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Conserved domains on  [gi|545215474|ref|XP_005609700|]
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L-selectin isoform X2 [Equus caballus]

Protein Classification

beta-2-glycoprotein 1( domain architecture ID 12933809)

beta-2-glycoprotein 1 is a heavily glycosylated plasma membrane-adhesion protein, which plays a role in blood coagulation and removal of apoptotic bodies

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 39-157 1.40e-47

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


:

Pssm-ID: 153062  Cd Length: 115  Bit Score: 160.62  E-value: 1.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  39 WTYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNE-VLPFNRNYYWIGIRKVGTTWTWVGTNKPLtEEAENWGDG 117
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 545215474 118 EPNNKKSkEDCVEIYIKrfrDAGKWNDDACHKNKTALCYT 157
Cdd:cd03592   80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 281-440 1.01e-13

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 281 FTSTCTFNCSEGTELIGERKTIC--GSSG--IWSSTSPKCQVIQCeplQAPELGTMACVHPLGNFSFSSQCV-FNCSEGR 355
Cdd:PHA02927 104 FGSSITYSCNSGYQLIGESKSYCelGSTGsmVWNPEAPICESVKC---QSPPSISNGRHNGYEDFYTDGSVVtYSCNSGY 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 356 EIVGIEETTCGpSGKWSSPePTCQVIQCEPLTAPDlGTMDCSHPLAdFSFTSTCTFNCSEGTELIGERKTICGSSGIWSS 435
Cdd:PHA02927 181 SLIGNSGVLCS-GGEWSDP-PTCQIVKCPHPTISN-GYLSSGFKRS-YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQP 256


                 ....*
gi 545215474 436 TSPMC 440
Cdd:PHA02927 257 ELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 197-255 7.71e-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: 54.78  E-value: 7.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 197 CEPLQAPELGTMACvhPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTCQ 255
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
 
Name Accession Description Interval E-value
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 39-157 1.40e-47

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 160.62  E-value: 1.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  39 WTYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNE-VLPFNRNYYWIGIRKVGTTWTWVGTNKPLtEEAENWGDG 117
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 545215474 118 EPNNKKSkEDCVEIYIKrfrDAGKWNDDACHKNKTALCYT 157
Cdd:cd03592   80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 47-157 3.56e-23

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 94.08  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474   47 PMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNRNYYWIGI--RKVGTTWTWVGTNkplTEEAENWGdGEPNNKKS 124
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWA-PEPNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 545215474  125 KEDCVEIYikrfRDAGKWNDDACHKNKTALCYT 157
Cdd:pfam00059  77 NEDCVELS----SSSGKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 27-155 2.29e-19

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: 83.80  E-value: 2.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474    27 CCDFFTHHGTNCwtYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLP--FNRNYYWIGIR--KVGTTWTWVG 102
Cdd:smart00034   1 CPSGWISYGGKC--YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSdpDSNGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 545215474   103 TNKPLTeeAENWGDGEPNNkkSKEDCVEIYIKRfrdaGKWNDDACHKNKTALC 155
Cdd:smart00034  79 GSGPVS--YSNWAPGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 281-440 1.01e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 281 FTSTCTFNCSEGTELIGERKTIC--GSSG--IWSSTSPKCQVIQCeplQAPELGTMACVHPLGNFSFSSQCV-FNCSEGR 355
Cdd:PHA02927 104 FGSSITYSCNSGYQLIGESKSYCelGSTGsmVWNPEAPICESVKC---QSPPSISNGRHNGYEDFYTDGSVVtYSCNSGY 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 356 EIVGIEETTCGpSGKWSSPePTCQVIQCEPLTAPDlGTMDCSHPLAdFSFTSTCTFNCSEGTELIGERKTICGSSGIWSS 435
Cdd:PHA02927 181 SLIGNSGVLCS-GGEWSDP-PTCQIVKCPHPTISN-GYLSSGFKRS-YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQP 256


                 ....*
gi 545215474 436 TSPMC 440
Cdd:PHA02927 257 ELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 197-255 7.71e-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: 54.78  E-value: 7.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 197 CEPLQAPELGTMACvhPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTCQ 255
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 321-379 7.71e-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: 54.78  E-value: 7.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 321 CEPLQAPELGTMACvhPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTCQ 379
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 197-254 4.02e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 49.83  E-value: 4.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   197 CEPLQAPELGTMACVHplGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 254
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 321-378 4.02e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 49.83  E-value: 4.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   321 CEPLQAPELGTMACVHplGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 378
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 217-316 7.22e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 217 FSFSSQCVFNCSEGR-----EIVGIEETTCGPSGKWSSPEPTCQVIQCEpLTAPDLGTMDCSHPLADFSFTSTCTFNCSE 291
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100
                 ....*....|....*....|....*
gi 545215474 292 GTELIGERKTICGSSGIWSSTSPKC 316
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
212-254 4.48e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.95  E-value: 4.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 545215474  212 HPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 254
Cdd:pfam00084  14 ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
336-378 4.48e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.95  E-value: 4.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 545215474  336 HPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 378
Cdd:pfam00084  14 ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
 
Name Accession Description Interval E-value
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 39-157 1.40e-47

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 160.62  E-value: 1.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  39 WTYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNE-VLPFNRNYYWIGIRKVGTTWTWVGTNKPLtEEAENWGDG 117
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGfALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 545215474 118 EPNNKKSkEDCVEIYIKrfrDAGKWNDDACHKNKTALCYT 157
Cdd:cd03592   80 EPNNGRN-ENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 47-157 3.56e-23

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 94.08  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474   47 PMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNRNYYWIGI--RKVGTTWTWVGTNkplTEEAENWGdGEPNNKKS 124
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWA-PEPNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 545215474  125 KEDCVEIYikrfRDAGKWNDDACHKNKTALCYT 157
Cdd:pfam00059  77 NEDCVELS----SSSGKWNDENCNSKNPFVCEK 105
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 33-155 1.78e-20

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: 86.97  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  33 HHGTNCwtYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNRNyYWIGIRKVGT--TWTWV-GTnkPLTE 109
Cdd:cd03590    7 SFQSSC--YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETegEWKWVdGT--PLNS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 545215474 110 EAENWGDGEPNNKKS-KEDCVEIyikrFRDAGKWNDDACHKNKTALC 155
Cdd:cd03590   82 SKTFWHPGEPNNWGGgGEDCAEL----VYDSGGWNDVPCNLEYRWIC 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 39-156 3.49e-20

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: 86.13  E-value: 3.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  39 WTYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLP-FNRNYYWIGIRKVGT--TWTWVGTNKPLTeeAENWG 115
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLSSegTWKWSDGSPLVD--YTNWA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 545215474 116 DGEPNNKKSkEDCVEIYIkrfRDAGKWNDDACHKNKTALCY 156
Cdd:cd00037   79 PGEPNPGGS-EDCVVLSS---SSDGKWNDVSCSSKLPFICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 27-155 2.29e-19

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: 83.80  E-value: 2.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474    27 CCDFFTHHGTNCwtYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLP--FNRNYYWIGIR--KVGTTWTWVG 102
Cdd:smart00034   1 CPSGWISYGGKC--YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSdpDSNGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 545215474   103 TNKPLTeeAENWGDGEPNNkkSKEDCVEIYIKRfrdaGKWNDDACHKNKTALC 155
Cdd:smart00034  79 GSGPVS--YSNWAPGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 48-155 9.97e-16

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 73.10  E-value: 9.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  48 MNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNRNYYWIGIRKVGTTWTWV-GTNKPLTeeAENWGDGEPNNKKSKE 126
Cdd:cd03591   11 KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVyLDGGPLT--YTNWKPGEPNNAGGGE 88

                         90       100
                 ....*....|....*....|....*....
gi 545215474 127 DCVEIYikrfrDAGKWNDDACHKNKTALC 155
Cdd:cd03591   89 DCVEMY-----TSGKWNDVACNLTRLFVC 112
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 281-440 1.01e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 281 FTSTCTFNCSEGTELIGERKTIC--GSSG--IWSSTSPKCQVIQCeplQAPELGTMACVHPLGNFSFSSQCV-FNCSEGR 355
Cdd:PHA02927 104 FGSSITYSCNSGYQLIGESKSYCelGSTGsmVWNPEAPICESVKC---QSPPSISNGRHNGYEDFYTDGSVVtYSCNSGY 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 356 EIVGIEETTCGpSGKWSSPePTCQVIQCEPLTAPDlGTMDCSHPLAdFSFTSTCTFNCSEGTELIGERKTICGSSGIWSS 435
Cdd:PHA02927 181 SLIGNSGVLCS-GGEWSDP-PTCQIVKCPHPTISN-GYLSSGFKRS-YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQP 256


                 ....*
gi 545215474 436 TSPMC 440
Cdd:PHA02927 257 ELPKC 261
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 40-156 1.11e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. 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. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 67.01  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  40 TYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNRNYYWIGIRKVGTTWTWVGTNkplTEEAENWGdgeP 119
Cdd:cd03602    2 TFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGS---ESSFRNWN---T 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 545215474 120 NNKKSKEDCVEIYIkrfrdAGKWNDDACHKNKTALCY 156
Cdd:cd03602   76 FQPFGQGDCATMYS-----SGRWYAALCSALKPFICY 107
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 214-378 1.71e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 64.67  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 214 LGNFSFSSQCVFNCSEGREIVGIEETTC--GPSGK--WSSPEPTCQVIQCEPLTAPDLGTMDCSHPLadFSFTSTCTFNC 289
Cdd:PHA02927  99 IGGVDFGSSITYSCNSGYQLIGESKSYCelGSTGSmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSC 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 290 SEGTELIGERKTICgSSGIWSStSPKCQVIQCePLQAPELGTMACVHPLgNFSFSSQCVFNCSEGREIVGIEETTCGPSG 369
Cdd:PHA02927 177 NSGYSLIGNSGVLC-SGGEWSD-PPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGN 252


                 ....*....
gi 545215474 370 KWSSPEPTC 378
Cdd:PHA02927 253 TWQPELPKC 261
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 40-151 8.79e-11

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 59.36  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  40 TYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPFNrNYYWIGIRKVGTTWTWVGTNKPlTEEAENWGDGEP 119
Cdd:cd03603    2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKWSDGE-ESTYTNWGSGEP 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545215474 120 -NNKKSKEDCVEIYIKRFRDaGKWNDDACHKNK 151
Cdd:cd03603   80 hNNGGGNEDYAAINHFPGIS-GKWNDLANSYNT 111
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 197-255 7.71e-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: 54.78  E-value: 7.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 197 CEPLQAPELGTMACvhPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTCQ 255
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 321-379 7.71e-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: 54.78  E-value: 7.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 321 CEPLQAPELGTMACvhPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTCQ 379
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 44-155 9.81e-10

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 56.39  E-value: 9.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  44 SEKPMNWSGARKFCQENYTDLvAIQNKGEIEYLNEVLPFN--RNY-YWIGI---RKVGTTWTWvGTNKPLTEEAENWGDG 117
Cdd:cd03601    6 SDETMNYAKAGAFCRSRGMRL-ASLAMRDSEMRDAILAFTlvKGHgYWVGAdnlQDGEYDFLW-NDGVSLPTDSDLWAPN 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 545215474 118 EPNNKKSKEDCVEIYIKRfrdaGKWNDDACHKNKTALC 155
Cdd:cd03601   84 EPSNPQSRQLCVQLWSKY----NLLDDEYCGRAKRVIC 117
PHA02639 PHA02639
EEV host range protein; Provisional
 287-440 1.10e-09

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 59.68  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 287 FNCSEGTELIGERKTIC---GSSGIWSSTSPKCQVIQCEplQAPELGTMACVHPLGNFSFSSQCVFNCSEGR----EIVG 359
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECN--DPPSIINGKIYNKREMYKVGDEIYYVCNEHKgvqySLVG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 360 IEETTCGPSGKWSSPEPTCQVIQCEpLTAPDLGTMDCSHPLADFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPM 439
Cdd:PHA02639 126 NEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPT 204


                 .
gi 545215474 440 C 440
Cdd:PHA02639 205 C 205
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 259-317 3.66e-09

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 52.85  E-value: 3.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 259 CEPLTAPDLGTMDCSHPlaDFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPKCQ 317
Cdd:cd00033    1 CPPPPVPENGTVTGSKG--SYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 383-441 1.12e-08

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: 51.31  E-value: 1.12e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545215474 383 CEPLTAPDLGTMDCSHPlaDFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPMCQ 441
Cdd:cd00033    1 CPPPPVPENGTVTGSKG--SYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02817 PHA02817
EEV Host range protein; Provisional
 341-450 3.03e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 54.18  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 341 FSFSSQCVFNCSEGR-----EIVGIEETTCGPSGKWSSPEPTCQVIQCEpLTAPDLGTMDCSHPLADFSFTSTCTFNCSE 415
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 545215474 416 GTELIGERKTICGSSGIWSSTSPMCQKLDRSFTAI 450
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPICSRDNITYNKI 155
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 27-147 3.70e-08

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: 52.36  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  27 CCDFFTHHGTNCWTYHYSEKPmnWSGARKFCQEnYT------DLVAIQNKGE----IEYLNEVLPFNRNY-YWIGI--RK 93
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLT--WEEAELRCRS-FSipgliaHLVSIHSQEEndfvYDLFESSRGPDTPYgLWIGLhdRT 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 545215474  94 VGTTWTWV-GTNKPLTeeaeNWGDGEPNNKKSKEDCVEIYiKRFRDAGKWNDDAC 147
Cdd:cd03589   78 SEGPFEWTdGSPVDFT----KWAGGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPC 127
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 197-254 4.02e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 49.83  E-value: 4.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   197 CEPLQAPELGTMACVHplGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 254
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 321-378 4.02e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 49.83  E-value: 4.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   321 CEPLQAPELGTMACVHplGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 378
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 259-316 8.23e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 48.68  E-value: 8.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   259 CEPLTAPDLGTMDCSHPlaDFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPKC 316
Cdd:smart00032   1 CPPPPDIENGTVTSSSG--TYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 383-440 3.80e-07

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: 47.14  E-value: 3.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474   383 CEPLTAPDLGTMDCSHPlaDFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPMC 440
Cdd:smart00032   1 CPPPPDIENGTVTSSSG--TYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 34-101 6.08e-06

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: 45.40  E-value: 6.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  34 HGTNCwtYHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVLPfnRNYYWIGIR--KVGTTWTWV 101
Cdd:cd03593    8 YGNKC--YYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG--SSSYWIGLSreKSEKPWKWI 73
PHA02817 PHA02817
EEV Host range protein; Provisional
 279-378 6.64e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 6.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 279 FSFTSTCTFNCSEGT-----ELIGERKTICGSSGIWSSTSPKCQVIQCEpLQAPELGTMACVHPLGNFSFSSQCVFNCSE 353
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100
                 ....*....|....*....|....*
gi 545215474 354 GREIVGIEETTCGPSGKWSSPEPTC 378
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02817 PHA02817
EEV Host range protein; Provisional
 217-316 7.22e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 217 FSFSSQCVFNCSEGR-----EIVGIEETTCGPSGKWSSPEPTCQVIQCEpLTAPDLGTMDCSHPLADFSFTSTCTFNCSE 291
Cdd:PHA02817  42 YNIGSNVTFFCGNNTrgvryTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKP 120

                         90       100
                 ....*....|....*....|....*
gi 545215474 292 GTELIGERKTICGSSGIWSSTSPKC 316
Cdd:PHA02817 121 GFVLIGTKYSVCGINSSWIPKVPIC 145
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 41-155 9.36e-06

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: 44.88  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  41 YHYSEKPMNWSGARKFCQENYTDLVAIQNKGEIEYLNEVlpfNRNYYWIGI--RKVGTTWTWVGTNkPLteEAENWGDGE 118
Cdd:cd03588   13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN---AQDYQWIGLndRTIEGDFRWSDGH-PL--QFENWRPNQ 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 545215474 119 PNNK-KSKEDCVeiyIKRFRDAGKWNDDACHKNKTALC 155
Cdd:cd03588   87 PDNFfATGEDCV---VMIWHEEGEWNDVPCNYHLPFTC 121
PHA02639 PHA02639
EEV host range protein; Provisional
 217-316 3.11e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.81  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 217 FSFSSQCVFNCSEGR----EIVGIEETTCGPSGKWSSPEPTCQVIQCEpLTAPDLGTMDCSHPLADFSFTSTCTFNCSEG 292
Cdd:PHA02639 103 YKVGDEIYYVCNEHKgvqySLVGNEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPSNKKFYYKTRVGFSCKSG 181

                         90       100
                 ....*....|....*....|....
gi 545215474 293 TELIGERKTICGSSGIWSSTSPKC 316
Cdd:PHA02639 182 FDLVGEKYSTCNINATWFPSIPTC 205
Sushi pfam00084
Sushi repeat (SCR repeat);
212-254 4.48e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.95  E-value: 4.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 545215474  212 HPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 254
Cdd:pfam00084  14 ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
336-378 4.48e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.95  E-value: 4.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 545215474  336 HPLGNFSFSSQCVFNCSEGREIVGIEETTCGPSGKWSSPEPTC 378
Cdd:pfam00084  14 ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 218-316 1.65e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 43.44  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 218 SFSSQCVFNCSEGREIVGIEETTCgPSGKWSSPEPTCQVIQCEpltAPDLGTMDCSHPLADFSFTSTCTFNCSEGTELIG 297
Cdd:PHA02831 101 SVTYACKVNKLEKYSIVGNETVKC-INKQWVPKYPVCKLIRCK---YPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLG 176

                         90
                 ....*....|....*....
gi 545215474 298 ERKTICGSSGIWSSTSPKC 316
Cdd:PHA02831 177 SSVSTCDINSIWYPGIPKC 195
PHA02831 PHA02831
EEV host range protein; Provisional
 342-442 5.48e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 41.90  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 342 SFSSQCVFNCSEGREIVGIEETTCgPSGKWSSPEPTCQVIQCEpltAPDLGTMDCSHPLADFSFTSTCTFNCSEGTELIG 421
Cdd:PHA02831 101 SVTYACKVNKLEKYSIVGNETVKC-INKQWVPKYPVCKLIRCK---YPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLG 176

                         90       100
                 ....*....|....*....|.
gi 545215474 422 ERKTICGSSGIWSSTSPMCQK 442
Cdd:PHA02831 177 SSVSTCDINSIWYPGIPKCVK 197
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 34-155 6.60e-04

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: 39.66  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474  34 HGTNCwtYHYSEKPMNWSGARKFCQENY--TDLVAIQNKGEIEYLNEVLPFNRN---YYWIGIR--KVGTTWTWVGTNKP 106
Cdd:cd03594    8 YKGNC--YGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQKayqPVWIGLHdpQQSRGWEWSDGSKL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 545215474 107 LTeeaENWGDGEPNNkkSKEDCVEiyIKRFRDAGKWNDDACHKNKTALC 155
Cdd:cd03594   86 DY---RSWDRNPPYA--RGGYCAE--LSRSTGFLKWNDANCEERNPFIC 127
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 279-453 2.30e-03

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 40.07  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 279 FSFTSTCTFNCSEGTELIGERKTICGSSgiWSSTSpKCQVIQCEPLQapeLGTMACVHPLGNFSFSSQCVFNCSEGREIV 358
Cdd:PHA02954  91 YEVNSTITLICKDETKYFRCEEKNGNTS--WNDTV-TCPNAECQPLQ---LEHGSCQPVKEKYSFGEHITINCDVGYEVI 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545215474 359 GIEETTCgPSGKWSSPePTCQviqcEPLTAPDLGTMDCSHplADFSFTSTCTFNCSEGTELIGERKTICgSSGIWSSTSP 438
Cdd:PHA02954 165 GASYISC-TANSWNVI-PSCQ----QKCDIPSLSNGLISG--STFSIGGVIHLSCKSGFTLTGSPSSTC-IDGKWNPVLP 235

                        170
                 ....*....|....*
gi 545215474 439 MCQKLDRSFTAIKEG 453
Cdd:PHA02954 236 ICVRSNEEFDPVDDG 250
Sushi pfam00084
Sushi repeat (SCR repeat);
259-316 6.53e-03

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 35.17  E-value: 6.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 545215474  259 CEPLTAPDLGtmDCSHPLADFSFTSTCTFNCSEGTELIGERKTICGSSGIWSSTSPKC 316
Cdd:pfam00084   1 CPPPPDIPNG--KVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 405-456 7.94e-03

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 38.10  E-value: 7.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 545215474 405 FTSTCTFNCSEGTELIGERKTIC--GSSG--IWSSTSPMCQKLD-RSFTAIKEGDYN 456
Cdd:PHA02927 104 FGSSITYSCNSGYQLIGESKSYCelGSTGsmVWNPEAPICESVKcQSPPSISNGRHN 160
 
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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