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Conserved domains on  [gi|157419154|ref|NP_002996|]
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P-selectin precursor [Homo sapiens]

Protein Classification

calcium-binding EGF-like domain-containing protein; wall-associated receptor kinase family protein( domain architecture ID 12933829)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions; wall-associated receptor kinase (WAK) family protein containing the calcium-binding EGF and serine/threonine kinase domains but lacking the WAK galacturonan-binding domain, catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and may function as a signaling receptor of extracellular matrix component

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 ...
42-160 1.31e-56

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: 189.51  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157419154 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
219-443 2.52e-18

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 85.86  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 219 NFSFNSQCSFHCTDGY--QVNGPSKLECLASGiWTnKPPQCLAAQCPPLKIPERGNMtclhSAKAFQHQSSCSFSCEEGF 296
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYrkQKMGPIYAKCTGTG-WT-LFNQCIKRRCPSPRDIDNGQL----DIGGVDFGSSITYSCNSGY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 297 ALVGPEVVQC----TASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLtaFAYGSSCKFECQPGYRVRGLDMLRCiDSG 372
Cdd:PHA02927 117 QLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGG 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419154 373 HWSAPlPTCEAISCePLESPVHGSMDcSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:PHA02927 194 EWSDP-PTCQIVKC-PHPTISNGYLS-SGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
342-567 1.37e-15

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.77  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419154 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
505-761 1.07e-14

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.07  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 505 CQAIPCTPL-LSPQNGtmtcVQPLGSSSYK--STCQFICDEGYSLS--GPERLDCTRSGrWTDSPpMCEAIKCPELFAPE 579
Cdd:PHA02927  20 CCTIPSRPInMKFKNS----VETDANANYNigDTIEYLCLPGYRKQkmGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDID 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 580 QGSLDCsdtrGEFNVGSTCHFSCDNGFKLEGPNNVEC----TTSGRWSATPPTCKGiaslptpgVQCPALTTPGQGtmyc 655
Cdd:PHA02927  94 NGQLDI----GGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICES--------VKCQSPPSISNG---- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 656 rHHPGTFGFNT---TCYFGCNAGFTLIGDSTLSCRpSGQWTAvTPACRAVKCSElhvnkPIAMN---CSNLWGNFSYGSI 729
Cdd:PHA02927 158 -RHNGYEDFYTdgsVVTYSCNSGYSLIGNSGVLCS-GGEWSD-PPTCQIVKCPH-----PTISNgylSSGFKRSYSYNDN 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157419154 730 CSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:PHA02927 230 VDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
168-195 4.33e-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: 38.39  E-value: 4.33e-04
                         10        20
                 ....*....|....*....|....*...
gi 157419154 168 CSKQGECLETIGNYTCSCYPGFYGPECE 195
Cdd:cd00054   11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
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 ...
42-160 1.31e-56

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: 189.51  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157419154 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
50-160 9.59e-29

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.65  E-value: 9.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154   50 AYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGI--RKNNKTWTWVGTKkalTNEAENWADnEPNNKRN 127
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWAP-EPNNNGE 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 157419154  128 NEDCVEIYIKSpsapGKWNDEHCLKKKHALCYT 160
Cdd:pfam00059  77 NEDCVELSSSS----GKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
42-158 7.43e-20

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: 86.11  E-value: 7.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154    42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYY--SSYYWIGIR--KNNKTWTWVGTKKALTNeaENW 117
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgsSDYYWIGLSdpDSNGSWQWSDGSGPVSY--SNW 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 157419154   118 ADNEPNNkrNNEDCVEIYIKSpsapGKWNDEHCLKKKHALC 158
Cdd:smart00034  89 APGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123
PHA02927 PHA02927
secreted complement-binding protein; Provisional
219-443 2.52e-18

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 85.86  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 219 NFSFNSQCSFHCTDGY--QVNGPSKLECLASGiWTnKPPQCLAAQCPPLKIPERGNMtclhSAKAFQHQSSCSFSCEEGF 296
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYrkQKMGPIYAKCTGTG-WT-LFNQCIKRRCPSPRDIDNGQL----DIGGVDFGSSITYSCNSGY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 297 ALVGPEVVQC----TASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLtaFAYGSSCKFECQPGYRVRGLDMLRCiDSG 372
Cdd:PHA02927 117 QLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGG 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419154 373 HWSAPlPTCEAISCePLESPVHGSMDcSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:PHA02927 194 EWSDP-PTCQIVKC-PHPTISNGYLS-SGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
342-567 1.37e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.77  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419154 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
505-761 1.07e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.07  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 505 CQAIPCTPL-LSPQNGtmtcVQPLGSSSYK--STCQFICDEGYSLS--GPERLDCTRSGrWTDSPpMCEAIKCPELFAPE 579
Cdd:PHA02927  20 CCTIPSRPInMKFKNS----VETDANANYNigDTIEYLCLPGYRKQkmGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDID 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 580 QGSLDCsdtrGEFNVGSTCHFSCDNGFKLEGPNNVEC----TTSGRWSATPPTCKGiaslptpgVQCPALTTPGQGtmyc 655
Cdd:PHA02927  94 NGQLDI----GGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICES--------VKCQSPPSISNG---- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 656 rHHPGTFGFNT---TCYFGCNAGFTLIGDSTLSCRpSGQWTAvTPACRAVKCSElhvnkPIAMN---CSNLWGNFSYGSI 729
Cdd:PHA02927 158 -RHNGYEDFYTdgsVVTYSCNSGYSLIGNSGVLCS-GGEWSD-PPTCQIVKCPH-----PTISNgylSSGFKRSYSYNDN 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157419154 730 CSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:PHA02927 230 VDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
572-630 2.53e-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: 65.18  E-value: 2.53e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 572 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCK 630
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
262-320 1.67e-12

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: 62.87  E-value: 1.67e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCK 320
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
510-568 6.42e-12

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: 60.94  E-value: 6.42e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCE 568
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
572-629 5.50e-11

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: 58.31  E-value: 5.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   572 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:smart00032   1 CPPPPDIENGTVTSS--SGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
572-629 4.29e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.97  E-value: 4.29e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  572 CPELFAPEQGSLDCsdTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
262-319 1.40e-09

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: 54.45  E-value: 1.40e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:smart00032   1 CPPPPDIENGTVTS--SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
510-567 2.03e-09

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: 54.07  E-value: 2.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
262-319 2.67e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 53.66  E-value: 2.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  262 CPPLKIPERGNMTCLHSAkaFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
448-505 4.48e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.19  E-value: 4.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  448 CQDLPVPNEARVncSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPEC 505
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
168-195 4.33e-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: 38.39  E-value: 4.33e-04
                         10        20
                 ....*....|....*....|....*...
gi 157419154 168 CSKQGECLETIGNYTCSCYPGFYGPECE 195
Cdd:cd00054   11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
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 ...
42-160 1.31e-56

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: 189.51  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157419154 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
50-160 9.59e-29

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.65  E-value: 9.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154   50 AYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGI--RKNNKTWTWVGTKkalTNEAENWADnEPNNKRN 127
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWAP-EPNNNGE 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 157419154  128 NEDCVEIYIKSpsapGKWNDEHCLKKKHALCYT 160
Cdd:pfam00059  77 NEDCVELSSSS----GKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
42-159 6.33e-21

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: 88.83  E-value: 6.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYL-NKVLPYYSSYYWIGIRKN--NKTWTWVGTKKALTNeaENWA 118
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLaSLLKKSSSSDVWIGLNDLssEGTWKWSDGSPLVDY--TNWA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157419154 119 DNEPNNKrNNEDCVEIYIkspSAPGKWNDEHCLKKKHALCY 159
Cdd:cd00037   79 PGEPNPG-GSEDCVVLSS---SSDGKWNDVSCSSKLPFICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
42-158 7.43e-20

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: 86.11  E-value: 7.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154    42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYY--SSYYWIGIR--KNNKTWTWVGTKKALTNeaENW 117
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgsSDYYWIGLSdpDSNGSWQWSDGSGPVSY--SNW 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 157419154   118 ADNEPNNkrNNEDCVEIYIKSpsapGKWNDEHCLKKKHALC 158
Cdd:smart00034  89 APGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
44-158 1.05e-18

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: 82.74  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  44 YHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPyYSSYYWIGIRKNNK--TWTWV-GTKkaLTNEAENWADN 120
Cdd:cd03590   13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEETegEWKWVdGTP--LNSSKTFWHPG 89
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157419154 121 EPNNKR-NNEDCVEIYikspSAPGKWNDEHCLKKKHALC 158
Cdd:cd03590   90 EPNNWGgGGEDCAELV----YDSGGWNDVPCNLEYRWIC 124
PHA02927 PHA02927
secreted complement-binding protein; Provisional
219-443 2.52e-18

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 85.86  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 219 NFSFNSQCSFHCTDGY--QVNGPSKLECLASGiWTnKPPQCLAAQCPPLKIPERGNMtclhSAKAFQHQSSCSFSCEEGF 296
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYrkQKMGPIYAKCTGTG-WT-LFNQCIKRRCPSPRDIDNGQL----DIGGVDFGSSITYSCNSGY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 297 ALVGPEVVQC----TASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLtaFAYGSSCKFECQPGYRVRGLDMLRCiDSG 372
Cdd:PHA02927 117 QLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGG 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419154 373 HWSAPlPTCEAISCePLESPVHGSMDcSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:PHA02927 194 EWSDP-PTCQIVKC-PHPTISNGYLS-SGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
342-567 1.37e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 77.77  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419154 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
505-761 1.07e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.07  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 505 CQAIPCTPL-LSPQNGtmtcVQPLGSSSYK--STCQFICDEGYSLS--GPERLDCTRSGrWTDSPpMCEAIKCPELFAPE 579
Cdd:PHA02927  20 CCTIPSRPInMKFKNS----VETDANANYNigDTIEYLCLPGYRKQkmGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDID 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 580 QGSLDCsdtrGEFNVGSTCHFSCDNGFKLEGPNNVEC----TTSGRWSATPPTCKGiaslptpgVQCPALTTPGQGtmyc 655
Cdd:PHA02927  94 NGQLDI----GGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICES--------VKCQSPPSISNG---- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 656 rHHPGTFGFNT---TCYFGCNAGFTLIGDSTLSCRpSGQWTAvTPACRAVKCSElhvnkPIAMN---CSNLWGNFSYGSI 729
Cdd:PHA02927 158 -RHNGYEDFYTdgsVVTYSCNSGYSLIGNSGVLCS-GGEWSD-PPTCQIVKCPH-----PTISNgylSSGFKRSYSYNDN 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 157419154 730 CSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:PHA02927 230 VDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
43-159 6.07e-14

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: 68.55  E-value: 6.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  43 TYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGtkkALTNEAENWAdneP 122
Cdd:cd03602    2 TFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSD---GSESSFRNWN---T 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157419154 123 NNKRNNEDCVEIYIKspsapGKWNDEHCLKKKHALCY 159
Cdd:cd03602   76 FQPFGQGDCATMYSS-----GRWYAALCSALKPFICY 107
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
572-630 2.53e-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: 65.18  E-value: 2.53e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 572 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCK 630
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
217-381 1.54e-12

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 68.53  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 217 LGNFSFNSQCSFHCTDGYQVNGPSKLEC----LASGIWTNKPPQCLAAQCPplKIPERGNMTCLHSAKAFQHQSSCSFSC 292
Cdd:PHA02927  99 IGGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICESVKCQ--SPPSISNGRHNGYEDFYTDGSVVTYSC 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 293 EEGFALVGPEVVQCTAsGVWTAPaPVCKAVQCQHlEAPSEGTMDCVHPlTAFAYGSSCKFECQPGYRVRGLDMLRCIDSG 372
Cdd:PHA02927 177 NSGYSLIGNSGVLCSG-GEWSDP-PTCQIVKCPH-PTISNGYLSSGFK-RSYSYNDNVDFKCKYGYKLSGSSSSTCSPGN 252

                 ....*....
gi 157419154 373 HWSAPLPTC 381
Cdd:PHA02927 253 TWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
262-320 1.67e-12

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: 62.87  E-value: 1.67e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCK 320
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
510-568 6.42e-12

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: 60.94  E-value: 6.42e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCE 568
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02639 PHA02639
EEV host range protein; Provisional
476-629 6.76e-12

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 67.00  E-value: 6.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 476 FTCNEGLLLVGASVLQCLATGN---WNSVPPECQAIPCTPLLSPQNGTMTCVQPL---GSSSYkstcqFICDE----GYS 545
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKIYNKREMykvGDEIY-----YVCNEhkgvQYS 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 546 LSGPERLDCTRSGRWTDSPPMCEAIKCpELFAPEQGSLDCSDTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSAT 625
Cdd:PHA02639 123 LVGNEKITCIQDKSWKPDPPICKMINC-RFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPS 201

                 ....
gi 157419154 626 PPTC 629
Cdd:PHA02639 202 IPTC 205
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
572-629 5.50e-11

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: 58.31  E-value: 5.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   572 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:smart00032   1 CPPPPDIENGTVTSS--SGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
43-147 8.22e-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: 60.13  E-value: 8.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  43 TYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYsSYYWIGIRKNNKTWTWV---GTKKALTneaeNWAD 119
Cdd:cd03603    2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKwsdGEESTYT----NWGS 76
                         90       100
                 ....*....|....*....|....*....
gi 157419154 120 NEP-NNKRNNEDCVEIYiKSPSAPGKWND 147
Cdd:cd03603   77 GEPhNNGGGNEDYAAIN-HFPGISGKWND 104
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
200-257 8.47e-11

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: 8.47e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154 200 CGELELPQHVLMNCShpLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
448-506 1.12e-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: 57.47  E-value: 1.12e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 448 CQDLPVPNEARVNCShpFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPECQ 506
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
44-158 1.93e-10

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: 58.85  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  44 YHYSTKA-YSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGI--RKNNKTWTWVgTKKALTneAENWADN 120
Cdd:cd03591    3 IFVTNGEeKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGItdLETEGQFVYL-DGGPLT--YTNWKPG 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157419154 121 EPNNKRNNEDCVEIYikspsAPGKWNDEHCLKKKHALC 158
Cdd:cd03591   80 EPNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
324-382 2.41e-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: 56.70  E-value: 2.41e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 324 CQHLEAPSEGTMDCvhPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTCE 382
Cdd:cd00033    1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
Sushi pfam00084
Sushi repeat (SCR repeat);
572-629 4.29e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.97  E-value: 4.29e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  572 CPELFAPEQGSLDCsdTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
228-381 1.20e-09

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 60.45  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 228 FHCTDGYQVNGPSKLECLA---SGIWTNKPPQCLAAQC--PPLKIpergNMTCLHSAKAFQHQSSCSFSCEE----GFAL 298
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECndPPSII----NGKIYNKREMYKVGDEIYYVCNEhkgvQYSL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 299 VGPEVVQCTASGVWTAPAPVCKAVQCQhLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPL 378
Cdd:PHA02639 124 VGNEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSI 202

                 ...
gi 157419154 379 PTC 381
Cdd:PHA02639 203 PTC 205
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
386-444 1.22e-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: 54.78  E-value: 1.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 386 CEPLESPVHGSMDCSPSLraFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQ 444
Cdd:cd00033    1 CPPPPVPENGTVTGSKGS--YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
262-319 1.40e-09

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: 54.45  E-value: 1.40e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:smart00032   1 CPPPPDIENGTVTS--SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
642-700 1.69e-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: 54.39  E-value: 1.69e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 642 CPALTTPGQGTMYCRHhpGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACR 700
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
510-567 2.03e-09

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: 54.07  E-value: 2.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
262-319 2.67e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 53.66  E-value: 2.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  262 CPPLKIPERGNMTCLHSAkaFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
324-381 7.19e-09

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: 52.53  E-value: 7.19e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   324 CQHLEAPSEGTMDCVHPLtaFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTC 381
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
704-762 9.94e-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: 52.08  E-value: 9.94e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 704 CSELHVNKPIAMNCSNlwGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQ 762
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
200-257 1.12e-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: 51.76  E-value: 1.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   200 CGELELPQHVLMNCSHplGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
58-158 1.24e-08

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: 53.69  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  58 KYCQNRYTDLVAIQNKN-EIDYL---NKVLPYYSsyYWIGI---RKNNKTWTWvGTKKALTNEAENWADNEPNNKRNNED 130
Cdd:cd03601   17 AFCRSRGMRLASLAMRDsEMRDAilaFTLVKGHG--YWVGAdnlQDGEYDFLW-NDGVSLPTDSDLWAPNEPSNPQSRQL 93
                         90       100
                 ....*....|....*....|....*...
gi 157419154 131 CVEIYIKspsaPGKWNDEHCLKKKHALC 158
Cdd:cd03601   94 CVQLWSK----YNLLDDEYCGRAKRVIC 117
PHA02639 PHA02639
EEV host range protein; Provisional
290-443 2.12e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 56.60  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 290 FSCEEGFALVGPEVVQCTA---SGVWTAPAPVCKAVQCQhlEAPSEGTMDCVHPLTAFAYGSSCKFECQP----GYRVRG 362
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECN--DPPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSLVG 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 363 LDMLRCIDSGHWSAPLPTCEAISCEpLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPV 442
Cdd:PHA02639 126 NEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPT 204

                 .
gi 157419154 443 C 443
Cdd:PHA02639 205 C 205
Sushi pfam00084
Sushi repeat (SCR repeat);
200-257 2.24e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.96  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  200 CGELELPQHvlMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:pfam00084   1 CPPPPDIPN--GKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
386-443 2.40e-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: 50.99  E-value: 2.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   386 CEPLESPVHGSMDCSPSLraFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
448-505 3.22e-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: 50.60  E-value: 3.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   448 CQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPEC 505
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02639 PHA02639
EEV host range protein; Provisional
537-720 4.48e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 55.44  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 537 QFICDEGYSLSGPERLDCTR---SGRWTDSPPMCEAIKCPELFAPEQGSLdcSDTRGEFNVGSTCHFSCDN----GFKLE 609
Cdd:PHA02639  47 EYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECNDPPSIINGKI--YNKREMYKVGDEIYYVCNEhkgvQYSLV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 610 GPNNVECTTSGRWSATPPTCKGIaslptpGVQCPALTtpgQGTMYCRHHPGTFGFNTTCYFGCNAGFTLIGDSTLSCRPS 689
Cdd:PHA02639 125 GNEKITCIQDKSWKPDPPICKMI------NCRFPALQ---NGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNIN 195
                        170       180       190
                 ....*....|....*....|....*....|..
gi 157419154 690 GQWTAVTPAC-RAVKCSELHVNKPIAMNCSNL 720
Cdd:PHA02639 196 ATWFPSIPTCvRNKPIDDIIYLKPVDDNFDDL 227
Sushi pfam00084
Sushi repeat (SCR repeat);
448-505 4.48e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.19  E-value: 4.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  448 CQDLPVPNEARVncSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPEC 505
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
44-158 8.77e-08

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: 51.18  E-value: 8.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  44 YHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLpyYSSYYWIGIRKN--NKTWTWVGTKKALtneaeNWADNE 121
Cdd:cd03593   13 YYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQI--GSSSYWIGLSREksEKPWKWIDGSPLN-----NLFNIR 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157419154 122 PNNKRNNedCVeiYIKSpsapGKWNDEHCLKKKHALC 158
Cdd:cd03593   86 GSTKSGN--CA--YLSS----TGIYSEDCSTKKRWIC 114
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
642-699 1.36e-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: 48.68  E-value: 1.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   642 CPALTTPGQGTMYCRHhpGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPAC 699
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
704-761 5.57e-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: 5.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154   704 CSELHVNKPIAMNCSNlwGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
339-381 1.06e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 46.34  E-value: 1.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 157419154  339 HPLTAFAYGSSCKFECQPGYRVRGLDMLRCIDSGHWSAPLPTC 381
Cdd:pfam00084  14 ATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
226-319 1.25e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 51.20  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 226 CSFHCTDGYQVNGPSKLECLASGIWTNKPPQCLAAQC--PPLkipERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEV 303
Cdd:PHA02639 113 CNEHKGVQYSLVGNEKITCIQDKSWKPDPPICKMINCrfPAL---QNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKY 189
                         90
                 ....*....|....*.
gi 157419154 304 VQCTASGVWTAPAPVC 319
Cdd:PHA02639 190 STCNINATWFPSIPTC 205
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
52-158 1.25e-06

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: 48.51  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  52 SWNISRKYCQN-----RYTDLVAIQNKNEIDYlnkVLPYYSS------YY--WIGI--RKNNKTWTWV-GTkkalTNEAE 115
Cdd:cd03589   21 TWEEAELRCRSfsipgLIAHLVSIHSQEENDF---VYDLFESsrgpdtPYglWIGLhdRTSEGPFEWTdGS----PVDFT 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157419154 116 NWADNEPNNKRNNEDCVEIYiKSPSAPGKWNDEHCLKKKHALC 158
Cdd:cd03589   94 KWAGGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPCDAVFPYIC 135
PHA02817 PHA02817
EEV Host range protein; Provisional
220-319 1.30e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 50.32  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 220 FSFNSQCSFHCTDG-----YQVNGPSKLECLASGIWTNKPPQCLAAQC--PPLkipERGNMTCLHSAKAFQHQSSCSFSC 292
Cdd:PHA02817  42 YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCrfPAL---QNGFVNGIPDSKKFYYESEVSFSC 118
                         90       100
                 ....*....|....*....|....*..
gi 157419154 293 EEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:PHA02817 119 KPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
510-567 1.35e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 45.95  E-value: 1.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  510 CTPLLSPQNGTMTCvqPLGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
534-629 1.53e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 49.94  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 534 STCQFICDEG-----YSLSGPERLDCTRSGRWTDSPPMCEAIKCpELFAPEQGSLDCSDTRGEFNVGSTCHFSCDNGFKL 608
Cdd:PHA02817  46 SNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRC-RFPALQNGFVNGIPDSKKFYYESEVSFSCKPGFVL 124
                         90       100
                 ....*....|....*....|.
gi 157419154 609 EGPNNVECTTSGRWSATPPTC 629
Cdd:PHA02817 125 IGTKYSVCGINSSWIPKVPIC 145
PHA02817 PHA02817
EEV Host range protein; Provisional
342-443 2.25e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 49.55  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 342 TAFAYGSSCKFECQPG-----YRVRGLDMLRCIDSGHWSAPLPTCEAISCEpLESPVHGSMDCSPSLRAFQYDTNCSFRC 416
Cdd:PHA02817  40 TEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSC 118
                         90       100
                 ....*....|....*....|....*..
gi 157419154 417 AEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:PHA02817 119 KPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02817 PHA02817
EEV Host range protein; Provisional
410-505 3.19e-06

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 49.17  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 410 TNCSFRCAEG-----FMLRGADIVRCDNLGQWTAPAPVCQALQCQdLPVPNEARVNCSHPFGAFRYQSVCSFTCNEGLLL 484
Cdd:PHA02817  46 SNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKPGFVL 124
                         90       100
                 ....*....|....*....|.
gi 157419154 485 VGASVLQCLATGNWNSVPPEC 505
Cdd:PHA02817 125 IGTKYSVCGINSSWIPKVPIC 145
PHA02831 PHA02831
EEV host range protein; Provisional
287-381 1.29e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 47.68  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 287 SCSFSCE----EGFALVGPEVVQCTaSGVWTAPAPVCKAVQCQHlEAPSEGTMDCVHplTAFAYGSSCKFECQPGYRVRG 362
Cdd:PHA02831 101 SVTYACKvnklEKYSIVGNETVKCI-NKQWVPKYPVCKLIRCKY-PALQNGFLNVFE--KKFYYGDIVNFKCKKGFILLG 176
                         90
                 ....*....|....*....
gi 157419154 363 LDMLRCIDSGHWSAPLPTC 381
Cdd:PHA02831 177 SSVSTCDINSIWYPGIPKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
286-381 1.48e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 286 SSCSFSCEEG-----FALVGPEVVQCTASGVWTAPAPVCKAVQCQhLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRV 360
Cdd:PHA02817  46 SNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKPGFVL 124
                         90       100
                 ....*....|....*....|.
gi 157419154 361 RGLDMLRCIDSGHWSAPLPTC 381
Cdd:PHA02817 125 IGTKYSVCGINSSWIPKVPIC 145
PHA02817 PHA02817
EEV Host range protein; Provisional
475-567 1.64e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 46.86  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 475 SFTCNEGLL-----LVGASVLQCLATGNWNSVPPECQAIPCT-PLLspQNGTMTCVQPLGSSSYKSTCQFICDEGYSLSG 548
Cdd:PHA02817  49 TFFCGNNTRgvrytLVGEKNIICEKDGKWNKEFPVCKIIRCRfPAL--QNGFVNGIPDSKKFYYESEVSFSCKPGFVLIG 126
                         90
                 ....*....|....*....
gi 157419154 549 PERLDCTRSGRWTDSPPMC 567
Cdd:PHA02817 127 TKYSVCGINSSWIPKVPIC 145
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
44-158 1.72e-05

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: 45.06  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  44 YHYSTKAYSWNISRKYCQNRY--TDLVAIQNKNEIDYLNKVLPYY---SSYYWIGIRKNNKTWTWVGTKKALTNEAeNWA 118
Cdd:cd03594   13 YGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHDPQQSRGWEWSDGSKLDYR-SWD 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157419154 119 DNEPnnKRNNEDCVEiyIKSPSAPGKWNDEHCLKKKHALC 158
Cdd:cd03594   92 RNPP--YARGGYCAE--LSRSTGFLKWNDANCEERNPFIC 127
Sushi pfam00084
Sushi repeat (SCR repeat);
722-761 2.41e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.49  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 157419154  722 GNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:pfam00084  17 NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
599-761 2.90e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 46.52  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 599 HFSCDNGFklegpNNVECT-TSGRWSaTPPTCKGIASLPTPgvqcpalTTPGQGtmYCRHHPGTFGFNTTCYFGCNAG-- 675
Cdd:PHA02831  47 EYKCNNNF-----DKVFVTcNNGSWS-TKNMCIGKRNCKDP-------VTILNG--YIKNKKDQYSFGDSVTYACKVNkl 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 676 --FTLIGDSTLSCrPSGQWTAVTPACRAVKCSELHVNKPIamnCSNLWGNFSYGSICSFHCLEGQLLNGSAQTACQENGH 753
Cdd:PHA02831 112 ekYSIVGNETVKC-INKQWVPKYPVCKLIRCKYPALQNGF---LNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSI 187

                 ....*...
gi 157419154 754 WSTTVPTC 761
Cdd:PHA02831 188 WYPGIPKC 195
PHA02639 PHA02639
EEV host range protein; Provisional
341-505 5.77e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.81  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 341 LTAFAYGSSCKFECQPGYRVRGLDMLRCI---DSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLraFQYDTNCSFRCA 417
Cdd:PHA02639  37 MEKYEIGKLIEYTCNTDYALIGDRFRTCIkdkNNAIWSNKAPFCMLKECNDPPSIINGKIYNKREM--YKVGDEIYYVCN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 418 E----GFMLRGADIVRCDNLGQWTAPAPVCQALQCQdLPVPNEARVNCSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCL 493
Cdd:PHA02639 115 EhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCN 193
                        170
                 ....*....|..
gi 157419154 494 ATGNWNSVPPEC 505
Cdd:PHA02639 194 INATWFPSIPTC 205
PHA02817 PHA02817
EEV Host range protein; Provisional
567-699 5.99e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 45.32  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 567 CEAIKCpeLFAPEQGSLDCSDTRGEFNVGSTCHFSCDNG-----FKLEGPNNVECTTSGRWSATPPTCKGIAslptpgVQ 641
Cdd:PHA02817  19 CDLNKC--CYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIR------CR 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 642 CPALTTPgqgtmYCRHHPGT--FGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPAC 699
Cdd:PHA02817  91 FPALQNG-----FVNGIPDSkkFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
386-443 8.41e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.95  E-value: 8.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  386 CEPLESPVHGSMdcSPSLRAFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 443
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
591-761 1.93e-04

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 44.27  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 591 EFNVGSTCHFSCDNGFKLEGPNNVEC---TTSGRWSATPPTCKGIASLPTPGVQcpalttpgQGTMYCRHHpgTFGFNTT 667
Cdd:PHA02639  39 KYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSII--------NGKIYNKRE--MYKVGDE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 668 CYFGCN----AGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHV-NKPIAMNCSNlwGNFSYGSICSFHCLEGQLLNG 742
Cdd:PHA02639 109 IYYVCNehkgVQYSLVGNEKITCIQDKSWKPDPPICKMINCRFPALqNGYINGIPSN--KKFYYKTRVGFSCKSGFDLVG 186
                        170
                 ....*....|....*....
gi 157419154 743 SAQTACQENGHWSTTVPTC 761
Cdd:PHA02639 187 EKYSTCNINATWFPSIPTC 205
PHA02817 PHA02817
EEV Host range protein; Provisional
651-761 1.93e-04

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 43.78  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 651 GTMYCRHHPGTFGFNTTCYFGCNA---GFTLIGDSTLSCRPSGQWTAVTPACRAVKC-----SELHVNKpIAMNcsnlwG 722
Cdd:PHA02817  33 GYIYNKKTEYNIGSNVTFFCGNNTrgvRYTLVGEKNIICEKDGKWNKEFPVCKIIRCrfpalQNGFVNG-IPDS-----K 106
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157419154 723 NFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTC 761
Cdd:PHA02817 107 KFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
642-699 1.98e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.79  E-value: 1.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419154  642 CPALTTPGQGTMYCRHhpGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPAC 699
Cdd:pfam00084   1 CPPPPDIPNGKVSATK--NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
542-629 2.59e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 43.83  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 542 EGYSLSGPERLDCTrSGRWTDSPPMCEAIKCpELFAPEQGSLDCSDTRgeFNVGSTCHFSCDNGFKLEGPNNVECTTSGR 621
Cdd:PHA02831 112 EKYSIVGNETVKCI-NKQWVPKYPVCKLIRC-KYPALQNGFLNVFEKK--FYYGDIVNFKCKKGFILLGSSVSTCDINSI 187

                 ....*...
gi 157419154 622 WSATPPTC 629
Cdd:PHA02831 188 WYPGIPKC 195
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
267-505 3.88e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.54  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 267 IPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAY 346
Cdd:PHA02954  23 VPTMNNAKLTSTETSFNDKQKVTFTCDSGYYSLDPNAVCETDKWKYENPCKKMCTVSDYVSELYDKPLYEVNSTITLICK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 347 GSSCKFECQPGYrvrgldmlrciDSGHWSAPLpTCEAISCEPLESPvHGSmdCSPSLRAFQYDTNCSFRCAEGFMLRGAD 426
Cdd:PHA02954 103 DETKYFRCEEKN-----------GNTSWNDTV-TCPNAECQPLQLE-HGS--CQPVKEKYSFGEHITINCDVGYEVIGAS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157419154 427 IVRCdNLGQWTApAPVCQalQCQDLPVPNEARVNCShpfgAFRYQSVCSFTCNEGLLLVGASVLQCLaTGNWNSVPPEC 505
Cdd:PHA02954 168 YISC-TANSWNV-IPSCQ--QKCDIPSLSNGLISGS----TFSIGGVIHLSCKSGFTLTGSPSSTCI-DGKWNPVLPIC 237
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
168-195 4.33e-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: 38.39  E-value: 4.33e-04
                         10        20
                 ....*....|....*....|....*...
gi 157419154 168 CSKQGECLETIGNYTCSCYPGFYGPECE 195
Cdd:cd00054   11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02831 PHA02831
EEV host range protein; Provisional
412-505 9.27e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 41.90  E-value: 9.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 412 CSFRCAEGFMLRGADIVRCDNlGQWTAPAPVCQALQCQdLPVPNEARVNCSHPfgAFRYQSVCSFTCNEGLLLVGASVLQ 491
Cdd:PHA02831 106 CKVNKLEKYSIVGNETVKCIN-KQWVPKYPVCKLIRCK-YPALQNGFLNVFEK--KFYYGDIVNFKCKKGFILLGSSVST 181
                         90
                 ....*....|....
gi 157419154 492 CLATGNWNSVPPEC 505
Cdd:PHA02831 182 CDINSIWYPGIPKC 195
PHA02831 PHA02831
EEV host range protein; Provisional
344-455 9.96e-04

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 41.90  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 344 FAYGSSCKFECQPG----YRVRGLDMLRCIDsGHWSAPLPTCEAISCE--PLESPVHGSMDcspslRAFQYDTNCSFRCA 417
Cdd:PHA02831  96 YSFGDSVTYACKVNklekYSIVGNETVKCIN-KQWVPKYPVCKLIRCKypALQNGFLNVFE-----KKFYYGDIVNFKCK 169
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157419154 418 EGFMLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPN 455
Cdd:PHA02831 170 KGFILLGSSVSTCDINSIWYPGIPKCVKDKVHNEIQPN 207
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
44-150 6.36e-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: 37.56  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154  44 YHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKvlpYYSSYYWIGIR----KNNKTWTwvgtkKALTNEAENWAD 119
Cdd:cd03588   13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNN---NAQDYQWIGLNdrtiEGDFRWS-----DGHPLQFENWRP 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 157419154 120 NEPNNK-RNNEDCVeIYIKSPSapGKWNDEHC 150
Cdd:cd03588   85 NQPDNFfATGEDCV-VMIWHEE--GEWNDVPC 113
PHA02831 PHA02831
EEV host range protein; Provisional
220-319 7.50e-03

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 39.21  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419154 220 FSFNSQCSFHCT----DGYQVNGPSKLECLaSGIWTNKPPQCLAAQCpplKIPERGNMTCLHSAKAFQHQSSCSFSCEEG 295
Cdd:PHA02831  96 YSFGDSVTYACKvnklEKYSIVGNETVKCI-NKQWVPKYPVCKLIRC---KYPALQNGFLNVFEKKFYYGDIVNFKCKKG 171
                         90       100
                 ....*....|....*....|....
gi 157419154 296 FALVGPEVVQCTASGVWTAPAPVC 319
Cdd:PHA02831 172 FILLGSSVSTCDINSIWYPGIPKC 195
 
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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