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Conserved domains on  [gi|386769253|ref|NP_001245923|]
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uninflatable, isoform E [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 326-435 3.15e-27

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 3.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  326 CGGTLKATLQrQILTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIAD----GRDFLMIRDGESPMSRTIAKLTGK 401
Cdd:cd00041     1 CGGTLTASTS-GTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 386769253  402 TAqnNRVIISTGNALYLYFKSSLGEAGKGFSLRY 435
Cdd:cd00041    80 TL--PPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 220-319 3.98e-21

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 90.93  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEK----TFDTVQILVGGRTEdkSVSLATLSGKQdlTTQPFVS 295
Cdd:cd00041    12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTS--SPLLGRFCGST--LPPPIIS 87

                          90       100
                  ....*....|....*....|....
gi 386769253  296 ASNFMIVKFTTDGSVERKGFRATW 319
Cdd:cd00041    88 SGNSLTVRFRSDSSVTGRGFKATY 111
FA58C super family cl25480
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 833-976 6.92e-19

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


The actual alignment was detected with superfamily member cd00057:

Pssm-ID: 330301 [Multi-domain]  Cd Length: 143  Bit Score: 85.87  E-value: 6.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  833 GDLGLgNGGIPDDSIT-TSVSEPGYSKEQLRLN-TNGWCGGSSEPgANWILIDLKAPTILRGFRTMSVQRPDGNvAFSSA 910
Cdd:cd00057     1 EPLGM-ESGLADDQITaSSSYSSGWEASRARLNsDNAWTPAVNDP-PQWLQVDLGKTRRVTGIQTQGRKGGGSS-EWVTS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  911 VRLQYTNDLTD--VFKD-------YANPDGTAVefrileptlsILN-LPLPIEARYIRFRIQDYVGAPCLRMELMG 976
Cdd:cd00057    78 YKVQYSLDGETwtTYKDkgeekvfTGNSDGSTP----------VTNdFPPPIVARYIRILPTTWNGNISLRLELYG 143
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 36-167 2.14e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 80.72  E-value: 2.14e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253     36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETLAIARasdpNQRASDKYWLGLASLDDLRTNTL 115
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLK----NSGSSDYYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386769253    116 ESASGAliSQYSgYWSLHQPNAESGECVaaAFAGKSQSWDLGTCESLLPFMC 167
Cdd:smart00034   77 SDGSGP--VSYS-NWAPGEPNNSSGDCV--VLSTSGGKWNDVSCTSKLPFVC 123
FA58C super family cl25480
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1303-1443 4.75e-17

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


The actual alignment was detected with superfamily member cd00057:

Pssm-ID: 330301 [Multi-domain]  Cd Length: 143  Bit Score: 80.47  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253 1303 PLGLSSGRIPDSAINATSERPNYEAKNIRLNSATGWC-GKQEAFTYVSVDLGQIYRVKAILVKGVVTNDIVGRPTEIRFF 1381
Cdd:cd00057     2 PLGMESGLADDQITASSSYSSGWEASRARLNSDNAWTpAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTSYKVQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769253 1382 YKQaESENYVVYFPNFNLtMRDPGNYGELAMIT--LPKFVQARFVILGIVSYMDNACLKFELMG 1443
Cdd:cd00057    82 YSL-DGETWTTYKDKGEE-KVFTGNSDGSTPVTndFPPPIVARYIRILPTTWNGNISLRLELYG 143
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 439-550 1.76e-15

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 75.14  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  439 CKATITA-RNGTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKSDN-----VQVFDGSSTSGLRLHSgngF 512
Cdd:cd00041     1 CGGTLTAsTSGTISSPNYP-NNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSSPLLGR---F 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386769253  513 TGPAAPKlTLTASSGEMLIKFTSDALHNAAGWSATFSA 550
Cdd:cd00041    77 CGSTLPP-PIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1862-1909 2.43e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.38  E-value: 2.43e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1862 GTYVSEGQNSCTYCPRGYYQNRDRQGTCLRCPAGTYTKEEGTKSQADC 1909
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3315-3362 3.08e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.00  E-value: 3.08e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3315 GTYLNATQNMCIECRKGYYQSESQQTSCLQCPPNHSTKITGATSKSEC 3362
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1973-2020 6.21e-14

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 68.53  E-value: 6.21e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1973 GTYSATGLAPCSPCPLHHYQGAAGAQSCNECPSNMRTDSPASKGREQC 2020
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
HYR super family cl47740
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 2799-2877 4.02e-13

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


The actual alignment was detected with superfamily member pfam02494:

Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 67.03  E-value: 4.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2799 VDKEPPVVEhCPGDLWVIAK--NGSAVVSWDEPHFSDNIGVTKIYERNGHrSGTTLLWGTYDITYIASDAAGNTASCSFK 2876
Cdd:pfam02494    1 VDTTPPTVK-CPNNIVRTVElgTSTVRVFFTEPTAFDNSGQAILVSRTAQ-PGDFFPVGTTTVTYVAYDNSGNRASCTFT 78


                   .
gi 386769253  2877 V 2877
Cdd:pfam02494   79 V 79
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1051-1106 4.49e-13

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: 66.33  E-value: 4.49e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253 1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3207-3254 2.94e-12

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 63.52  E-value: 2.94e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3207 GKYFDAETGLCRSCGHGFYQPNEGSFSCELCGLGQTTRSTEATSRKEC 3254
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3268-3307 3.19e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 60.83  E-value: 3.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386769253  3268 GRCEPCPRGTYRLQGVQPSCAACPLGRTTPKVGASSVEEC 3307
Cdd:pfam07699    9 EPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3149-3200 6.90e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 59.67  E-value: 6.90e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386769253  3149 GTFYDSANKTCIACSRGTYQSEAGQLQCSKCPviagRPGVTAGPGARSAADC 3200
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACP----LGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1916-1966 1.15e-10

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 58.90  E-value: 1.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386769253  1916 GTYSPTGLVPCLECPRNSFTaepPTGGFKDCQACPAQSFTYQPAASNKDLC 1966
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQ---PEEGQLSCLACPLGTTTDSPGATSISDC 48
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 675-731 4.45e-10

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: 57.86  E-value: 4.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:cd00033     1 CPPPPVPENGTVTGSKGS-YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2059-2095 8.05e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.49  E-value: 8.05e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2059 DIDECASQ-PCYNGGQCKDLPQGYRCECPAGYSGINCQ 2095
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 568-733 2.72e-09

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  568 TAFGTLVSFTCPIGQEFaTGKTRlvTECLRGGNWSVSYIPK---CQEVYCGPVPQIDNGFSIGSSNVTYRG-IAMYQCYA 643
Cdd:PHA02927  102 VDFGSSITYSCNSGYQL-IGESK--SYCELGSTGSMVWNPEapiCESVKCQSPPSISNGRHNGYEDFYTDGsVVTYSCNS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  644 GFAFASGAPIekisCLPDGRWERQPHCMASQCaalPEVAHANVTLLNGGGRSYG--TIVQYECEPGYERNGHPVLTCMSN 721
Cdd:PHA02927  179 GYSLIGNSGV----LCSGGEWSDPPTCQIVKC---PHPTISNGYLSSGFKRSYSynDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|..
gi 386769253  722 GTWSGDVPRCTR 733
Cdd:PHA02927  252 NTWQPELPKCVR 263
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 172-206 3.32e-09

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: 54.52  E-value: 3.32e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 386769253  172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDELDC 206
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
PHA02639 super family cl31493
EEV host range protein; Provisional
 697-834 1.05e-08

EEV host range protein; Provisional


The actual alignment was detected with superfamily member PHA02639:

Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 59.68  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  697 GTIVQYECEPGYERNGHPVLTCM---SNGTWSGDVPRCTRKRCFEFPTIANGFVVDSTRAYLFGDEARVQC--FKG--YK 769
Cdd:PHA02639   43 GKLIEYTCNTDYALIGDRFRTCIkdkNNAIWSNKAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVCneHKGvqYS 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  770 LIGSNIMRCSEAQKFE-QPPTCEDINeCSSSQCDLTTTECQNTNGSFHCQCRTGFTATTECRPVGD 834
Cdd:PHA02639  123 LVGNEKITCIQDKSWKpDPPICKMIN-CRFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGE 187
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2292-2327 1.59e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.64  E-value: 1.59e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2292 IDDCAS-NPCQHGATCVDQLDGFSCKCRPGYVGLSCE 2327
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2253-2289 2.22e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.25  E-value: 2.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2253 NIDDCENR-PCANEGTCVDLVDGYSCNCEPGYTGKNCQ 2289
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2178-2214 3.28e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 3.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2178 NINDC-SENPCLLGANCTDLVNDFQCACPPGFTGKRCE 2214
Cdd:cd00054     1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2369-2405 4.95e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.48  E-value: 4.95e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2369 DIDDCE-AQPCLNNGICRDRVGGFECGCEPGWSGMRCE 2405
Cdd:cd00054     1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2486-2520 5.91e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.10  E-value: 5.91e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386769253 2486 DACEE-HVCQNGATCVDNGAGYSCQCPPGFTGRNCE 2520
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
HYR super family cl47740
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1463-1547 8.59e-08

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


The actual alignment was detected with superfamily member pfam02494:

Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 52.01  E-value: 8.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1463 VDNEPPIFqNCPQQpiVVRRDENG-GVLPVNFTEPTAVDNSGSIARLEIKPQnfrtPSYIFK--DTVVKYVAFDYDGNVA 1539
Cdd:pfam02494    1 VDTTPPTV-KCPNN--IVRTVELGtSTVRVFFTEPTAFDNSGQAILVSRTAQ----PGDFFPvgTTTVTYVAYDNSGNRA 73


                   ....*...
gi 386769253  1540 ICEINITV 1547
Cdd:pfam02494   74 SCTFTVTV 81
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 988-1016 4.69e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.70  E-value: 4.69e-06
                           10        20
                   ....*....|....*....|....*....
gi 386769253   988 CSKNNGGCDQKCINSPGGFACGCNTGYQL 1016
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYEL 29
HYR super family cl47740
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1548-1631 5.38e-06

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


The actual alignment was detected with superfamily member pfam02494:

Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 47.00  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1548 PDVTPPLLQCPQS--YVIELvdrqDSYTVNFNDTRKRIKTSDDTGDVRLQFSPESANIKIGnFENVTVTATDKYNNRAAC 1625
Cdd:pfam02494    1 VDTTPPTVKCPNNivRTVEL----GTSTVRVFFTEPTAFDNSGQAILVSRTAQPGDFFPVG-TTTVTYVAYDNSGNRASC 75


                   ....*.
gi 386769253  1626 HFQVSV 1631
Cdd:pfam02494   76 TFTVTV 81
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2138-2176 2.60e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 2.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 386769253 2138 IDPCtANGNPCGNGASCQALEqGRYKCECVPGWEGIHCE 2176
Cdd:cd00054     2 IDEC-ASGNPCQNGGTCVNTV-GSYRCSCPPGYTGRNCE 38
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 2590-2735 1.59e-04

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00560:

Pssm-ID: 473984 [Multi-domain]  Cd Length: 133  Bit Score: 44.33  E-value: 1.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   2590 SLTVAMWVQFAQkddrgifftlYGVQSARMTQQrrmLLQAHSSgvqvslFEDQPDAFLSFGEY----------TSVNDGQ 2659
Cdd:smart00560    2 SFTLEAWVKLES----------AGGSQPIITGA---AVAQPTI------SEKALTFFLRAKSVqgwqtartgaTADWIGV 62

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   2660 WHHVAVVWDGISGQLQLITEGLIASKMEYGAGGSLPgylwavlGLPQPYGLSNELAYSDSgFQGTITKAQVWARAL 2735
Cdd:smart00560   63 WVHLAGVYDGGAGKLSLYVNGVEVATSETQPSPSSG-------NLPQGGRILLGGAGGEN-FSGRLDEVRVYNRAL 130
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2411-2444 3.95e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.31  E-value: 3.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253 2411 CGAQAPCQNDASCIDLFQDYFCVCPSGTDGKNCE 2444
Cdd:cd00054     5 CASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2025-2055 1.42e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.52  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2025 CGEGACQHGGLCVPMGHDIQCFCPAGFSGRR 2055
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2522-2557 2.54e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2522 DIVDCKD-NSCPPGATCVDLTNGFYCQCPFNMTGDDC 2557
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 326-435 3.15e-27

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 3.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  326 CGGTLKATLQrQILTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIAD----GRDFLMIRDGESPMSRTIAKLTGK 401
Cdd:cd00041     1 CGGTLTASTS-GTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 386769253  402 TAqnNRVIISTGNALYLYFKSSLGEAGKGFSLRY 435
Cdd:cd00041    80 TL--PPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 338-435 3.15e-22

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 93.99  E-value: 3.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    338 ILTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIADGR----DFLMIRDGESPMSRTIAKLTGKTAqNNRVIISTG 413
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEA-PPPVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 386769253    414 NALYLYFKSSLGEAGKGFSLRY 435
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 220-319 3.98e-21

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 90.93  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEK----TFDTVQILVGGRTEdkSVSLATLSGKQdlTTQPFVS 295
Cdd:cd00041    12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTS--SPLLGRFCGST--LPPPIIS 87

                          90       100
                  ....*....|....*....|....
gi 386769253  296 ASNFMIVKFTTDGSVERKGFRATW 319
Cdd:cd00041    88 SGNSLTVRFRSDSSVTGRGFKATY 111
CUB pfam00431
CUB domain;
326-435 9.95e-21

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 90.05  E-value: 9.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   326 CGGTLKATLQRqiLTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIADGR----DFLMIRDGESPMSRTIAKLTGK 401
Cdd:pfam00431    1 CGGVLTDSSGS--ISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 386769253   402 taQNNRVIISTGNALYLYFKSSLGEAGKGFSLRY 435
Cdd:pfam00431   79 --GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 833-976 6.92e-19

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 85.87  E-value: 6.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  833 GDLGLgNGGIPDDSIT-TSVSEPGYSKEQLRLN-TNGWCGGSSEPgANWILIDLKAPTILRGFRTMSVQRPDGNvAFSSA 910
Cdd:cd00057     1 EPLGM-ESGLADDQITaSSSYSSGWEASRARLNsDNAWTPAVNDP-PQWLQVDLGKTRRVTGIQTQGRKGGGSS-EWVTS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  911 VRLQYTNDLTD--VFKD-------YANPDGTAVefrileptlsILN-LPLPIEARYIRFRIQDYVGAPCLRMELMG 976
Cdd:cd00057    78 YKVQYSLDGETwtTYKDkgeekvfTGNSDGSTP----------VTNdFPPPIVARYIRILPTTWNGNISLRLELYG 143
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 220-319 1.40e-18

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 83.59  E-value: 1.40e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEK----TFDTVQILVGgrTEDKSVSLATLSGKQdLTTQPFVS 295
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDG--PSASSPLLGRFCGSE-APPPVISS 78

                            90       100
                    ....*....|....*....|....
gi 386769253    296 ASNFMIVKFTTDGSVERKGFRATW 319
Cdd:smart00042   79 SSNSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 36-167 2.14e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 80.72  E-value: 2.14e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253     36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETLAIARasdpNQRASDKYWLGLASLDDLRTNTL 115
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLK----NSGSSDYYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386769253    116 ESASGAliSQYSgYWSLHQPNAESGECVaaAFAGKSQSWDLGTCESLLPFMC 167
Cdd:smart00034   77 SDGSGP--VSYS-NWAPGEPNNSSGDCV--VLSTSGGKWNDVSCTSKLPFVC 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1303-1443 4.75e-17

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 80.47  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253 1303 PLGLSSGRIPDSAINATSERPNYEAKNIRLNSATGWC-GKQEAFTYVSVDLGQIYRVKAILVKGVVTNDIVGRPTEIRFF 1381
Cdd:cd00057     2 PLGMESGLADDQITASSSYSSGWEASRARLNSDNAWTpAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTSYKVQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769253 1382 YKQaESENYVVYFPNFNLtMRDPGNYGELAMIT--LPKFVQARFVILGIVSYMDNACLKFELMG 1443
Cdd:cd00057    82 YSL-DGETWTTYKDKGEE-KVFTGNSDGSTPVTndFPPPIVARYIRILPTTWNGNISLRLELYG 143
CUB pfam00431
CUB domain;
220-318 3.96e-16

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 76.56  E-value: 3.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEKT----FDTVQILVGGrtEDKSVSLATLSGKQdlTTQPFVS 295
Cdd:pfam00431   11 SISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgYDYVEIRDGP--SASSPLLGRFCGSG--IPEDIVS 86

                           90       100
                   ....*....|....*....|...
gi 386769253   296 ASNFMIVKFTTDGSVERKGFRAT 318
Cdd:pfam00431   87 SSNQMTIKFVSDASVQKRGFKAT 109
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 439-550 1.76e-15

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 75.14  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  439 CKATITA-RNGTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKSDN-----VQVFDGSSTSGLRLHSgngF 512
Cdd:cd00041     1 CGGTLTAsTSGTISSPNYP-NNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSSPLLGR---F 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386769253  513 TGPAAPKlTLTASSGEMLIKFTSDALHNAAGWSATFSA 550
Cdd:cd00041    77 CGSTLPP-PIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 846-974 2.22e-15

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 75.18  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   846 SITTSVSEPGYSKEQLRLNTN---GWCGGSSEPGAnWILIDLKAPTILRGFRTmsVQRPDGNVAFSSAVRLQYTNDLTDv 922
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDpntAWSAWSGDDPQ-WIQVDLGKPKKITGVVT--QGRQDGSNGYVTSYKIEYSLDGEN- 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386769253   923 FKDYANPDGTAVefrILEPTLSILNLPLPIEARYIRFRIQDYVG--APCLRMEL 974
Cdd:pfam00754   77 WTTVKDEKIPGN---NDNNTPVTNTFDPPIKARYVRIVPTSWNGgnGIALRAEL 127
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1862-1909 2.43e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.38  E-value: 2.43e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1862 GTYVSEGQNSCTYCPRGYYQNRDRQGTCLRCPAGTYTKEEGTKSQADC 1909
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3315-3362 3.08e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.00  E-value: 3.08e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3315 GTYLNATQNMCIECRKGYYQSESQQTSCLQCPPNHSTKITGATSKSEC 3362
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 828-977 4.47e-14

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 71.77  E-value: 4.47e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    828 ECR-PVGDLGlgnggipDDSITTSVSEPGYskEQLRLN---TNGWCGGSSEPGaNWILIDLKAPTILRGFRTmsvQRPDG 903
Cdd:smart00231    1 PCNePLGLES-------DSQITASSSYWAA--KIARLNggsDGGWCPAKNDLP-PWIQVDLGRLRTVTGVIT---GRRHG 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    904 NVAFSSAvRLQYTNDLTD--VFKD------YANPDGTAVefrileptlSILNLPLPIEARYIRFRIQDYVGAPCLRMELM 975
Cdd:smart00231   68 NGDWVTY-KLEYSDDGVNwtTYKDgnskvfPGNSDAGTV---------VLNDFPPPIVARYVRILPTGWNGNIILRVELL 137


                    ..
gi 386769253    976 GC 977
Cdd:smart00231  138 GC 139
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1973-2020 6.21e-14

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 68.53  E-value: 6.21e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1973 GTYSATGLAPCSPCPLHHYQGAAGAQSCNECPSNMRTDSPASKGREQC 2020
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 448-548 7.99e-14

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 69.73  E-value: 7.99e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    448 GTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKSDN-----VQVFDGSSTSGLRLHSgngFTGPAAPKLTL 522
Cdd:smart00042    1 GTITSPNYP-QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNceydyVEIYDGPSASSPLLGR---FCGSEAPPPVI 76

                            90       100
                    ....*....|....*....|....*.
gi 386769253    523 TASSGEMLIKFTSDALHNAAGWSATF 548
Cdd:smart00042   77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
439-548 1.36e-13

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 69.63  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   439 CKATITARNGTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKS-----DNVQVFDGSSTSGLRLHSgngFT 513
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYP-NPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGR---FC 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 386769253   514 GPAAPkLTLTASSGEMLIKFTSDALHNAAGWSATF 548
Cdd:pfam00431   77 GSGIP-EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 46-167 1.56e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 69.57  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   46 NCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETLAIARASDpnqraSDKYWLGLasLDDLRTNTLESASGALISQ 125
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSS-----SSDVWIGL--NDLSSEGTWKWSDGSPLVD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 386769253  126 YSgYWSLHQPNAESGECVAAAFAGKSQSWDLGTCESLLPFMC 167
Cdd:cd00037    74 YT-NWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFIC 114
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 2799-2877 4.02e-13

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 67.03  E-value: 4.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2799 VDKEPPVVEhCPGDLWVIAK--NGSAVVSWDEPHFSDNIGVTKIYERNGHrSGTTLLWGTYDITYIASDAAGNTASCSFK 2876
Cdd:pfam02494    1 VDTTPPTVK-CPNNIVRTVElgTSTVRVFFTEPTAFDNSGQAILVSRTAQ-PGDFFPVGTTTVTYVAYDNSGNRASCTFT 78


                   .
gi 386769253  2877 V 2877
Cdd:pfam02494   79 V 79
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1051-1106 4.49e-13

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: 66.33  E-value: 4.49e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253 1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1051-1106 1.96e-12

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: 64.47  E-value: 1.96e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 54-167 2.85e-12

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.58  E-value: 2.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    54 KHSWDKSAELCRRYGAELVAIDSYAENNETLAIArasdpnQRASDKYWLGLASLDDLRTNTLESASGALISQysgyWSLH 133
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL------KKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN----WAPE 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 386769253   134 Q-PNAESGECVAAAFagKSQSWDLGTCESLLPFMC 167
Cdd:pfam00059   71 PnNNGENEDCVELSS--SSGKWNDENCNSKNPFVC 103
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3207-3254 2.94e-12

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 63.52  E-value: 2.94e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3207 GKYFDAETGLCRSCGHGFYQPNEGSFSCELCGLGQTTRSTEATSRKEC 3254
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3268-3307 3.19e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 60.83  E-value: 3.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386769253  3268 GRCEPCPRGTYRLQGVQPSCAACPLGRTTPKVGASSVEEC 3307
Cdd:pfam07699    9 EPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3149-3200 6.90e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 59.67  E-value: 6.90e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386769253  3149 GTFYDSANKTCIACSRGTYQSEAGQLQCSKCPviagRPGVTAGPGARSAADC 3200
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACP----LGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1916-1966 1.15e-10

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 58.90  E-value: 1.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386769253  1916 GTYSPTGLVPCLECPRNSFTaepPTGGFKDCQACPAQSFTYQPAASNKDLC 1966
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQ---PEEGQLSCLACPLGTTTDSPGATSISDC 48
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1297-1444 3.16e-10

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 60.99  E-value: 3.16e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   1297 ECKVikPLGLSSgripDSAINATSerPNYEAKNIRLN--SATGWCGKQEAFT-YVSVDLGQIYRVKAIlvkgvvtndIVG 1373
Cdd:smart00231    1 PCNE--PLGLES----DSQITASS--SYWAAKIARLNggSDGGWCPAKNDLPpWIQVDLGRLRTVTGV---------ITG 63

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   1374 RPTEIR-----FFYKQAESENYVVYFPNFNLTMRDPGNYGELAMITLPKFVQARFVILGIVSYMDNACLKFELMGC 1444
Cdd:smart00231   64 RRHGNGdwvtyKLEYSDDGVNWTTYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 675-731 4.45e-10

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: 57.86  E-value: 4.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:cd00033     1 CPPPPVPENGTVTGSKGS-YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 675-731 4.57e-10

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: 57.54  E-value: 4.57e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253    675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:smart00032    1 CPPPPDIENGTVTSSSGT-YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
1051-1106 7.31e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.12  E-value: 7.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2059-2095 8.05e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.49  E-value: 8.05e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2059 DIDECASQ-PCYNGGQCKDLPQGYRCECPAGYSGINCQ 2095
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 568-733 2.72e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  568 TAFGTLVSFTCPIGQEFaTGKTRlvTECLRGGNWSVSYIPK---CQEVYCGPVPQIDNGFSIGSSNVTYRG-IAMYQCYA 643
Cdd:PHA02927  102 VDFGSSITYSCNSGYQL-IGESK--SYCELGSTGSMVWNPEapiCESVKCQSPPSISNGRHNGYEDFYTDGsVVTYSCNS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  644 GFAFASGAPIekisCLPDGRWERQPHCMASQCaalPEVAHANVTLLNGGGRSYG--TIVQYECEPGYERNGHPVLTCMSN 721
Cdd:PHA02927  179 GYSLIGNSGV----LCSGGEWSDPPTCQIVKC---PHPTISNGYLSSGFKRSYSynDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|..
gi 386769253  722 GTWSGDVPRCTR 733
Cdd:PHA02927  252 NTWQPELPKCVR 263
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 172-206 3.32e-09

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: 54.52  E-value: 3.32e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 386769253  172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDELDC 206
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Sushi pfam00084
Sushi repeat (SCR repeat);
675-731 6.87e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.43  E-value: 6.87e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253   675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNE-YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 697-834 1.05e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 59.68  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  697 GTIVQYECEPGYERNGHPVLTCM---SNGTWSGDVPRCTRKRCFEFPTIANGFVVDSTRAYLFGDEARVQC--FKG--YK 769
Cdd:PHA02639   43 GKLIEYTCNTDYALIGDRFRTCIkdkNNAIWSNKAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVCneHKGvqYS 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  770 LIGSNIMRCSEAQKFE-QPPTCEDINeCSSSQCDLTTTECQNTNGSFHCQCRTGFTATTECRPVGD 834
Cdd:PHA02639  123 LVGNEKITCIQDKSWKpDPPICKMIN-CRFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGE 187
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1315-1441 1.22e-08

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 55.92  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1315 AINATSERPNYEAKNIRL--NSATGWCGKQEAFT-YVSVDLGQIYRVKAILVKGvVTNDIVGRPTEIRFFYKQaESENYV 1391
Cdd:pfam00754    1 QITASSSYSGEGPAAAALdgDPNTAWSAWSGDDPqWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSL-DGENWT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386769253  1392 VYFpnfnlTMRDPGNYGE--LAMITLPKFVQARFVILGIVSYMDNA--CLKFEL 1441
Cdd:pfam00754   79 TVK-----DEKIPGNNDNntPVTNTFDPPIKARYVRIVPTSWNGGNgiALRAEL 127
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2292-2327 1.59e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.64  E-value: 1.59e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2292 IDDCAS-NPCQHGATCVDQLDGFSCKCRPGYVGLSCE 2327
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2253-2289 2.22e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.25  E-value: 2.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2253 NIDDCENR-PCANEGTCVDLVDGYSCNCEPGYTGKNCQ 2289
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2178-2214 3.28e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 3.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2178 NINDC-SENPCLLGANCTDLVNDFQCACPPGFTGKRCE 2214
Cdd:cd00054     1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2369-2405 4.95e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.48  E-value: 4.95e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2369 DIDDCE-AQPCLNNGICRDRVGGFECGCEPGWSGMRCE 2405
Cdd:cd00054     1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
2059-2095 5.28e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 5.28e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2059 DIDECAS-QPCYNGGQCKDLPQGYRCECPAGYS-GINCQ 2095
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2486-2520 5.91e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.10  E-value: 5.91e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386769253 2486 DACEE-HVCQNGATCVDNGAGYSCQCPPGFTGRNCE 2520
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1463-1547 8.59e-08

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 52.01  E-value: 8.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1463 VDNEPPIFqNCPQQpiVVRRDENG-GVLPVNFTEPTAVDNSGSIARLEIKPQnfrtPSYIFK--DTVVKYVAFDYDGNVA 1539
Cdd:pfam02494    1 VDTTPPTV-KCPNN--IVRTVELGtSTVRVFFTEPTAFDNSGQAILVSRTAQ----PGDFFPvgTTTVTYVAYDNSGNRA 73


                   ....*...
gi 386769253  1540 ICEINITV 1547
Cdd:pfam02494   74 SCTFTVTV 81
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 172-203 1.54e-07

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: 49.94  E-value: 1.54e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 386769253    172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDE 203
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
2292-2327 4.51e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.78  E-value: 4.51e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 386769253   2292 IDDCAS-NPCQHGATCVDQLDGFSCKCRPGYV-GLSCE 2327
Cdd:smart00179    2 IDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
172-206 5.62e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 5.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 386769253   172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDELDC 206
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
2253-2289 7.22e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.01  E-value: 7.22e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2253 NIDDCENR-PCANEGTCVDLVDGYSCNCEPGYT-GKNCQ 2289
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
2369-2405 9.60e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 9.60e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2369 DIDDCE-AQPCLNNGICRDRVGGFECGCEPGWS-GMRCE 2405
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
2178-2214 2.19e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.86  E-value: 2.19e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2178 NINDC-SENPCLLGANCTDLVNDFQCACPPGFT-GKRCE 2214
Cdd:smart00179    1 DIDECaSGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
2486-2520 2.93e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.47  E-value: 2.93e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 386769253   2486 DACEE-HVCQNGATCVDNGAGYSCQCPPGFT-GRNCE 2520
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 736-791 4.31e-06

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: 46.30  E-value: 4.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  736 CFEFPTIANGFVVDSTRAYLFGDEARVQCFKGYKLIGSNIMRCSEAQKFEQ-PPTCE 791
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPpPPTCE 57
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 988-1016 4.69e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.70  E-value: 4.69e-06
                           10        20
                   ....*....|....*....|....*....
gi 386769253   988 CSKNNGGCDQKCINSPGGFACGCNTGYQL 1016
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYEL 29
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1548-1631 5.38e-06

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 47.00  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1548 PDVTPPLLQCPQS--YVIELvdrqDSYTVNFNDTRKRIKTSDDTGDVRLQFSPESANIKIGnFENVTVTATDKYNNRAAC 1625
Cdd:pfam02494    1 VDTTPPTVKCPNNivRTVEL----GTSTVRVFFTEPTAFDNSGQAILVSRTAQPGDFFPVG-TTTVTYVAYDNSGNRASC 75


                   ....*.
gi 386769253  1626 HFQVSV 1631
Cdd:pfam02494   76 TFTVTV 81
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 995-1106 9.29e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 50.42  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  995 CDQKCINSPGGFACGCNTGYQLYTSNGT-------AGYHIERSESGERDGDTYQRNKTCVPLMCPElEAPENGQLLSD-K 1066
Cdd:PHA02927  143 CESVKCQSPPSISNGRHNGYEDFYTDGSvvtyscnSGYSLIGNSGVLCSGGEWSDPPTCQIVKCPH-PTISNGYLSSGfK 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386769253 1067 NDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:PHA02927  222 RSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2488-2518 9.61e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 9.61e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2488 CEEHVCQNGATCVDNGAGYSCQCPPGFTGRN 2518
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2063-2093 1.91e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.91  E-value: 1.91e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2063 CASQPCYNGGQCKDLPQGYRCECPAGYSGIN 2093
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2138-2176 2.60e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 2.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 386769253 2138 IDPCtANGNPCGNGASCQALEqGRYKCECVPGWEGIHCE 2176
Cdd:cd00054     2 IDEC-ASGNPCQNGGTCVNTV-GSYRCSCPPGYTGRNCE 38
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 736-790 3.66e-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: 43.67  E-value: 3.66e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253    736 CFEFPTIANGFVVDSTRAYLFGDEARVQCFKGYKLIGSNIMRCSEAQKF-EQPPTC 790
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWsPPPPTC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 1036-1106 5.47e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 48.06  E-value: 5.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769253 1036 DGDTYQRNKTCVPLMCpELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:PHA02831  126 NKQWVPKYPVCKLIRC-KYPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKC 195
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2295-2323 7.92e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.98  E-value: 7.92e-05
                           10        20
                   ....*....|....*....|....*....
gi 386769253  2295 CASNPCQHGATCVDQLDGFSCKCRPGYVG 2323
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2257-2287 8.00e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.98  E-value: 8.00e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2257 CENRPCANEGTCVDLVDGYSCNCEPGYTGKN 2287
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
LamGL smart00560
LamG-like jellyroll fold domain;
2590-2735 1.59e-04

LamG-like jellyroll fold domain;


Pssm-ID: 214722 [Multi-domain]  Cd Length: 133  Bit Score: 44.33  E-value: 1.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   2590 SLTVAMWVQFAQkddrgifftlYGVQSARMTQQrrmLLQAHSSgvqvslFEDQPDAFLSFGEY----------TSVNDGQ 2659
Cdd:smart00560    2 SFTLEAWVKLES----------AGGSQPIITGA---AVAQPTI------SEKALTFFLRAKSVqgwqtartgaTADWIGV 62

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   2660 WHHVAVVWDGISGQLQLITEGLIASKMEYGAGGSLPgylwavlGLPQPYGLSNELAYSDSgFQGTITKAQVWARAL 2735
Cdd:smart00560   63 WVHLAGVYDGGAGKLSLYVNGVEVATSETQPSPSSG-------NLPQGGRILLGGAGGEN-FSGRLDEVRVYNRAL 130
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2182-2212 2.24e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.83  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2182 CSENPCLLGANCTDLVNDFQCACPPGFTGKR 2212
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2411-2444 3.95e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.31  E-value: 3.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253 2411 CGAQAPCQNDASCIDLFQDYFCVCPSGTDGKNCE 2444
Cdd:cd00054     5 CASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 2581-2742 4.78e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 43.14  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2581 VPFPTGEANSLTVAMWVQFAQKDDRG-IFFTL--YGVQSARMTQQRRMLLQAHSSGVQVSLFEDQpdaflsfgeyTSVND 2657
Cdd:pfam13385    9 LPDALLPTSDFTVSAWVKPDSLPGWArAIISSsgGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSG----------ASVPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2658 GQWHHVAVVWDG------ISGQLQLITEGliaskmeygaGGSLPGYLWAVLGLPQPYGlsnelaySDSGFQGTITKAQVW 2731
Cdd:pfam13385   79 GQWTHVAVTYDGgtlrlyVNGVLVGSSTL----------TGGPPPGTGGPLYIGRSPG-------GDDYFNGLIDEVRIY 141

                          170
                   ....*....|.
gi 386769253  2732 ARALDiTSEIQ 2742
Cdd:pfam13385  142 DRALS-AAEIA 151
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2025-2055 1.42e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.52  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2025 CGEGACQHGGLCVPMGHDIQCFCPAGFSGRR 2055
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
2138-2176 1.77e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 1.77e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 386769253   2138 IDPCtANGNPCGNGASCQALEqGRYKCECVPGWE-GIHCE 2176
Cdd:smart00179    2 IDEC-ASGNPCQNGGTCVNTV-GSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2373-2401 1.85e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.13  E-value: 1.85e-03
                           10        20
                   ....*....|....*....|....*....
gi 386769253  2373 CEAQPCLNNGICRDRVGGFECGCEPGWSG 2401
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2522-2557 2.54e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2522 DIVDCKD-NSCPPGATCVDLTNGFYCQCPFNMTGDDC 2557
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
2411-2444 2.79e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.00  E-value: 2.79e-03
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 386769253   2411 CGAQAPCQNDASCIDLFQDYFCVCPSG-TDGKNCE 2444
Cdd:smart00179    5 CASGNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 984-1016 8.03e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.46  E-value: 8.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253  984 DINECSKNNG-GCDQKCINSPGGFACGCNTGYQL 1016
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
984-1015 8.66e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 8.66e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 386769253    984 DINECSKNNG-GCDQKCINSPGGFACGCNTGYQ 1015
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGYT 33
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 326-435 3.15e-27

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 3.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  326 CGGTLKATLQrQILTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIAD----GRDFLMIRDGESPMSRTIAKLTGK 401
Cdd:cd00041     1 CGGTLTASTS-GTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 386769253  402 TAqnNRVIISTGNALYLYFKSSLGEAGKGFSLRY 435
Cdd:cd00041    80 TL--PPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 338-435 3.15e-22

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 93.99  E-value: 3.15e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    338 ILTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIADGR----DFLMIRDGESPMSRTIAKLTGKTAqNNRVIISTG 413
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEA-PPPVISSSS 80

                            90       100
                    ....*....|....*....|..
gi 386769253    414 NALYLYFKSSLGEAGKGFSLRY 435
Cdd:smart00042   81 NSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 220-319 3.98e-21

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 90.93  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEK----TFDTVQILVGGRTEdkSVSLATLSGKQdlTTQPFVS 295
Cdd:cd00041    12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTS--SPLLGRFCGST--LPPPIIS 87

                          90       100
                  ....*....|....*....|....
gi 386769253  296 ASNFMIVKFTTDGSVERKGFRATW 319
Cdd:cd00041    88 SGNSLTVRFRSDSSVTGRGFKATY 111
CUB pfam00431
CUB domain;
326-435 9.95e-21

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 90.05  E-value: 9.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   326 CGGTLKATLQRqiLTSPNYPKQYPGGLECLYVIKAQPGRIISIEVDDLDIADGR----DFLMIRDGESPMSRTIAKLTGK 401
Cdd:pfam00431    1 CGGVLTDSSGS--ISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 386769253   402 taQNNRVIISTGNALYLYFKSSLGEAGKGFSLRY 435
Cdd:pfam00431   79 --GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 833-976 6.92e-19

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 85.87  E-value: 6.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  833 GDLGLgNGGIPDDSIT-TSVSEPGYSKEQLRLN-TNGWCGGSSEPgANWILIDLKAPTILRGFRTMSVQRPDGNvAFSSA 910
Cdd:cd00057     1 EPLGM-ESGLADDQITaSSSYSSGWEASRARLNsDNAWTPAVNDP-PQWLQVDLGKTRRVTGIQTQGRKGGGSS-EWVTS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  911 VRLQYTNDLTD--VFKD-------YANPDGTAVefrileptlsILN-LPLPIEARYIRFRIQDYVGAPCLRMELMG 976
Cdd:cd00057    78 YKVQYSLDGETwtTYKDkgeekvfTGNSDGSTP----------VTNdFPPPIVARYIRILPTTWNGNISLRLELYG 143
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 220-319 1.40e-18

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 83.59  E-value: 1.40e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEK----TFDTVQILVGgrTEDKSVSLATLSGKQdLTTQPFVS 295
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDG--PSASSPLLGRFCGSE-APPPVISS 78

                            90       100
                    ....*....|....*....|....
gi 386769253    296 ASNFMIVKFTTDGSVERKGFRATW 319
Cdd:smart00042   79 SSNSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 36-167 2.14e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 80.72  E-value: 2.14e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253     36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETLAIARasdpNQRASDKYWLGLASLDDLRTNTL 115
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLK----NSGSSDYYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 386769253    116 ESASGAliSQYSgYWSLHQPNAESGECVaaAFAGKSQSWDLGTCESLLPFMC 167
Cdd:smart00034   77 SDGSGP--VSYS-NWAPGEPNNSSGDCV--VLSTSGGKWNDVSCTSKLPFVC 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1303-1443 4.75e-17

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 80.47  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253 1303 PLGLSSGRIPDSAINATSERPNYEAKNIRLNSATGWC-GKQEAFTYVSVDLGQIYRVKAILVKGVVTNDIVGRPTEIRFF 1381
Cdd:cd00057     2 PLGMESGLADDQITASSSYSSGWEASRARLNSDNAWTpAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTSYKVQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769253 1382 YKQaESENYVVYFPNFNLtMRDPGNYGELAMIT--LPKFVQARFVILGIVSYMDNACLKFELMG 1443
Cdd:cd00057    82 YSL-DGETWTTYKDKGEE-KVFTGNSDGSTPVTndFPPPIVARYIRILPTTWNGNISLRLELYG 143
CUB pfam00431
CUB domain;
220-318 3.96e-16

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 76.56  E-value: 3.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   220 VIETPNYPHKYGALSKCKWTLEGPLGSNIILQFQDFETEKT----FDTVQILVGGrtEDKSVSLATLSGKQdlTTQPFVS 295
Cdd:pfam00431   11 SISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgYDYVEIRDGP--SASSPLLGRFCGSG--IPEDIVS 86

                           90       100
                   ....*....|....*....|...
gi 386769253   296 ASNFMIVKFTTDGSVERKGFRAT 318
Cdd:pfam00431   87 SSNQMTIKFVSDASVQKRGFKAT 109
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 439-550 1.76e-15

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 75.14  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  439 CKATITA-RNGTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKSDN-----VQVFDGSSTSGLRLHSgngF 512
Cdd:cd00041     1 CGGTLTAsTSGTISSPNYP-NNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSSPLLGR---F 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386769253  513 TGPAAPKlTLTASSGEMLIKFTSDALHNAAGWSATFSA 550
Cdd:cd00041    77 CGSTLPP-PIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 846-974 2.22e-15

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 75.18  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   846 SITTSVSEPGYSKEQLRLNTN---GWCGGSSEPGAnWILIDLKAPTILRGFRTmsVQRPDGNVAFSSAVRLQYTNDLTDv 922
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDpntAWSAWSGDDPQ-WIQVDLGKPKKITGVVT--QGRQDGSNGYVTSYKIEYSLDGEN- 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386769253   923 FKDYANPDGTAVefrILEPTLSILNLPLPIEARYIRFRIQDYVG--APCLRMEL 974
Cdd:pfam00754   77 WTTVKDEKIPGN---NDNNTPVTNTFDPPIKARYVRIVPTSWNGgnGIALRAEL 127
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1862-1909 2.43e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.38  E-value: 2.43e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1862 GTYVSEGQNSCTYCPRGYYQNRDRQGTCLRCPAGTYTKEEGTKSQADC 1909
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3315-3362 3.08e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 72.00  E-value: 3.08e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3315 GTYLNATQNMCIECRKGYYQSESQQTSCLQCPPNHSTKITGATSKSEC 3362
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 828-977 4.47e-14

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 71.77  E-value: 4.47e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    828 ECR-PVGDLGlgnggipDDSITTSVSEPGYskEQLRLN---TNGWCGGSSEPGaNWILIDLKAPTILRGFRTmsvQRPDG 903
Cdd:smart00231    1 PCNePLGLES-------DSQITASSSYWAA--KIARLNggsDGGWCPAKNDLP-PWIQVDLGRLRTVTGVIT---GRRHG 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    904 NVAFSSAvRLQYTNDLTD--VFKD------YANPDGTAVefrileptlSILNLPLPIEARYIRFRIQDYVGAPCLRMELM 975
Cdd:smart00231   68 NGDWVTY-KLEYSDDGVNwtTYKDgnskvfPGNSDAGTV---------VLNDFPPPIVARYVRILPTGWNGNIILRVELL 137


                    ..
gi 386769253    976 GC 977
Cdd:smart00231  138 GC 139
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1973-2020 6.21e-14

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 68.53  E-value: 6.21e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  1973 GTYSATGLAPCSPCPLHHYQGAAGAQSCNECPSNMRTDSPASKGREQC 2020
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 448-548 7.99e-14

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 69.73  E-value: 7.99e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    448 GTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKSDN-----VQVFDGSSTSGLRLHSgngFTGPAAPKLTL 522
Cdd:smart00042    1 GTITSPNYP-QSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNceydyVEIYDGPSASSPLLGR---FCGSEAPPPVI 76

                            90       100
                    ....*....|....*....|....*.
gi 386769253    523 TASSGEMLIKFTSDALHNAAGWSATF 548
Cdd:smart00042   77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
439-548 1.36e-13

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 69.63  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   439 CKATITARNGTVTSPAFGlADYPKNQECYFTIRNNARAPLSLKFDKFTVHKS-----DNVQVFDGSSTSGLRLHSgngFT 513
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYP-NPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGR---FC 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 386769253   514 GPAAPkLTLTASSGEMLIKFTSDALHNAAGWSATF 548
Cdd:pfam00431   77 GSGIP-EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 46-167 1.56e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 69.57  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   46 NCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETLAIARASDpnqraSDKYWLGLasLDDLRTNTLESASGALISQ 125
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSS-----SSDVWIGL--NDLSSEGTWKWSDGSPLVD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 386769253  126 YSgYWSLHQPNAESGECVAAAFAGKSQSWDLGTCESLLPFMC 167
Cdd:cd00037    74 YT-NWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFIC 114
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 2799-2877 4.02e-13

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 67.03  E-value: 4.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2799 VDKEPPVVEhCPGDLWVIAK--NGSAVVSWDEPHFSDNIGVTKIYERNGHrSGTTLLWGTYDITYIASDAAGNTASCSFK 2876
Cdd:pfam02494    1 VDTTPPTVK-CPNNIVRTVElgTSTVRVFFTEPTAFDNSGQAILVSRTAQ-PGDFFPVGTTTVTYVAYDNSGNRASCTFT 78


                   .
gi 386769253  2877 V 2877
Cdd:pfam02494   79 V 79
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1051-1106 4.49e-13

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: 66.33  E-value: 4.49e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253 1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1051-1106 1.96e-12

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: 64.47  E-value: 1.96e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 54-167 2.85e-12

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.58  E-value: 2.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253    54 KHSWDKSAELCRRYGAELVAIDSYAENNETLAIArasdpnQRASDKYWLGLASLDDLRTNTLESASGALISQysgyWSLH 133
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL------KKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN----WAPE 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 386769253   134 Q-PNAESGECVAAAFagKSQSWDLGTCESLLPFMC 167
Cdd:pfam00059   71 PnNNGENEDCVELSS--SSGKWNDENCNSKNPFVC 103
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3207-3254 2.94e-12

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 63.52  E-value: 2.94e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 386769253  3207 GKYFDAETGLCRSCGHGFYQPNEGSFSCELCGLGQTTRSTEATSRKEC 3254
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 36-169 1.41e-11

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 64.32  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   36 CPNGWELRGLNCYKYFNIKHSWDKsAEL-CRRY--GAELVAIDSYAennETLAIARASDPNQRASDKYWLGLAslDDLRT 112
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSD-AELfCQKYgpGAHLASIHSPA---EAAAIASLISSYQKAYQPVWIGLH--DPQQS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  113 NTLESASGALISQYSgyWSLHQPNAESGECVAAAFAGKSQSWDLGTCESLLPFMCRA 169
Cdd:cd03594    75 RGWEWSDGSKLDYRS--WDRNPPYARGGYCAELSRSTGFLKWNDANCEERNPFICKY 129
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3268-3307 3.19e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 60.83  E-value: 3.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386769253  3268 GRCEPCPRGTYRLQGVQPSCAACPLGRTTPKVGASSVEEC 3307
Cdd:pfam07699    9 EPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 3149-3200 6.90e-11

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 59.67  E-value: 6.90e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386769253  3149 GTFYDSANKTCIACSRGTYQSEAGQLQCSKCPviagRPGVTAGPGARSAADC 3200
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACP----LGTTTDSPGATSISDC 48
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1916-1966 1.15e-10

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 58.90  E-value: 1.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386769253  1916 GTYSPTGLVPCLECPRNSFTaepPTGGFKDCQACPAQSFTYQPAASNKDLC 1966
Cdd:pfam07699    1 GTYSNTGLEPCIPCPRGTYQ---PEEGQLSCLACPLGTTTDSPGATSISDC 48
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1297-1444 3.16e-10

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 60.99  E-value: 3.16e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   1297 ECKVikPLGLSSgripDSAINATSerPNYEAKNIRLN--SATGWCGKQEAFT-YVSVDLGQIYRVKAIlvkgvvtndIVG 1373
Cdd:smart00231    1 PCNE--PLGLES----DSQITASS--SYWAAKIARLNggSDGGWCPAKNDLPpWIQVDLGRLRTVTGV---------ITG 63

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   1374 RPTEIR-----FFYKQAESENYVVYFPNFNLTMRDPGNYGELAMITLPKFVQARFVILGIVSYMDNACLKFELMGC 1444
Cdd:smart00231   64 RRHGNGdwvtyKLEYSDDGVNWTTYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 675-731 4.45e-10

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: 57.86  E-value: 4.45e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:cd00033     1 CPPPPVPENGTVTGSKGS-YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 675-731 4.57e-10

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: 57.54  E-value: 4.57e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253    675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:smart00032    1 CPPPPDIENGTVTSSSGT-YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
1051-1106 7.31e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.12  E-value: 7.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  1051 CPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2059-2095 8.05e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.49  E-value: 8.05e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2059 DIDECASQ-PCYNGGQCKDLPQGYRCECPAGYSGINCQ 2095
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 36-168 1.61e-09

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 58.91  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYG-----AELVAIDSYAENNETLAIARASDPNQRASDkYWLGLAslDDL 110
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYG-LWIGLH--DRT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769253  111 RTNTLESASGAlISQYSgYWSLHQP-NAESGE-CVAAAFAGKS-QSWDLGTCESLLPFMCR 168
Cdd:cd03589    78 SEGPFEWTDGS-PVDFT-KWAGGQPdNYGGNEdCVQMWRRGDAgQSWNDMPCDAVFPYICK 136
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 568-733 2.72e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 60.82  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  568 TAFGTLVSFTCPIGQEFaTGKTRlvTECLRGGNWSVSYIPK---CQEVYCGPVPQIDNGFSIGSSNVTYRG-IAMYQCYA 643
Cdd:PHA02927  102 VDFGSSITYSCNSGYQL-IGESK--SYCELGSTGSMVWNPEapiCESVKCQSPPSISNGRHNGYEDFYTDGsVVTYSCNS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  644 GFAFASGAPIekisCLPDGRWERQPHCMASQCaalPEVAHANVTLLNGGGRSYG--TIVQYECEPGYERNGHPVLTCMSN 721
Cdd:PHA02927  179 GYSLIGNSGV----LCSGGEWSDPPTCQIVKC---PHPTISNGYLSSGFKRSYSynDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|..
gi 386769253  722 GTWSGDVPRCTR 733
Cdd:PHA02927  252 NTWQPELPKCVR 263
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 172-206 3.32e-09

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: 54.52  E-value: 3.32e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 386769253  172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDELDC 206
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Sushi pfam00084
Sushi repeat (SCR repeat);
675-731 6.87e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.43  E-value: 6.87e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253   675 CAALPEVAHANVTLLNGGgRSYGTIVQYECEPGYERNGHPVLTCMSNGTWSGDVPRC 731
Cdd:pfam00084    1 CPPPPDIPNGKVSATKNE-YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 598-790 9.75e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 59.28  E-value: 9.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  598 GGNWSVsyIPKCQEVYCGPVPQIDNGfSIGSSNVTYRGIAMYQCYAGFAF-ASGAPIEKISCLPDGRWE-RQPHCMASQC 675
Cdd:PHA02927   72 GTGWTL--FNQCIKRRCPSPRDIDNG-QLDIGGVDFGSSITYSCNSGYQLiGESKSYCELGSTGSMVWNpEAPICESVKC 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  676 AALPEVAHANvtlLNGGGRSY--GTIVQYECEPGYERNGHPVLTCmSNGTWSgDVPRCTRKRCfEFPTIANGFVVDS-TR 752
Cdd:PHA02927  149 QSPPSISNGR---HNGYEDFYtdGSVVTYSCNSGYSLIGNSGVLC-SGGEWS-DPPTCQIVKC-PHPTISNGYLSSGfKR 222

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 386769253  753 AYLFGDEARVQCFKGYKLIGSNIMRCSEAQKFE-QPPTC 790
Cdd:PHA02927  223 SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQpELPKC 261
PHA02639 PHA02639
EEV host range protein; Provisional
 697-834 1.05e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 59.68  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  697 GTIVQYECEPGYERNGHPVLTCM---SNGTWSGDVPRCTRKRCFEFPTIANGFVVDSTRAYLFGDEARVQC--FKG--YK 769
Cdd:PHA02639   43 GKLIEYTCNTDYALIGDRFRTCIkdkNNAIWSNKAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVCneHKGvqYS 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  770 LIGSNIMRCSEAQKFE-QPPTCEDINeCSSSQCDLTTTECQNTNGSFHCQCRTGFTATTECRPVGD 834
Cdd:PHA02639  123 LVGNEKITCIQDKSWKpDPPICKMIN-CRFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGE 187
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1315-1441 1.22e-08

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 55.92  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1315 AINATSERPNYEAKNIRL--NSATGWCGKQEAFT-YVSVDLGQIYRVKAILVKGvVTNDIVGRPTEIRFFYKQaESENYV 1391
Cdd:pfam00754    1 QITASSSYSGEGPAAAALdgDPNTAWSAWSGDDPqWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSL-DGENWT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386769253  1392 VYFpnfnlTMRDPGNYGE--LAMITLPKFVQARFVILGIVSYMDNA--CLKFEL 1441
Cdd:pfam00754   79 TVK-----DEKIPGNNDNntPVTNTFDPPIKARYVRIVPTSWNGGNgiALRAEL 127
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2292-2327 1.59e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.64  E-value: 1.59e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2292 IDDCAS-NPCQHGATCVDQLDGFSCKCRPGYVGLSCE 2327
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2253-2289 2.22e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 52.25  E-value: 2.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2253 NIDDCENR-PCANEGTCVDLVDGYSCNCEPGYTGKNCQ 2289
Cdd:cd00054     1 DIDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2178-2214 3.28e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 3.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2178 NINDC-SENPCLLGANCTDLVNDFQCACPPGFTGKRCE 2214
Cdd:cd00054     1 DIDECaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2369-2405 4.95e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.48  E-value: 4.95e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386769253 2369 DIDDCE-AQPCLNNGICRDRVGGFECGCEPGWSGMRCE 2405
Cdd:cd00054     1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
2059-2095 5.28e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 5.28e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2059 DIDECAS-QPCYNGGQCKDLPQGYRCECPAGYS-GINCQ 2095
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 36-167 5.57e-08

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 53.85  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   36 CPNGWELRGLNCYkYF-NIKHSWDKSAELCRRYGAELVAIDSYAENNetlaiarASDPNQRASDKYWLGLAslDDLRTNT 114
Cdd:cd03590     1 CPTNWKSFQSSCY-FFsTEKKSWEESRQFCEDMGAHLVIINSQEEQE-------FISKILSGNRSYWIGLS--DEETEGE 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  115 LESASGALISQYSGYWSLHQPN--AESGE-CvaAAFAGKSQSWDLGTCESLLPFMC 167
Cdd:cd03590    71 WKWVDGTPLNSSKTFWHPGEPNnwGGGGEdC--AELVYDSGGWNDVPCNLEYRWIC 124
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2486-2520 5.91e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.10  E-value: 5.91e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386769253 2486 DACEE-HVCQNGATCVDNGAGYSCQCPPGFTGRNCE 2520
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1463-1547 8.59e-08

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 52.01  E-value: 8.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1463 VDNEPPIFqNCPQQpiVVRRDENG-GVLPVNFTEPTAVDNSGSIARLEIKPQnfrtPSYIFK--DTVVKYVAFDYDGNVA 1539
Cdd:pfam02494    1 VDTTPPTV-KCPNN--IVRTVELGtSTVRVFFTEPTAFDNSGQAILVSRTAQ----PGDFFPvgTTTVTYVAYDNSGNRA 73


                   ....*...
gi 386769253  1540 ICEINITV 1547
Cdd:pfam02494   74 SCTFTVTV 81
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 172-203 1.54e-07

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: 49.94  E-value: 1.54e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 386769253    172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDE 203
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
2292-2327 4.51e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.78  E-value: 4.51e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 386769253   2292 IDDCAS-NPCQHGATCVDQLDGFSCKCRPGYV-GLSCE 2327
Cdd:smart00179    2 IDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
172-206 5.62e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 5.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 386769253   172 CPQGSLHCANGKCINQAFKCDGSDDCGDGTDELDC 206
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
2253-2289 7.22e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.01  E-value: 7.22e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2253 NIDDCENR-PCANEGTCVDLVDGYSCNCEPGYT-GKNCQ 2289
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
2369-2405 9.60e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 9.60e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2369 DIDDCE-AQPCLNNGICRDRVGGFECGCEPGWS-GMRCE 2405
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
PHA02831 PHA02831
EEV host range protein; Provisional
 661-778 1.18e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 53.07  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  661 DGRWERQPHCMASQCAALPevahanVTLLNGGGR------SYGTIVQYECEPG----YERNGHPVLTCMsNGTWSGDVPR 730
Cdd:PHA02831   63 NGSWSTKNMCIGKRNCKDP------VTILNGYIKnkkdqySFGDSVTYACKVNklekYSIVGNETVKCI-NKQWVPKYPV 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386769253  731 CTRKRCfEFPTIANGFVVDSTRAYLFGDEARVQCFKGYKLIGSNIMRC 778
Cdd:PHA02831  136 CKLIRC-KYPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTC 182
EGF_CA smart00179
Calcium-binding EGF-like domain;
2178-2214 2.19e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.86  E-value: 2.19e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 386769253   2178 NINDC-SENPCLLGANCTDLVNDFQCACPPGFT-GKRCE 2214
Cdd:smart00179    1 DIDECaSGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
2486-2520 2.93e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.47  E-value: 2.93e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 386769253   2486 DACEE-HVCQNGATCVDNGAGYSCQCPPGFT-GRNCE 2520
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 736-791 4.31e-06

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: 46.30  E-value: 4.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769253  736 CFEFPTIANGFVVDSTRAYLFGDEARVQCFKGYKLIGSNIMRCSEAQKFEQ-PPTCE 791
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPpPPTCE 57
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 988-1016 4.69e-06

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 45.70  E-value: 4.69e-06
                           10        20
                   ....*....|....*....|....*....
gi 386769253   988 CSKNNGGCDQKCINSPGGFACGCNTGYQL 1016
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYEL 29
HYR pfam02494
HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin ...
 1548-1631 5.38e-06

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.


Pssm-ID: 460572 [Multi-domain]  Cd Length: 81  Bit Score: 47.00  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  1548 PDVTPPLLQCPQS--YVIELvdrqDSYTVNFNDTRKRIKTSDDTGDVRLQFSPESANIKIGnFENVTVTATDKYNNRAAC 1625
Cdd:pfam02494    1 VDTTPPTVKCPNNivRTVEL----GTSTVRVFFTEPTAFDNSGQAILVSRTAQPGDFFPVG-TTTVTYVAYDNSGNRASC 75


                   ....*.
gi 386769253  1626 HFQVSV 1631
Cdd:pfam02494   76 TFTVTV 81
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 995-1106 9.29e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 50.42  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  995 CDQKCINSPGGFACGCNTGYQLYTSNGT-------AGYHIERSESGERDGDTYQRNKTCVPLMCPElEAPENGQLLSD-K 1066
Cdd:PHA02927  143 CESVKCQSPPSISNGRHNGYEDFYTDGSvvtyscnSGYSLIGNSGVLCSGGEWSDPPTCQIVKCPH-PTISNGYLSSGfK 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386769253 1067 NDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:PHA02927  222 RSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2488-2518 9.61e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 9.61e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2488 CEEHVCQNGATCVDNGAGYSCQCPPGFTGRN 2518
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PHA02639 PHA02639
EEV host range protein; Provisional
 603-790 1.29e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 50.05  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  603 VSYIPKCQEVYCGPVPQIDNGFSIGSSNVTYRG-IAMYQCYAGFAFASGAPIEKISCLPDGRWE-RQPHCMASQCAALPE 680
Cdd:PHA02639   11 VCYVHGVKSIYCDKPDDISNGFITELMEKYEIGkLIEYTCNTDYALIGDRFRTCIKDKNNAIWSnKAPFCMLKECNDPPS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  681 VAHANVTLLNGGGRsYGTIVQYECEP----GYERNGHPVLTCMSNGTWSGDVPRCTRKRCfEFPTIANGFV--VDSTRAY 754
Cdd:PHA02639   91 IINGKIYNKREMYK-VGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINC-RFPALQNGYIngIPSNKKF 168

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 386769253  755 LFGDEARVQCFKGYKLIGSNIMRCS-EAQKFEQPPTC 790
Cdd:PHA02639  169 YYKTRVGFSCKSGFDLVGEKYSTCNiNATWFPSIPTC 205
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 963-1111 1.86e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 49.27  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  963 DYVGAPCLRMELMG-----CTRLDCVDINECSK---------NNGGCDQKCINSPGGFACGCNTGYQL------YTSNGT 1022
Cdd:PHA02927   51 EYLCLPGYRKQKMGpiyakCTGTGWTLFNQCIKrrcpsprdiDNGQLDIGGVDFGSSITYSCNSGYQLigesksYCELGS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253 1023 AGYHIERSESgerdgdtyqrnKTCVPLMCPELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALClSSGQWnAS 1102
Cdd:PHA02927  131 TGSMVWNPEA-----------PICESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSCNSGYSLIGNSGVLC-SGGEW-SD 197


                  ....*....
gi 386769253 1103 VPECNYAKC 1111
Cdd:PHA02927  198 PPTCQIVKC 206
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2063-2093 1.91e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.91  E-value: 1.91e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2063 CASQPCYNGGQCKDLPQGYRCECPAGYSGIN 2093
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2138-2176 2.60e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 2.60e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 386769253 2138 IDPCtANGNPCGNGASCQALEqGRYKCECVPGWEGIHCE 2176
Cdd:cd00054     2 IDEC-ASGNPCQNGGTCVNTV-GSYRCSCPPGYTGRNCE 38
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2491-2520 3.59e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 43.23  E-value: 3.59e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386769253 2491 HVCQNGATCVDNGAGYSCQCPPGFTG-RNCE 2520
Cdd:cd00053     6 NPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 736-790 3.66e-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: 43.67  E-value: 3.66e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253    736 CFEFPTIANGFVVDSTRAYLFGDEARVQCFKGYKLIGSNIMRCSEAQKF-EQPPTC 790
Cdd:smart00032    1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWsPPPPTC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 1036-1106 5.47e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 48.06  E-value: 5.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769253 1036 DGDTYQRNKTCVPLMCpELEAPENGQLLSDKNDYHFGDVVRFQCHFGYIMSGSSAALCLSSGQWNASVPEC 1106
Cdd:PHA02831  126 NKQWVPKYPVCKLIRC-KYPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
 708-790 7.86e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 46.86  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  708 YERNGHPVLTCMSNGTWSGDVPRCTRKRCfEFPTIANGFV--VDSTRAYLFGDEARVQCFKGYKLIGSNIMRCS-EAQKF 784
Cdd:PHA02817   61 YTLVGEKNIICEKDGKWNKEFPVCKIIRC-RFPALQNGFVngIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGiNSSWI 139


                  ....*.
gi 386769253  785 EQPPTC 790
Cdd:PHA02817  140 PKVPIC 145
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2295-2323 7.92e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.98  E-value: 7.92e-05
                           10        20
                   ....*....|....*....|....*....
gi 386769253  2295 CASNPCQHGATCVDQLDGFSCKCRPGYVG 2323
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2257-2287 8.00e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.98  E-value: 8.00e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2257 CENRPCANEGTCVDLVDGYSCNCEPGYTGKN 2287
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2296-2327 1.27e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 41.69  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 386769253 2296 ASNPCQHGATCVDQLDGFSCKCRPGYVG-LSCE 2327
Cdd:cd00053     4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
792-829 1.38e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.46  E-value: 1.38e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 386769253    792 DINECSSSQCDLTTTECQNTNGSFHCQCRTGFTATTEC 829
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRNC 38
LamGL smart00560
LamG-like jellyroll fold domain;
2590-2735 1.59e-04

LamG-like jellyroll fold domain;


Pssm-ID: 214722 [Multi-domain]  Cd Length: 133  Bit Score: 44.33  E-value: 1.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   2590 SLTVAMWVQFAQkddrgifftlYGVQSARMTQQrrmLLQAHSSgvqvslFEDQPDAFLSFGEY----------TSVNDGQ 2659
Cdd:smart00560    2 SFTLEAWVKLES----------AGGSQPIITGA---AVAQPTI------SEKALTFFLRAKSVqgwqtartgaTADWIGV 62

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253   2660 WHHVAVVWDGISGQLQLITEGLIASKMEYGAGGSLPgylwavlGLPQPYGLSNELAYSDSgFQGTITKAQVWARAL 2735
Cdd:smart00560   63 WVHLAGVYDGGAGKLSLYVNGVEVATSETQPSPSSG-------NLPQGGRILLGGAGGEN-FSGRLDEVRVYNRAL 130
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2182-2212 2.24e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.83  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2182 CSENPCLLGANCTDLVNDFQCACPPGFTGKR 2212
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2062-2095 2.41e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.92  E-value: 2.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386769253 2062 ECA-SQPCYNGGQCKDLPQGYRCECPAGYSG-INCQ 2095
Cdd:cd00053     1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 2493-2514 2.57e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 40.40  E-value: 2.57e-04
                           10        20
                   ....*....|....*....|..
gi 386769253  2493 CQNGATCVDNGAGYSCQCPPGF 2514
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 36-104 2.81e-04

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 43.09  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769253   36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYGAELVAIDsyaeNNETLAIARasdpNQRASDKYWLGL 104
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID----DEEELEFLQ----SQIGSSSYWIGL 61
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2411-2444 3.95e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.31  E-value: 3.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253 2411 CGAQAPCQNDASCIDLFQDYFCVCPSGTDGKNCE 2444
Cdd:cd00054     5 CASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02639 PHA02639
EEV host range protein; Provisional
 571-735 4.03e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.43  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  571 GTLVSFTCpiGQEFATGKTRLVTeCLRGGN---WSvSYIPKCQEVYCGPVPQIDNGFSIGSSNVTYRGIAMYQC---YAG 644
Cdd:PHA02639   43 GKLIEYTC--NTDYALIGDRFRT-CIKDKNnaiWS-NKAPFCMLKECNDPPSIINGKIYNKREMYKVGDEIYYVcneHKG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  645 FAFaSGAPIEKISCLPDGRWERQPHCMASQCAALPEVAHANVTLLNGGGR-SYGTIVQYECEPGYERNGHPVLTCMSNGT 723
Cdd:PHA02639  119 VQY-SLVGNEKITCIQDKSWKPDPPICKMINCRFPALQNGYINGIPSNKKfYYKTRVGFSCKSGFDLVGEKYSTCNINAT 197

                         170
                  ....*....|..
gi 386769253  724 WSGDVPRCTRKR 735
Cdd:PHA02639  198 WFPSIPTCVRNK 209
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 2581-2742 4.78e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 43.14  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2581 VPFPTGEANSLTVAMWVQFAQKDDRG-IFFTL--YGVQSARMTQQRRMLLQAHSSGVQVSLFEDQpdaflsfgeyTSVND 2657
Cdd:pfam13385    9 LPDALLPTSDFTVSAWVKPDSLPGWArAIISSsgGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSG----------ASVPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  2658 GQWHHVAVVWDG------ISGQLQLITEGliaskmeygaGGSLPGYLWAVLGLPQPYGlsnelaySDSGFQGTITKAQVW 2731
Cdd:pfam13385   79 GQWTHVAVTYDGgtlrlyVNGVLVGSSTL----------TGGPPPGTGGPLYIGRSPG-------GDDYFNGLIDEVRIY 141

                          170
                   ....*....|.
gi 386769253  2732 ARALDiTSEIQ 2742
Cdd:pfam13385  142 DRALS-AAEIA 151
VSP pfam03302
Giardia variant-specific surface protein;
3127-3342 7.64e-04

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 44.96  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  3127 GSEYACPVGQVVMIPDCVPCAIGTFYDSANKTCIACSRGTYQSEAGQLQCSKCPVIAGRPGVTAGP--------GARSAA 3198
Cdd:pfam03302   44 SNNYLTPTSQCIDDCAKIGNYYYTTNANNKKICKECTVANCKTCEDQGQCQACNDGFYKSGDACSPchescktcSGGTAS 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  3199 DCKErCPAGK---YFDAETGLcrSCGHGFYQpNEGSFSCELCGL--GQTTRSTEATSRKE-----------CRDECSSGQ 3262
Cdd:pfam03302  124 DCTE-CLTGKalrYGNDGTKG--TCGEGCTT-GTGAGACKTCGLtiDGTSYCSECATETEypqngvctstaARATATCKA 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  3263 QLGADGRCEPCPRGTYRLQG---------VQPSCAACPLGRTTPK-VGASSVEECTLPVCSAGTYLNATQNMCIECRKGY 3332
Cdd:pfam03302  200 SSVANGMCSSCANGYFRMNGgcyettkfpGKSVCEEANSGGTCQKeAPGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGY 279

                          250
                   ....*....|
gi 386769253  3333 YQSESQQTSC 3342
Cdd:pfam03302  280 VKTSDSCTKC 289
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2258-2289 9.55e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 39.38  E-value: 9.55e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 386769253 2258 ENRPCANEGTCVDLVDGYSCNCEPGYTG-KNCQ 2289
Cdd:cd00053     4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 47-167 9.87e-04

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 41.67  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   47 CYKYFNIKHSWDKSAELCRR-YGAELVAIDSYAENNETLAIARASDPNQrasdkYWLGLASLDDLRTNTLESASGAliSQ 125
Cdd:cd03598     3 CYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQ-----VWIGGIITGKGRCRRFSWVDGS--VW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 386769253  126 YSGYWSLHQPNAESGECVaaAFAGKSQSWDLGTCESLLPFMC 167
Cdd:cd03598    76 NYAYWAPGQPGNRRGHCV--ELCTRGGHWRRAHCKLRRPFIC 115
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2025-2055 1.42e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.52  E-value: 1.42e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386769253  2025 CGEGACQHGGLCVPMGHDIQCFCPAGFSGRR 2055
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 36-168 1.52e-03

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 41.41  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253   36 CPNGWELRGLNCYKYFNIKHSWDKSAELCRRYGAELVAIDSYAENNETlaiarasdpNQRASDKYWLGLAslDDLRTNTL 115
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---------NNNAQDYQWIGLN--DRTIEGDF 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769253  116 ESASGALIsQYSGyWSLHQPNA--ESGE-CVAAAFAGKSQsWDLGTCESLLPFMCR 168
Cdd:cd03588    70 RWSDGHPL-QFEN-WRPNQPDNffATGEdCVVMIWHEEGE-WNDVPCNYHLPFTCK 122
EGF_CA smart00179
Calcium-binding EGF-like domain;
2138-2176 1.77e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 1.77e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 386769253   2138 IDPCtANGNPCGNGASCQALEqGRYKCECVPGWE-GIHCE 2176
Cdd:smart00179    2 IDEC-ASGNPCQNGGTCVNTV-GSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2373-2401 1.85e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.13  E-value: 1.85e-03
                           10        20
                   ....*....|....*....|....*....
gi 386769253  2373 CEAQPCLNNGICRDRVGGFECGCEPGWSG 2401
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
PHA02831 PHA02831
EEV host range protein; Provisional
 700-793 2.44e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 42.67  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769253  700 VQYECEPGYERnghpVLTCMSNGTWSGDVPRCTRKRCFEFPTIANGFVVDSTRAYLFGDEARVQC----FKGYKLIGSNI 775
Cdd:PHA02831   46 LEYKCNNNFDK----VFVTCNNGSWSTKNMCIGKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNET 121

                          90
                  ....*....|....*...
gi 386769253  776 MRCSEAQKFEQPPTCEDI 793
Cdd:PHA02831  122 VKCINKQWVPKYPVCKLI 139
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2522-2557 2.54e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769253 2522 DIVDCKD-NSCPPGATCVDLTNGFYCQCPFNMTGDDC 2557
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
2411-2444 2.79e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.00  E-value: 2.79e-03
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 386769253   2411 CGAQAPCQNDASCIDLFQDYFCVCPSG-TDGKNCE 2444
Cdd:smart00179    5 CASGNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39
LamG smart00282
Laminin G domain;
2618-2676 2.97e-03

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 40.40  E-value: 2.97e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769253   2618 RMTQQRRMLLQAHSSG----VQVSLFEDQPDAFLSFG--------EYTSVNDGQWHHVAVVWDGISGQLQL 2676
Cdd:smart00282    7 RTTSPNGLLLYAGSKGggdyLALELRDGRLVLRYDLGsgparltsDPTPLNDGQWHRVAVERNGRSVTLSV 77
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 2068-2089 3.29e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 37.31  E-value: 3.29e-03
                           10        20
                   ....*....|....*....|..
gi 386769253  2068 CYNGGQCKDLPQGYRCECPAGY 2089
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2185-2214 3.30e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.84  E-value: 3.30e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386769253 2185 NPCLLGANCTDLVNDFQCACPPGFTG-KRCE 2214
Cdd:cd00053     6 NPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 792-824 3.58e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 3.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253  792 DINECSS-SQCDLTTTeCQNTNGSFHCQCRTGFT 824
Cdd:cd00054     1 DIDECASgNPCQNGGT-CVNTVGSYRCSCPPGYT 33
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 2300-2321 3.63e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 37.31  E-value: 3.63e-03
                           10        20
                   ....*....|....*....|..
gi 386769253  2300 CQHGATCVDQLDGFSCKCRPGY 2321
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2376-2405 3.64e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.46  E-value: 3.64e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386769253 2376 QPCLNNGICRDRVGGFECGCEPGWSG-MRCE 2405
Cdd:cd00053     6 NPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 1046-1115 4.03e-03

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 41.95  E-value: 4.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769253 1046 CVPLMCPELEAPENGQLlsDKNDYHFGDVVRFQCHFGYIMSGSSAALC----LSSGQWNASVPECNYAKCVSLP 1115
Cdd:PHA02927   81 CIKRRCPSPRDIDNGQL--DIGGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPP 152
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 2262-2283 7.81e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 36.16  E-value: 7.81e-03
                           10        20
                   ....*....|....*....|..
gi 386769253  2262 CANEGTCVDLVDGYSCNCEPGY 2283
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 984-1016 8.03e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.46  E-value: 8.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386769253  984 DINECSKNNG-GCDQKCINSPGGFACGCNTGYQL 1016
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
984-1015 8.66e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 8.66e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 386769253    984 DINECSKNNG-GCDQKCINSPGGFACGCNTGYQ 1015
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGYT 33
 
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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