMFGAGVDRLVLSVKPASLQIDDMWnsfrsnsskFEITGSQGTHWLENTITIDKMHEDFQVVFTATDARSQF 294
Cdd:cd06263   72 SHCLSFWYHMYGSGVGTLNVYVREEGGGLGTLL---------WSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSR 142

                        170
                 ....*....|....
gi 320543806 295 GDIAIDDVKLMTGS 308
Cdd:cd06263  143 GDIALDDISLSPGP 156
Somatomedin_B pfam01033
Somatomedin B domain;
340-388 5.77e-07

Somatomedin B domain;


Pssm-ID: 460034  Cd Length: 40  Bit Score: 46.14  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 320543806  340 MSCTFRCG-SISPGSPlfsdegivmsCGCDDSCILNNNCCPNYFEKCVKE 388
Cdd:pfam01033   1 ESCKGRCGeSFDRGRL----------CQCDDDCVKYGDCCPDYESLCLGE 40
Sushi pfam00084
Sushi repeat (SCR repeat);
27-72 3.09e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.02  E-value: 3.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320543806   27 DLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:pfam00084   6 DIPNGKVSATKNEYnygasVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 22-72 3.41e-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: 38.98  E-value: 3.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320543806  22 CEGSLDLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYsygstVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 22-72 4.24e-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: 38.66  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 320543806    22 CEGSLDLENGRFFTRSNNL-----VIFQCNRGFVLQGNSIHTCDRDGRLREKKPFC 72
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYsygdtVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
 338-389 4.58e-04

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 38.12  E-value: 4.58e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 320543806   338 DMMSCTFRCGSISPGSPLfsdegivmsCGCDDSCILNNNCCPNYFEKCVKEL 389
Cdd:smart00201   1 AIGSCKGRCGESFNEGNA---------CRCDALCLSYGDCCTDYESVCKKEV 43
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 22-127 1.48e-03

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.79  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  22 CEGSLDLENGR------FFTrSNNLVIFQCNRGFVLQGNSIHTCdrDGRLREKKPFCARKGCDKPEdPTNGYVLDNPVKA 95
Cdd:PHA02927 148 CQSPPSISNGRhngyedFYT-DGSVVTYSCNSGYSLIGNSGVLC--SGGEWSDPPTCQIVKCPHPT-ISNGYLSSGFKRS 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 320543806  96 -------EIVCLDGFVLYGSRTAFCD-GEKWSTQLGACRR 127
Cdd:PHA02927 224 ysyndnvDFKCKYGYKLSGSSSSTCSpGNTWQPELPKCVR 263
PHA02817 PHA02817
EEV Host range protein; Provisional
 49-133 6.50e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 38.38  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543806  49 FVLQGNSIHTCDRDGRLREKKPFCARKGCDKPEdPTNGYVLDNP--------VKAEIVCLDGFVLYGSRTAFCD-GEKWS 119
Cdd:PHA02817  61 YTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPA-LQNGFVNGIPdskkfyyeSEVSFSCKPGFVLIGTKYSVCGiNSSWI 139

                         90
                 ....*....|....
gi 320543806 120 TQLGACRRSNHTMD 133
Cdd:PHA02817 140 PKVPICSRDNITYN 153
 
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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