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Conserved domains on  [gi|266458|sp|Q00690|]
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RecName: Full=E-selectin; AltName: Full=CD62 antigen-like family member E; AltName: Full=Endothelial leukocyte adhesion molecule 1; Short=ELAM-1; AltName: Full=Leukocyte-endothelial cell adhesion molecule 2; Short=LECAM2; AltName: CD_antigen=CD62E; Flags: Precursor

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 12933816)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

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 ...
 22-140 3.42e-53

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: 177.57  E-value: 3.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSN-LKHSPSYYWIGIRKVNNVWIWVGTGKPLtEEAQNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 266458   101 EPNNKqRNEDCVEIYIqrtKDSGMWNDERCNKKKLALCYT 140
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 262-489 1.81e-17

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 82.78  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    262 SYPWNTTCTFDCVEGYRR--VGAQNLQCTSSGiWdNETPSCKAVTCdaiPQPQNgfVSCSHSTAGELAFKSSCNFTCEQS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-W-TLFNQCIKRRC---PSPRD--IDNGQLDIGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    340 FTLQGPAQVEC----SAQGQWTPQIPVCKAVQCEALSAPQQGNMKclpSASGPFQNGSSCEFSCEEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHN---GYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266458    416 rGEWdSKKPTCSAVKCDDvPRPQNGVMECAHATTgeFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPH-PTISNGYLSSGFKRS--YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 494-549 3.80e-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: 55.55  E-value: 3.80e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 266458   494 CPSLDVPGKMNMSCS-GTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTCE 549
Cdd:cd00033   1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 180-238 2.63e-08

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


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 50.54  E-value: 2.63e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458   180 CKPQEHPDYGSLNCShpFGPFSYNSSCSFGCKRGYLPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-175 6.73e-06

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


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 6.73e-06
                        10        20
                ....*....|....*....|....*...
gi 266458   148 CSGHGECIETINSYTCKCHPGFLGPNCE 175
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 ...
 22-140 3.42e-53

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: 177.57  E-value: 3.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSN-LKHSPSYYWIGIRKVNNVWIWVGTGKPLtEEAQNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 266458   101 EPNNKqRNEDCVEIYIqrtKDSGMWNDERCNKKKLALCYT 140
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 31-140 4.90e-28

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 108.33  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458      31 MTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYYWIGI--RKVNNVWIWVGTGKPLTEeaqNWAPgEPNNKQRN 108
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGSPVNYT---NWAP-EPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 266458     109 EDCVEIYiqrtKDSGMWNDERCNKKKLALCYT 140
Cdd:pfam00059  78 EDCVELS----SSSGKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 22-138 6.95e-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: 85.73  E-value: 6.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458       22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLK--HSPSYYWIGIR--KVNNVWIWVGTGKPLTeeAQNW 97
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 266458       98 APGEPNNkqRNEDCVEIYiqrtKDSGMWNDERCNKKKLALC 138
Cdd:smart00034  89 APGEPNN--SSGDCVVLS----TSGGKWNDVSCTSKLPFVC 123
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 262-489 1.81e-17

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 82.78  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    262 SYPWNTTCTFDCVEGYRR--VGAQNLQCTSSGiWdNETPSCKAVTCdaiPQPQNgfVSCSHSTAGELAFKSSCNFTCEQS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-W-TLFNQCIKRRC---PSPRD--IDNGQLDIGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    340 FTLQGPAQVEC----SAQGQWTPQIPVCKAVQCEALSAPQQGNMKclpSASGPFQNGSSCEFSCEEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHN---GYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266458    416 rGEWdSKKPTCSAVKCDDvPRPQNGVMECAHATTgeFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPH-PTISNGYLSSGFKRS--YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 431-490 2.65e-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: 61.71  E-value: 2.65e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458   431 CDDVPRPQNGVMECahaTTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSCQ 490
Cdd:cd00033   1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 494-549 3.80e-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: 55.55  E-value: 3.80e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 266458   494 CPSLDVPGKMNMSCS-GTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTCE 549
Cdd:cd00033   1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 431-489 1.29e-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: 1.29e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      431 CDDVPRPQNGVMECahaTTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:smart00032   1 CPPPPDIENGTVTS---SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
431-489 2.10e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 2.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458     431 CDDVPRPQNGVmecAHATTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:pfam00084   1 CPPPPDIPNGK---VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 180-238 2.63e-08

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 50.54  E-value: 2.63e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458   180 CKPQEHPDYGSLNCShpFGPFSYNSSCSFGCKRGYLPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 494-548 3.17e-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: 47.52  E-value: 3.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 266458      494 CPSLDVPGKMNMSCS-GTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:smart00032   1 CPPPPDIENGTVTSSsGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 180-238 1.65e-06

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: 45.60  E-value: 1.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      180 CKPQEHPDYGSLNCSHpfGPFSYNSSCSFGCKRGYLPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIG-SSTITCLENGTWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-175 6.73e-06

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 6.73e-06
                        10        20
                ....*....|....*....|....*...
gi 266458   148 CSGHGECIETINSYTCKCHPGFLGPNCE 175
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Sushi pfam00084
Sushi repeat (SCR repeat);
180-238 1.27e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.87  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458     180 CKPQEHPDYGSLncSHPFGPFSYNSSCSFGCKRGYLPSSMETTVrCTSSGEWSAPAPAC 238
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTIT-CQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
494-548 2.75e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.02  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 266458     494 CPslDVPGKMNMSCSGTA---VFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:pfam00084   1 CP--PPPDIPNGKVSATKneyNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
148-175 7.13e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 7.13e-04
                           10        20
                   ....*....|....*....|....*....
gi 266458      148 CSGHGECIETINSYTCKCHPGF-LGPNCE 175
Cdd:smart00179  11 CQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
DUF3844 pfam12955
Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It ...
 138-167 5.21e-03

Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It contains 8 largely conserved cysteine residues. This domain is found in proteins that are thought to be found in the endoplasmic reticulum.


Pssm-ID: 432898  Cd Length: 104  Bit Score: 36.82  E-value: 5.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 266458     138 CYT--ASCTNA--SCSGHGECIETINS------YTCKCHP 167
Cdd:pfam12955   1 CFTseDACENAtnNCSGHGECVKKYKSksgrdcFACKCKA 40
 
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 ...
 22-140 3.42e-53

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: 177.57  E-value: 3.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSN-LKHSPSYYWIGIRKVNNVWIWVGTGKPLtEEAQNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 266458   101 EPNNKqRNEDCVEIYIqrtKDSGMWNDERCNKKKLALCYT 140
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 31-140 4.90e-28

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 108.33  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458      31 MTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYYWIGI--RKVNNVWIWVGTGKPLTEeaqNWAPgEPNNKQRN 108
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGSPVNYT---NWAP-EPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 266458     109 EDCVEIYiqrtKDSGMWNDERCNKKKLALCYT 140
Cdd:pfam00059  78 EDCVELS----SSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 22-139 8.63e-23

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: 93.84  E-value: 8.63e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLK-HSPSYYWIGIRKV--NNVWIWVGTGKPLTeeAQNWA 98
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLssEGTWKWSDGSPLVD--YTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 266458    99 PGEPNNkQRNEDCVEIYiqrTKDSGMWNDERCNKKKLALCY 139
Cdd:cd00037  79 PGEPNP-GGSEDCVVLS---SSSDGKWNDVSCSSKLPFICE 115
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 22-138 4.27e-22

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: 91.98  E-value: 4.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    22 WYYnASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKhSPSYYWIGI--RKVNNVWIWVgTGKPLTEEAQNWAP 99
Cdd:cd03590  12 CYF-FSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLsdEETEGEWKWV-DGTPLNSSKTFWHP 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 266458   100 GEPNNKQ-RNEDCVEIyiqrTKDSGMWNDERCNKKKLALC 138
Cdd:cd03590  89 GEPNNWGgGGEDCAEL----VYDSGGWNDVPCNLEYRWIC 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 22-138 6.95e-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: 85.73  E-value: 6.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458       22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLK--HSPSYYWIGIR--KVNNVWIWVGTGKPLTeeAQNW 97
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnsGSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 266458       98 APGEPNNkqRNEDCVEIYiqrtKDSGMWNDERCNKKKLALC 138
Cdd:smart00034  89 APGEPNN--SSGDCVVLS----TSGGKWNDVSCTSKLPFVC 123
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 23-138 1.75e-18

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: 81.19  E-value: 1.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYYWIGI--RKVNNVWIWVgTGKPLTeeAQNWAPG 100
Cdd:cd03591   3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGItdLETEGQFVYL-DGGPLT--YTNWKPG 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 266458   101 EPNNKQRNEDCVEIYiqrtkDSGMWNDERCNKKKLALC 138
Cdd:cd03591  80 EPNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 262-489 1.81e-17

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 82.78  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    262 SYPWNTTCTFDCVEGYRR--VGAQNLQCTSSGiWdNETPSCKAVTCdaiPQPQNgfVSCSHSTAGELAFKSSCNFTCEQS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-W-TLFNQCIKRRC---PSPRD--IDNGQLDIGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    340 FTLQGPAQVEC----SAQGQWTPQIPVCKAVQCEALSAPQQGNMKclpSASGPFQNGSSCEFSCEEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHN---GYEDFYTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266458    416 rGEWdSKKPTCSAVKCDDvPRPQNGVMECAHATTgeFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPH-PTISNGYLSSGFKRS--YSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 344-548 2.38e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 76.23  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    344 GPAQVECSAQGqWTpQIPVCKAVQCEALSAPQQGNMKClpsasGPFQNGSSCEFSCEEGFELKGSRRLQC--GPRGE--W 419
Cdd:PHA02927  64 GPIYAKCTGTG-WT-LFNQCIKRRCPSPRDIDNGQLDI-----GGVDFGSSITYSCNSGYQLIGESKSYCelGSTGSmvW 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    420 DSKKPTCSAVKCDDVPRPQNGvmecAHATTGEF-TYKSSCAFQCNEGFSLHGSAQLECtSQGKWTqEVPSCQVVQCPSLD 498
Cdd:PHA02927 137 NPEAPICESVKCQSPPSISNG----RHNGYEDFyTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWS-DPPTCQIVKCPHPT 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 266458    499 VP-GKMNMSCSGTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:PHA02927 211 ISnGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 28-139 2.26e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 66.63  E-value: 2.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    28 SELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYYWIGIRKVNNVWIWVGTGkplTEEAQNWAPGEPnnkQR 107
Cdd:cd03602   7 NESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGS---ESSFRNWNTFQP---FG 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 266458   108 NEDCVEIYIqrtkdSGMWNDERCNKKKLALCY 139
Cdd:cd03602  81 QGDCATMYS-----SGRWYAALCSALKPFICY 107
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 431-490 2.65e-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: 61.71  E-value: 2.65e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458   431 CDDVPRPQNGVMECahaTTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSCQ 490
Cdd:cd00033   1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 27-138 5.50e-12

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: 62.94  E-value: 5.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    27 SSELMTYDEASAYCQRDYTHLVAIQNKE-EINYLNSNLKHSPSY-YWIGIRKVNNV---WIWvGTGKPLTEEAQNWAPGE 101
Cdd:cd03601   6 SDETMNYAKAGAFCRSRGMRLASLAMRDsEMRDAILAFTLVKGHgYWVGADNLQDGeydFLW-NDGVSLPTDSDLWAPNE 84

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 266458   102 PNNKQRNEDCVEIYIQRtkdsGMWNDERCNKKKLALC 138
Cdd:cd03601  85 PSNPQSRQLCVQLWSKY----NLLDDEYCGRAKRVIC 117
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 28-133 7.36e-12

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: 63.15  E-value: 7.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    28 SELMTYDEASAYCqRDYT------HLVAIQNKEEINYL-----NSNLKHSPSYYWIGI--RKVNNVWIWV-GTGKPLTee 93
Cdd:cd03589  17 GDRLTWEEAELRC-RSFSipgliaHLVSIHSQEENDFVydlfeSSRGPDTPYGLWIGLhdRTSEGPFEWTdGSPVDFT-- 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 266458    94 aqNWAPGEPNNKQRNEDCVEIYiQRTKDSGMWNDERCNKK 133
Cdd:cd03589  94 --KWAGGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPCDAV 130
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 243-301 9.71e-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: 60.17  E-value: 9.71e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458   243 CEALTHPAHGIRKCSSnpGSYPWNTTCTFDCVEGYRRVGAQNLQCTSSGIWDNETPSCK 301
Cdd:cd00033   1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 198-363 1.17e-11

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 65.44  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    198 GPFSYNSSCSFGCKRGY-LPSSMETTVRCTSSGE--WSAPAPACHVVECEALTHPAHGIRKCSSNpgSYPWNTTCTFDCV 274
Cdd:PHA02927 100 GGVDFGSSITYSCNSGYqLIGESKSYCELGSTGSmvWNPEAPICESVKCQSPPSISNGRHNGYED--FYTDGSVVTYSCN 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    275 EGYRRVGAQNLQCtSSGIWDNeTPSCKAVTCDAiPQPQNGFVSCSHSTAgeLAFKSSCNFTCEQSFTLQGPAQVECSAQG 354
Cdd:PHA02927 178 SGYSLIGNSGVLC-SGGEWSD-PPTCQIVKCPH-PTISNGYLSSGFKRS--YSYNDNVDFKCKYGYKLSGSSSSTCSPGN 252


                 ....*....
gi 266458    355 QWTPQIPVC 363
Cdd:PHA02927 253 TWQPELPKC 261
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 23-127 1.73e-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: 61.67  E-value: 1.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSpSYYWIGIRKVNNVWIWV-GTGKPLTeeAQNWAPGE 101
Cdd:cd03603   2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKwSDGEEST--YTNWGSGE 78

                        90       100
                ....*....|....*....|....*..
gi 266458   102 P-NNKQRNEDCVEIYiQRTKDSGMWND 127
Cdd:cd03603  79 PhNNGGGNEDYAAIN-HFPGISGKWND 104
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 305-364 6.60e-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: 6.60e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458   305 CDAIPQPQNGFVSCSHstaGELAFKSSCNFTCEQSFTLQGPAQVECSAQGQWTPQIPVCK 364
Cdd:cd00033   1 CPPPPVPENGTVTGSK---GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 368-426 1.79e-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: 1.79e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458   368 CEALSAPQQGNMKClpsASGPFQNGSSCEFSCEEGFELKGSRRLQCGPRGEWDSKKPTC 426
Cdd:cd00033   1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 299-427 2.93e-10

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 60.72  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    299 SCKAVTCDAIPQPQNGFVscsHSTAGELAFKSSCNFTCEQS-----FTLQGPAQVECSAQGQWTPQIPVCKAVQCEaLSA 373
Cdd:PHA02817  18 LCDLNKCCYPPSIKNGYI---YNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 266458    374 PQQGNMKCLPSaSGPFQNGSSCEFSCEEGFELKGSRRLQCGPRGEWDSKKPTCS 427
Cdd:PHA02817  94 LQNGFVNGIPD-SKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPICS 146
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 494-549 3.80e-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: 55.55  E-value: 3.80e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 266458   494 CPSLDVPGKMNMSCS-GTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTCE 549
Cdd:cd00033   1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02817 PHA02817
EEV Host range protein; Provisional
 277-363 5.29e-10

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 59.95  E-value: 5.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    277 YRRVGAQNLQCTSSGIWDNETPSCKAVTCdAIPQPQNGFVSCSHSTAgELAFKSSCNFTCEQSFTLQGPAQVECSAQGQW 356
Cdd:PHA02817  61 YTLVGEKNIICEKDGKWNKEFPVCKIIRC-RFPALQNGFVNGIPDSK-KFYYESEVSFSCKPGFVLIGTKYSVCGINSSW 138


                 ....*..
gi 266458    357 TPQIPVC 363
Cdd:PHA02817 139 IPKVPIC 145
PHA02639 PHA02639
EEV host range protein; Provisional
 221-363 8.02e-10

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 60.45  E-value: 8.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    221 TTVRCTSSGEWSAPAPACHVVECEALTHPAHGirKCSSNPGSYPWNTTCTFDCVE----GYRRVGAQNLQCTSSGIWDNE 296
Cdd:PHA02639  63 TCIKDKNNAIWSNKAPFCMLKECNDPPSIING--KIYNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPD 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266458    297 TPSCKAVTCdAIPQPQNGFVSCSHSTAgELAFKSSCNFTCEQSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:PHA02639 141 PPICKMINC-RFPALQNGYINGIPSNK-KFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 431-489 1.29e-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: 1.29e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      431 CDDVPRPQNGVMECahaTTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:smart00032   1 CPPPPDIENGTVTS---SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 243-300 4.93e-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: 4.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 266458      243 CEALTHPAHGIRKCSSNPgsYPWNTTCTFDCVEGYRRVGAQNLQCTSSGIWDNETPSC 300
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 305-363 6.23e-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: 52.14  E-value: 6.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      305 CDAIPQPQNGFVSCSHSTageLAFKSSCNFTCEQSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT---YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 389-548 1.18e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 56.60  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    389 FQNGSSCEFSCEEGFELKGSRRLQC---GPRGEWDSKKPTCSAVKCDDVPRPQNGVMecaHATTGEFTYKSSCAFQCNE- 464
Cdd:PHA02639  40 YEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKI---YNKREMYKVGDEIYYVCNEh 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    465 ---GFSLHGSAQLECTSQGKWTQEVPSCQVVQC--PSLDVPGKMNMSCSGTAVFGTVCEFTCPDDWTLNGSAVLTCGATG 539
Cdd:PHA02639 117 kgvQYSLVGNEKITCIQDKSWKPDPPICKMINCrfPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINA 196


                 ....*....
gi 266458    540 RWSGMPPTC 548
Cdd:PHA02639 197 TWFPSIPTC 205
PHA02639 PHA02639
EEV host range protein; Provisional
 301-489 1.47e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 56.60  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    301 KAVTCDAIPQPQNGFVScshSTAGELAFKSSCNFTCEQSFTLQGPAQVEC---SAQGQWTPQIPVCKAVQCEalSAPQQG 377
Cdd:PHA02639  18 KSIYCDKPDDISNGFIT---ELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECN--DPPSII 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    378 NMKcLPSASGPFQNGSSCEFSCEE----GFELKGSRRLQCGPRGEWDSKKPTCSAVKCDdVPRPQNGVMEcAHATTGEFT 453
Cdd:PHA02639  93 NGK-IYNKREMYKVGDEIYYVCNEhkgvQYSLVGNEKITCIQDKSWKPDPPICKMINCR-FPALQNGYIN-GIPSNKKFY 169

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 266458    454 YKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02639 170 YKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205
Sushi pfam00084
Sushi repeat (SCR repeat);
431-489 2.10e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 2.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458     431 CDDVPRPQNGVmecAHATTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:pfam00084   1 CPPPPDIPNGK---VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 180-238 2.63e-08

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 50.54  E-value: 2.63e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458   180 CKPQEHPDYGSLNCShpFGPFSYNSSCSFGCKRGYLPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
305-363 3.23e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.19  E-value: 3.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458     305 CDAIPQPQNGFVSCshsTAGELAFKSSCNFTCEQSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:pfam00084   1 CPPPPDIPNGKVSA---TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 368-426 3.89e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 49.83  E-value: 3.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      368 CEALSAPQQGNMKClpsASGPFQNGSSCEFSCEEGFELKGSRRLQCGPRGEWDSKKPTC 426
Cdd:smart00032   1 CPPPPDIENGTVTS---SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 262-437 4.55e-08

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 54.61  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    262 SYPWNTTCTFDCVEGYRRVgaqnLQCTSSGIWDNETPSCKAVTCDAIPQPQNGFVScshSTAGELAFKSSCNFTCE---- 337
Cdd:PHA02831  39 VYEENENLEYKCNNNFDKV----FVTCNNGSWSTKNMCIGKRNCKDPVTILNGYIK---NKKDQYSFGDSVTYACKvnkl 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    338 QSFTLQGPAQVECsAQGQWTPQIPVCKAVQCEaLSAPQQGnmkCLPSASGPFQNGSSCEFSCEEGFELKGSRRLQCGPRG 417
Cdd:PHA02831 112 EKYSIVGNETVKC-INKQWVPKYPVCKLIRCK-YPALQNG---FLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINS 186

                        170       180
                 ....*....|....*....|
gi 266458    418 EWDSKKPTCSAVKCDDVPRP 437
Cdd:PHA02831 187 IWYPGIPKCVKDKVHNEIQP 206
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 32-131 1.66e-07

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: 50.27  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    32 TYDEASAYCQRDYTHLVAIQNKEEINYLNsnlKHSPSYYWIGI--RKVNNVWIWvGTGKPLTEEaqNWAPGEPNNK-QRN 108
Cdd:cd03588  21 TWEDAERRCREQQGHLSSIVTPEEQEFVN---NNAQDYQWIGLndRTIEGDFRW-SDGHPLQFE--NWRPNQPDNFfATG 94

                        90       100
                ....*....|....*....|...
gi 266458   109 EDCVeiyIQRTKDSGMWNDERCN 131
Cdd:cd03588  95 EDCV---VMIWHEEGEWNDVPCN 114
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 494-548 3.17e-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: 47.52  E-value: 3.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 266458      494 CPSLDVPGKMNMSCS-GTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:smart00032   1 CPPPPDIENGTVTSSsGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 389-489 4.92e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 51.09  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    389 FQNGSSCEFSCEEG-----FELKGSRRLQCGPRGEWDSKKPTCSAVKCDdVPRPQNGVMEcAHATTGEFTYKSSCAFQCN 463
Cdd:PHA02817  42 YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVN-GIPDSKKFYYESEVSFSCK 119

                         90       100
                 ....*....|....*....|....*.
gi 266458    464 EGFSLHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02817 120 PGFVLIGTKYSVCGINSSWIPKVPIC 145
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 180-238 1.65e-06

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: 45.60  E-value: 1.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458      180 CKPQEHPDYGSLNCSHpfGPFSYNSSCSFGCKRGYLPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIG-SSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
387-426 2.32e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 44.80  E-value: 2.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 266458     387 GPFQNGSSCEFSCEEGFELKGSRRLQCGPRGEWDSKKPTC 426
Cdd:pfam00084  17 NEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 238-363 3.98e-06

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 49.31  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    238 CHVVECEALtHPAHGirKCSSNPGSYPWNTTCTFDCVEGYRRVGAQNLQCTSSGiWdNETPSCKAvTCDaIPQPQNGFVS 317
Cdd:PHA02954 125 CPNAECQPL-QLEHG--SCQPVKEKYSFGEHITINCDVGYEVIGASYISCTANS-W-NVIPSCQQ-KCD-IPSLSNGLIS 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 266458    318 CSHSTAGELafkssCNFTCEQSFTLQGPAQVECsAQGQWTPQIPVC 363
Cdd:PHA02954 198 GSTFSIGGV-----IHLSCKSGFTLTGSPSSTC-IDGKWNPVLPIC 237
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 23-138 4.54e-06

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 46.81  E-value: 4.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEE---INYLNSNLKHSPSYYWIGIRK----------VNNVWIWVgTGKP 89
Cdd:cd03595  17 YFQDSRRRLNFEEARQACREDGGELLSIESENEqklIERFIQTLRASDGDFWIGLRRssqynvtssaCSSLYYWL-DGSI 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 266458    90 LTeeAQNWAPGEPNNKqrNEDCVEIYIQRTKDSGM-------WNDERCNKKKLALC 138
Cdd:cd03595  96 ST--FRNWYVDEPSCG--SEVCVVMYHQPSAPAGQggpylfqWNDDNCNMKNNFIC 147
PHA02831 PHA02831
EEV host range protein; Provisional
 392-489 5.03e-06

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 48.45  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    392 GSSCEFSCE----EGFELKGSRRLQCgPRGEWDSKKPTCSAVKCDdVPRPQNGVMEcahATTGEFTYKSSCAFQCNEGFS 467
Cdd:PHA02831  99 GDSVTYACKvnklEKYSIVGNETVKC-INKQWVPKYPVCKLIRCK-YPALQNGFLN---VFEKKFYYGDIVNFKCKKGFI 173

                         90       100
                 ....*....|....*....|..
gi 266458    468 LHGSAQLECTSQGKWTQEVPSC 489
Cdd:PHA02831 174 LLGSSVSTCDINSIWYPGIPKC 195
Sushi pfam00084
Sushi repeat (SCR repeat);
243-300 5.45e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 44.03  E-value: 5.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 266458     243 CEALTHPAHGIRKCSSNPgsYPWNTTCTFDCVEGYRRVGAQNLQCTSSGIWDNETPSC 300
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-175 6.73e-06

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.01  E-value: 6.73e-06
                        10        20
                ....*....|....*....|....*...
gi 266458   148 CSGHGECIETINSYTCKCHPGFLGPNCE 175
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA02831 PHA02831
EEV host range protein; Provisional
 389-548 1.06e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 47.29  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    389 FQNGSSCEFSCEEGFElkgSRRLQCGpRGEWDSKKPTCSAVKCDDVPRPQNGVMEcahATTGEFTYKSSCAFQCN----E 464
Cdd:PHA02831  40 YEENENLEYKCNNNFD---KVFVTCN-NGSWSTKNMCIGKRNCKDPVTILNGYIK---NKKDQYSFGDSVTYACKvnklE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    465 GFSLHGSAQLECTSqGKWTQEVPSCQVVQC--PSLDvPGKMNmSCSGTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWS 542
Cdd:PHA02831 113 KYSIVGNETVKCIN-KQWVPKYPVCKLIRCkyPALQ-NGFLN-VFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWY 189


                 ....*.
gi 266458    543 GMPPTC 548
Cdd:PHA02831 190 PGIPKC 195
Sushi pfam00084
Sushi repeat (SCR repeat);
180-238 1.27e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.87  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 266458     180 CKPQEHPDYGSLncSHPFGPFSYNSSCSFGCKRGYLPSSMETTVrCTSSGEWSAPAPAC 238
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTIT-CQEDGTWSPPFPEC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 426-548 4.41e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 45.32  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    426 CSAVKCDDVPRPQNGVMecaHATTGEFTYKSSCAFQCNEG-----FSLHGSAQLECTSQGKWTQEVPSCQVVQC--PSLD 498
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYI---YNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCrfPALQ 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 266458    499 VPGKMNMSCSGTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:PHA02817  96 NGFVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 27-138 2.16e-04

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 41.16  E-value: 2.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    27 SSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHspSYYWIGIR--KVNNVWIWVGtGKPLTeeaqNWapGEPNN 104
Cdd:cd03593  16 SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSreKSEKPWKWID-GSPLN----NL--FNIRG 86

                        90       100       110
                ....*....|....*....|....*....|....
gi 266458   105 KQRNEDCVeiYIQRTKdsgmWNDERCNKKKLALC 138
Cdd:cd03593  87 STKSGNCA--YLSSTG----IYSEDCSTKKRWIC 114
Sushi pfam00084
Sushi repeat (SCR repeat);
494-548 2.75e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.02  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 266458     494 CPslDVPGKMNMSCSGTA---VFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTC 548
Cdd:pfam00084   1 CP--PPPDIPNGKVSATKneyNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
148-175 7.13e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 7.13e-04
                           10        20
                   ....*....|....*....|....*....
gi 266458      148 CSGHGECIETINSYTCKCHPGF-LGPNCE 175
Cdd:smart00179  11 CQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 32-104 2.11e-03

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 38.72  E-value: 2.11e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266458    32 TYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYY-----WIGIRKVN-NVWIWVGTgKPLTEEAQNWAPGEPNN 104
Cdd:cd03597  21 SYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKqkltpWVGLRKINvSYWCWEDM-SPFTNTTLQWLPGEPSD 98
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 24-138 2.36e-03

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 38.52  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    24 YNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSY---YWIGIRKVNNVWIWVG-TGKPLTeeAQNW-- 97
Cdd:cd03596  12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGnweVWLGINDMVAEGKWVDvNGSPIS--YFNWer 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 266458    98 -APGEPNNKQRnEDCVeiyIQRTKDSGMWNDERCNKKKLALC 138
Cdd:cd03596  90 eITAQPDGGKR-ENCV---ALSSSAQGKWFDEDCRREKPYVC 127
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 148-175 4.51e-03

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


Pssm-ID: 238010  Cd Length: 36  Bit Score: 35.15  E-value: 4.51e-03
                        10        20
                ....*....|....*....|....*....
gi 266458   148 CSGHGECIETINSYTCKCHPGFLGP-NCE 175
Cdd:cd00053   8 CSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 32-138 5.16e-03

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 37.05  E-value: 5.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266458    32 TYDEASAYCQRDYT-HLVAIQN---KEEINYLNSNLkhSPSYYWIG----IRKVNNVWIWVgTGKPLTeeAQNWAPGEPN 103
Cdd:cd03598  12 TFRDAQVICRRCYRgNLASIHSfafNYRVQRLVSTL--NQAQVWIGgiitGKGRCRRFSWV-DGSVWN--YAYWAPGQPG 86

                        90       100       110
                ....*....|....*....|....*....|....*
gi 266458   104 NKQRNedCVEIyiqrTKDSGMWNDERCNKKKLALC 138
Cdd:cd03598  87 NRRGH--CVEL----CTRGGHWRRAHCKLRRPFIC 115
DUF3844 pfam12955
Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It ...
 138-167 5.21e-03

Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It contains 8 largely conserved cysteine residues. This domain is found in proteins that are thought to be found in the endoplasmic reticulum.


Pssm-ID: 432898  Cd Length: 104  Bit Score: 36.82  E-value: 5.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 266458     138 CYT--ASCTNA--SCSGHGECIETINS------YTCKCHP 167
Cdd:pfam12955   1 CFTseDACENAtnNCSGHGECVKKYKSksgrdcFACKCKA 40
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 143-173 5.48e-03

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 34.67  E-value: 5.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 266458     143 CTNASCSGHGECIETINSYTCKCHPGFLGPN 173
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
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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