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Conserved domains on  [gi|20302053|ref|NP_620234|]
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E-selectin precursor [Rattus norvegicus]

Protein Classification

CLECT_selectins_like and CCP domain-containing protein( domain architecture ID 12933815)

protein containing domains CLECT_selectins_like, EGF_CA, and CCP

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 9.11e-54

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: 9.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNST-LRYSPSYYWIGIRKVNNVWIWVGTQKPLtEEAKNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20302053 101 EPNNKqRNEDCVEIYIqrpKDSGMWNDERCDKKKLALCYT 140
Cdd:cd03592  80 EPNNG-RNENCLEIYI---KDNGKWNDEPCSKKKSAICYT 115
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 262-485 1.32e-13

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  262 SYPWNTTCTFDCEEGYRR--VGAQNLQCTSSGvWDNEKpSCKAVTCDAIPRPQNGSVSCsnstaGALAFKSSCNFTCEHS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDIDNGQLDI-----GGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  340 FTLQGPAQVEC----SAQGQWTPQIPVCKASQCEALSAPQRGHMKCLPSAsapFQSGSSCKFSCDEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF---YTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20302053  416 rGEWdSEKPTCAGVQCSSLDLP-GKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPHPTISnGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 186-238 7.78e-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: 49.00  E-value: 7.78e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 20302053 186 PDHGSLNCThpFGLFSYNSSCSFSCERGYVPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   7 PENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-174 3.72e-05

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


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 3.72e-05
                        10        20
                ....*....|....*....|....*..
gi 20302053 148 CSGHGECVETINSYTCKCHPGFLGPKC 174
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNC 37
 
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 9.11e-54

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: 9.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNST-LRYSPSYYWIGIRKVNNVWIWVGTQKPLtEEAKNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20302053 101 EPNNKqRNEDCVEIYIqrpKDSGMWNDERCDKKKLALCYT 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 1.04e-27

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 106.79  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053    31 MTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGI--RKVNNVWIWVGTQkplTEEAKNWAPgEPNNKQRN 108
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWAP-EPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 20302053   109 EDCVEIYiqrpKDSGMWNDERCDKKKLALCYT 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 3.76e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 86.11  E-value: 3.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053     22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRY--SPSYYWIGIR--KVNNVWIWVGTQKPLTeeAKNW 97
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 20302053     98 APGEPNNkqRNEDCVEIYiqrpKDSGMWNDERCDKKKLALC 138
Cdd:smart00034  89 APGEPNN--SSGDCVVLS----TSGGKWNDVSCTSKLPFVC 123
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 262-485 1.32e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  262 SYPWNTTCTFDCEEGYRR--VGAQNLQCTSSGvWDNEKpSCKAVTCDAIPRPQNGSVSCsnstaGALAFKSSCNFTCEHS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDIDNGQLDI-----GGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  340 FTLQGPAQVEC----SAQGQWTPQIPVCKASQCEALSAPQRGHMKCLPSAsapFQSGSSCKFSCDEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF---YTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20302053  416 rGEWdSEKPTCAGVQCSSLDLP-GKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPHPTISnGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 243-301 5.49e-12

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 60.94  E-value: 5.49e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053 243 CKALTQPAHGVRKCSSnpGSYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSCK 301
Cdd:cd00033   1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 243-300 1.05e-09

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 54.45  E-value: 1.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 20302053    243 CKALTQPAHGVRKCSSNPgsYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSC 300
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 186-238 7.78e-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: 49.00  E-value: 7.78e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 20302053 186 PDHGSLNCThpFGLFSYNSSCSFSCERGYVPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   7 PENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
305-363 7.85e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 7.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053   305 CDAIPRPQNGSVSCsnsTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:pfam00084   1 CPPPPDIPNGKVSA---TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 180-238 5.37e-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: 46.75  E-value: 5.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053    180 CQEQEYPDHGSLNCTHpfGLFSYNSSCSFSCERGYVPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIG-SSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
186-238 2.22e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 44.80  E-value: 2.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20302053   186 PDHGSLNCTHPFglFSYNSSCSFSCERGYVPSSMETTVrCTSSGEWSAPAPAC 238
Cdd:pfam00084   7 IPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTIT-CQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-174 3.72e-05

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 3.72e-05
                        10        20
                ....*....|....*....|....*..
gi 20302053 148 CSGHGECVETINSYTCKCHPGFLGPKC 174
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 143-172 2.81e-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: 35.44  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 20302053   143 CTNTSCSGHGECVETINSYTCKCHPGFLGP 172
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
148-175 4.68e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 4.68e-03
                           10        20
                   ....*....|....*....|....*....
gi 20302053    148 CSGHGECVETINSYTCKCHPGF-LGPKCD 175
Cdd:smart00179  11 CQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
 
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 9.11e-54

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: 9.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNST-LRYSPSYYWIGIRKVNNVWIWVGTQKPLtEEAKNWAPG 100
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFaLKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20302053 101 EPNNKqRNEDCVEIYIqrpKDSGMWNDERCDKKKLALCYT 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 1.04e-27

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 106.79  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053    31 MTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGI--RKVNNVWIWVGTQkplTEEAKNWAPgEPNNKQRN 108
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdRKNEGTWKWVDGS---PVNYTNWAP-EPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 20302053   109 EDCVEIYiqrpKDSGMWNDERCDKKKLALCYT 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 2.20e-22

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: 92.30  E-value: 2.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLR-YSPSYYWIGIRKV--NNVWIWVGTQKPLTeeAKNWA 98
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLssEGTWKWSDGSPLVD--YTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 20302053  99 PGEPNNkQRNEDCVEIYIQrpkDSGMWNDERCDKKKLALCY 139
Cdd:cd00037  79 PGEPNP-GGSEDCVVLSSS---SDGKWNDVSCSSKLPFICE 115
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 22-138 1.01e-21

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: 90.83  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  22 WYYnASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRySPSYYWIGI--RKVNNVWIWV-GTqkPLTEEAKNWA 98
Cdd:cd03590  12 CYF-FSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLsdEETEGEWKWVdGT--PLNSSKTFWH 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 20302053  99 PGEPNNKQ-RNEDCVEIYiqrpKDSGMWNDERCDKKKLALC 138
Cdd:cd03590  88 PGEPNNWGgGGEDCAELV----YDSGGWNDVPCNLEYRWIC 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 22-138 3.76e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 86.11  E-value: 3.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053     22 WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRY--SPSYYWIGIR--KVNNVWIWVGTQKPLTeeAKNW 97
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSdpDSNGSWQWSDGSGPVS--YSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 20302053     98 APGEPNNkqRNEDCVEIYiqrpKDSGMWNDERCDKKKLALC 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 3.57e-16

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 74.64  E-value: 3.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEE----INYLNSTLRYSpsyyWIGI--RKVNNVWIWVgTQKPLTeeAKN 96
Cdd:cd03591   3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKKGNTYA----FIGItdLETEGQFVYL-DGGPLT--YTN 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 20302053  97 WAPGEPNNKQRNEDCVEIYiqrpkDSGMWNDERCDKKKLALC 138
Cdd:cd03591  76 WKPGEPNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 262-485 1.32e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 71.22  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  262 SYPWNTTCTFDCEEGYRR--VGAQNLQCTSSGvWDNEKpSCKAVTCDAIPRPQNGSVSCsnstaGALAFKSSCNFTCEHS 339
Cdd:PHA02927  43 NYNIGDTIEYLCLPGYRKqkMGPIYAKCTGTG-WTLFN-QCIKRRCPSPRDIDNGQLDI-----GGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  340 FTLQGPAQVEC----SAQGQWTPQIPVCKASQCEALSAPQRGHMKCLPSAsapFQSGSSCKFSCDEGFELKGSRRLQCGP 415
Cdd:PHA02927 116 YQLIGESKSYCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF---YTDGSVVTYSCNSGYSLIGNSGVLCSG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20302053  416 rGEWdSEKPTCAGVQCSSLDLP-GKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:PHA02927 193 -GEW-SDPPTCQIVKCPHPTISnGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 187-363 2.71e-13

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 70.07  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  187 DHGSLNcthpFGLFSYNSSCSFSCERGYV---PSSMETTVRCTSSGEWSAPAPACHVVECKALTQPAHGVRKCSSNpgSY 263
Cdd:PHA02927  93 DNGQLD----IGGVDFGSSITYSCNSGYQligESKSYCELGSTGSMVWNPEAPICESVKCQSPPSISNGRHNGYED--FY 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  264 PWNTTCTFDCEEGYRRVGAQNLQCtSSGVWDNeKPSCKAVTCdaiPRPQNGSVSCSNSTAGALAFKSSCNFTCEHSFTLQ 343
Cdd:PHA02927 167 TDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSD-PPTCQIVKC---PHPTISNGYLSSGFKRSYSYNDNVDFKCKYGYKLS 241

                        170       180
                 ....*....|....*....|
gi 20302053  344 GPAQVECSAQGQWTPQIPVC 363
Cdd:PHA02927 242 GSSSSTCSPGNTWQPELPKC 261
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 28-139 5.61e-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: 65.09  E-value: 5.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  28 SELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGIRKVNNVWIWVGTQkplTEEAKNWAPGEPnnkQR 107
Cdd:cd03602   7 NESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGS---ESSFRNWNTFQP---FG 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 20302053 108 NEDCVEIYIqrpkdSGMWNDERCDKKKLALCY 139
Cdd:cd03602  81 QGDCATMYS-----SGRWYAALCSALKPFICY 107
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 243-301 5.49e-12

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 60.94  E-value: 5.49e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053 243 CKALTQPAHGVRKCSSnpGSYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSCK 301
Cdd:cd00033   1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 28-133 1.31e-11

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: 62.38  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  28 SELMTYDEASAYCqRDYT------HLVAIQNKEEINYL----NSTLRYSPSY-YWIGI--RKVNNVWIWV-GTQKPLTee 93
Cdd:cd03589  17 GDRLTWEEAELRC-RSFSipgliaHLVSIHSQEENDFVydlfESSRGPDTPYgLWIGLhdRTSEGPFEWTdGSPVDFT-- 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20302053  94 akNWAPGEPNNKQRNEDCVEIYiQRPKDSGMWNDERCDKK 133
Cdd:cd03589  94 --KWAGGQPDNYGGNEDCVQMW-RRGDAGQSWNDMPCDAV 130
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 368-426 3.62e-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: 58.63  E-value: 3.62e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053 368 CEALSAPQRGHMKClpsASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTC 426
Cdd:cd00033   1 CPPPPVPENGTVTG---SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 27-138 4.20e-11

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: 60.24  E-value: 4.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  27 SSELMTYDEASAYCQRDYTHLVAIQNKE-EINYLNSTLRYSPSY-YWIGIRKVNNV---WIWvGTQKPLTEEAKNWAPGE 101
Cdd:cd03601   6 SDETMNYAKAGAFCRSRGMRLASLAMRDsEMRDAILAFTLVKGHgYWVGADNLQDGeydFLW-NDGVSLPTDSDLWAPNE 84

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 20302053 102 PNNKQRNEDCVEIYIQRpkdsGMWNDERCDKKKLALC 138
Cdd:cd03601  85 PSNPQSRQLCVQLWSKY----NLLDDEYCGRAKRVIC 117
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 23-127 4.73e-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: 60.13  E-value: 4.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSpSYYWIGIRKVNNVWIWVGTQKPlTEEAKNWAPGEP 102
Cdd:cd03603   2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKWSDGE-ESTYTNWGSGEP 79

                        90       100
                ....*....|....*....|....*.
gi 20302053 103 -NNKQRNEDCVEIYiQRPKDSGMWND 127
Cdd:cd03603  80 hNNGGGNEDYAAIN-HFPGISGKWND 104
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 305-364 5.91e-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: 5.91e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053 305 CDAIPRPQNGSVSCSNSTagaLAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVCK 364
Cdd:cd00033   1 CPPPPVPENGTVTGSKGS---YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02639 PHA02639
EEV host range protein; Provisional
 271-426 7.46e-11

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 63.14  E-value: 7.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  271 FDCEEGYRRVGAQNLQC---TSSGVWDNEKPSCKAVTCDAIPRPQNGSVSCSNSTagaLAFKSSCNFTC-EH---SFTLQ 343
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIYNKREM---YKVGDEIYYVCnEHkgvQYSLV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  344 GPAQVECSAQGQWTPQIPVCKASQCEaLSAPQRGHMKCLPSaSAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEK 423
Cdd:PHA02639 125 GNEKITCIQDKSWKPDPPICKMINCR-FPALQNGYINGIPS-NKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSI 202


                 ...
gi 20302053  424 PTC 426
Cdd:PHA02639 203 PTC 205
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 431-486 4.30e-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: 4.30e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20302053 431 CSSLDLPGKMNMSCS-GPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTCE 486
Cdd:cd00033   1 CPPPPVPENGTVTGSkGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57
PHA02639 PHA02639
EEV host range protein; Provisional
 208-363 6.98e-10

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 60.45  E-value: 6.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  208 FSCERGY--VPSSMETTVRCTSSGEWSAPAPACHVVECKALTQPAHGvrKCSSNPGSYPWNTTCTFDCEE----GYRRVG 281
Cdd:PHA02639  48 YTCNTDYalIGDRFRTCIKDKNNAIWSNKAPFCMLKECNDPPSIING--KIYNKREMYKVGDEIYYVCNEhkgvQYSLVG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  282 AQNLQCTSSGVWDNEKPSCKAVTCdAIPRPQNGSVSCSNSTAgALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIP 361
Cdd:PHA02639 126 NEKITCIQDKSWKPDPPICKMINC-RFPALQNGYINGIPSNK-KFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIP 203


                 ..
gi 20302053  362 VC 363
Cdd:PHA02639 204 TC 205
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 243-300 1.05e-09

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 54.45  E-value: 1.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 20302053    243 CKALTQPAHGVRKCSSNPgsYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSC 300
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 368-426 3.49e-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: 52.91  E-value: 3.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053    368 CEALSAPQRGHMKClpsASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTC 426
Cdd:smart00032   1 CPPPPDIENGTVTS---SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 263-363 1.14e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 55.72  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  263 YPWNTTCTFDCEEG-----YRRVGAQNLQCTSSGVWDNEKPSCKAVTCdAIPRPQNGSVSCSNSTAgALAFKSSCNFTCE 337
Cdd:PHA02817  42 YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRC-RFPALQNGFVNGIPDSK-KFYYESEVSFSCK 119

                         90       100
                 ....*....|....*....|....*.
gi 20302053  338 HSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:PHA02817 120 PGFVLIGTKYSVCGINSSWIPKVPIC 145
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 305-363 1.19e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 51.37  E-value: 1.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053    305 CDAIPRPQNGSVSCSNSTagaLAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT---YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 186-238 7.78e-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: 49.00  E-value: 7.78e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 20302053 186 PDHGSLNCThpFGLFSYNSSCSFSCERGYVPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:cd00033   7 PENGTVTGS--KGSYSYGSTVTYSCNEGYTLVG-SSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
305-363 7.85e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.03  E-value: 7.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053   305 CDAIPRPQNGSVSCsnsTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVC 363
Cdd:pfam00084   1 CPPPPDIPNGKVSA---TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02817 PHA02817
EEV Host range protein; Provisional
 299-426 1.25e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 52.64  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  299 SCKAVTCDAIPRPQNGSVSCSNSTagaLAFKSSCNFTCEHS-----FTLQGPAQVECSAQGQWTPQIPVCKASQCEaLSA 373
Cdd:PHA02817  18 LCDLNKCCYPPSIKNGYIYNKKTE---YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20302053  374 PQRGHMKCLPSaSAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTC 426
Cdd:PHA02817  94 LQNGFVNGIPD-SKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
Sushi pfam00084
Sushi repeat (SCR repeat);
243-300 3.04e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 47.49  E-value: 3.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20302053   243 CKALTQPAHGVRKCSSNPgsYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSC 300
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 450-485 3.07e-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: 3.07e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 20302053    450 FGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:smart00032  21 YGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 247-485 3.72e-07

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 52.01  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  247 TQPAHGVRKCSSNPGSYPWNTTCTFDCEEGYRRVGAqNLQCTSSGvWDNEKPSCKAVTC-DAIPRPQNGSVSCSNSTAGA 325
Cdd:PHA02954  22 TVPTMNNAKLTSTETSFNDKQKVTFTCDSGYYSLDP-NAVCETDK-WKYENPCKKMCTVsDYVSELYDKPLYEVNSTITL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  326 LAFKSSCNFTCEhsftlqgpaqvECSAQGQWTPQIpVCKASQCEALsapQRGHMKCLPsASAPFQSGSSCKFSCDEGFEL 405
Cdd:PHA02954 100 ICKDETKYFRCE-----------EKNGNTSWNDTV-TCPNAECQPL---QLEHGSCQP-VKEKYSFGEHITINCDVGYEV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  406 KGSRRLQCGPrGEWDSeKPTCAgvqcSSLDLPGKMNMSCSGPAV-FGTVCEFTCPEGWTLNGSSILTCgATGRWSAMLPT 484
Cdd:PHA02954 164 IGASYISCTA-NSWNV-IPSCQ----QKCDIPSLSNGLISGSTFsIGGVIHLSCKSGFTLTGSPSSTC-IDGKWNPVLPI 236


                 .
gi 20302053  485 C 485
Cdd:PHA02954 237 C 237
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 208-369 3.89e-07

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 52.01  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  208 FSCERGYVPSSMETTVRCTSSgewsapapachvvECKALtQPAHGvrKCSSNPGSYPWNTTCTFDCEEGYRRVGAQNLQC 287
Cdd:PHA02954 108 FRCEEKNGNTSWNDTVTCPNA-------------ECQPL-QLEHG--SCQPVKEKYSFGEHITINCDVGYEVIGASYISC 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  288 TSSGvWdNEKPSCKAvTCDaIPRPQNGSVSCSNSTAGALafkssCNFTCEHSFTLQGPAQVECsAQGQWTPQIPVCKASQ 367
Cdd:PHA02954 172 TANS-W-NVIPSCQQ-KCD-IPSLSNGLISGSTFSIGGV-----IHLSCKSGFTLTGSPSSTC-IDGKWNPVLPICVRSN 241


                 ..
gi 20302053  368 CE 369
Cdd:PHA02954 242 EE 243
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 180-238 5.37e-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: 46.75  E-value: 5.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053    180 CQEQEYPDHGSLNCTHpfGLFSYNSSCSFSCERGYVPSSmETTVRCTSSGEWSAPAPAC 238
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIG-SSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
368-426 1.64e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 45.18  E-value: 1.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053   368 CEALSAPQRGHmkcLPSASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTC 426
Cdd:pfam00084   1 CPPPPDIPNGK---VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
186-238 2.22e-06

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 44.80  E-value: 2.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 20302053   186 PDHGSLNCTHPFglFSYNSSCSFSCERGYVPSSMETTVrCTSSGEWSAPAPAC 238
Cdd:pfam00084   7 IPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTIT-CQEDGTWSPPFPEC 56
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 23-138 7.88e-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: 46.04  E-value: 7.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  23 YYNASSELMTYDEASAYCQRDYTHLVAIQNKEE---INYLNSTLRYSPSYYWIGIRK----------VNNVWIWV-GTQK 88
Cdd:cd03595  17 YFQDSRRRLNFEEARQACREDGGELLSIESENEqklIERFIQTLRASDGDFWIGLRRssqynvtssaCSSLYYWLdGSIS 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20302053  89 PLteeaKNWAPGEPNNKqrNEDCVEIYIQRPKDSGM-------WNDERCDKKKLALC 138
Cdd:cd03595  97 TF----RNWYVDEPSCG--SEVCVVMYHQPSAPAGQggpylfqWNDDNCNMKNNFIC 147
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 32-131 2.13e-05

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 44.11  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  32 TYDEASAYCQRDYTHLVAIQNKEEINYLNstlRYSPSYYWIGI--RKVNNVWIWVGTQKPLTEeakNWAPGEPNNK-QRN 108
Cdd:cd03588  21 TWEDAERRCREQQGHLSSIVTPEEQEFVN---NNAQDYQWIGLndRTIEGDFRWSDGHPLQFE---NWRPNQPDNFfATG 94

                        90       100
                ....*....|....*....|...
gi 20302053 109 EDCVeiyIQRPKDSGMWNDERCD 131
Cdd:cd03588  95 EDCV---VMIWHEEGEWNDVPCN 114
PHA02831 PHA02831
EEV host range protein; Provisional
 327-426 3.03e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 45.75  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  327 AFKSSCNFTCE----HSFTLQGPAQVECsAQGQWTPQIPVCKASQCEaLSAPQRGhmkCLPSASAPFQSGSSCKFSCDEG 402
Cdd:PHA02831  97 SFGDSVTYACKvnklEKYSIVGNETVKC-INKQWVPKYPVCKLIRCK-YPALQNG---FLNVFEKKFYYGDIVNFKCKKG 171

                         90       100
                 ....*....|....*....|....
gi 20302053  403 FELKGSRRLQCGPRGEWDSEKPTC 426
Cdd:PHA02831 172 FILLGSSVSTCDINSIWYPGIPKC 195
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 148-174 3.72e-05

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 3.72e-05
                        10        20
                ....*....|....*....|....*..
gi 20302053 148 CSGHGECVETINSYTCKCHPGFLGPKC 174
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNC 37
PHA02831 PHA02831
EEV host range protein; Provisional
 203-363 3.89e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 45.37  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  203 NSSCSFSCERGYvpssMETTVRCtSSGEWSAPAPACHVVECKALTQPAHGVRKCSSNpgSYPWNTTCTFDCE----EGYR 278
Cdd:PHA02831  43 NENLEYKCNNNF----DKVFVTC-NNGSWSTKNMCIGKRNCKDPVTILNGYIKNKKD--QYSFGDSVTYACKvnklEKYS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  279 RVGAQNLQCTSsGVWDNEKPSCKAVTCDaIPRPQNGSVscsNSTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTP 358
Cdd:PHA02831 116 IVGNETVKCIN-KQWVPKYPVCKLIRCK-YPALQNGFL---NVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYP 190


                 ....*
gi 20302053  359 QIPVC 363
Cdd:PHA02831 191 GIPKC 195
PHA02831 PHA02831
EEV host range protein; Provisional
 395-485 4.70e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 45.37  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  395 CKFSCDEGFELKGSRRLQCgPRGEWDSEKPTCAGVQCSSLDLPGKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGA 474
Cdd:PHA02831 106 CKVNKLEKYSIVGNETVKC-INKQWVPKYPVCKLIRCKYPALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDI 184

                         90
                 ....*....|.
gi 20302053  475 TGRWSAMLPTC 485
Cdd:PHA02831 185 NSIWYPGIPKC 195
PHA02639 PHA02639
EEV host range protein; Provisional
 334-485 4.80e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 45.43  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  334 FTCEHSFTLQGPAQVEC---SAQGQWTPQIPVCKASQCEALSAPQRGHMKclpSASAPFQSGSSCKFSCDE----GFELK 406
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIY---NKREMYKVGDEIYYVCNEhkgvQYSLV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  407 GSRRLQCGPRGEWDSEKPTCAGVQCSsldLPGKMNMSCSG-PA----VFGTVCEFTCPEGWTLNGSSILTCGATGRWSAM 481
Cdd:PHA02639 125 GNEKITCIQDKSWKPDPPICKMINCR---FPALQNGYINGiPSnkkfYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPS 201


                 ....
gi 20302053  482 LPTC 485
Cdd:PHA02639 202 IPTC 205
Sushi pfam00084
Sushi repeat (SCR repeat);
450-485 1.18e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 40.18  E-value: 1.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 20302053   450 FGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:pfam00084  21 YGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 32-138 2.70e-04

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 40.90  E-value: 2.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  32 TYDEASAYCQRDYT-HLVAIQNkEEINY--LNSTLRYSPSYYWIGIRkvnnVWIWVGTQKPLTEEAK-----NWAPGEPN 103
Cdd:cd03598  12 TFRDAQVICRRCYRgNLASIHS-FAFNYrvQRLVSTLNQAQVWIGGI----ITGKGRCRRFSWVDGSvwnyaYWAPGQPG 86

                        90       100       110
                ....*....|....*....|....*....|....*
gi 20302053 104 NKQRNedCVEIYiqrpKDSGMWNDERCDKKKLALC 138
Cdd:cd03598  87 NRRGH--CVELC----TRGGHWRRAHCKLRRPFIC 115
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 32-104 1.14e-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: 39.10  E-value: 1.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20302053  32 TYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYY-----WIGIRKVN-NVWIWvGTQKPLTEEAKNWAPGEPNN 104
Cdd:cd03597  21 SYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKqkltpWVGLRKINvSYWCW-EDMSPFTNTTLQWLPGEPSD 98
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 143-172 2.81e-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: 35.44  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 20302053   143 CTNTSCSGHGECVETINSYTCKCHPGFLGP 172
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 148-173 3.26e-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: 35.53  E-value: 3.26e-03
                        10        20
                ....*....|....*....|....*.
gi 20302053 148 CSGHGECVETINSYTCKCHPGFLGPK 173
Cdd:cd00053   8 CSNGGTCVNTPGSYRCVCPPGYTGDR 33
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 27-138 3.31e-03

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: 37.70  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  27 SSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRysPSYYWIGIR--KVNNVWIWVGTQKPlteeaKNWapGEPNN 104
Cdd:cd03593  16 SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG--SSSYWIGLSreKSEKPWKWIDGSPL-----NNL--FNIRG 86

                        90       100       110
                ....*....|....*....|....*....|....
gi 20302053 105 KQRNEDCVeiYIQrpkdSGMWNDERCDKKKLALC 138
Cdd:cd03593  87 STKSGNCA--YLS----STGIYSEDCSTKKRWIC 114
PHA02817 PHA02817
EEV Host range protein; Provisional
 389-485 3.92e-03

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 39.15  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  389 FQSGSSCKFSCDEG-----FELKGSRRLQCGPRGEWDSEKPTCAGVQCSsldLPGKMNMSCSG-PA----VFGTVCEFTC 458
Cdd:PHA02817  42 YNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR---FPALQNGFVNGiPDskkfYYESEVSFSC 118

                         90       100
                 ....*....|....*....|....*..
gi 20302053  459 PEGWTLNGSSILTCGATGRWSAMLPTC 485
Cdd:PHA02817 119 KPGFVLIGTKYSVCGINSSWIPKVPIC 145
EGF_CA smart00179
Calcium-binding EGF-like domain;
148-175 4.68e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 4.68e-03
                           10        20
                   ....*....|....*....|....*....
gi 20302053    148 CSGHGECVETINSYTCKCHPGF-LGPKCD 175
Cdd:smart00179  11 CQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
DUF3844 pfam12955
Domain of unknown function (DUF3844); This presumed domain is found in fungal species. It ...
 138-167 5.10e-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: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 20302053   138 CYT--ASCTNT--SCSGHGECVETINS------YTCKCHP 167
Cdd:pfam12955   1 CFTseDACENAtnNCSGHGECVKKYKSksgrdcFACKCKA 40
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 24-138 5.78e-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: 37.37  E-value: 5.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302053  24 YNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSY---YWIGIRKVNNVWIWVG-TQKPLTeeAKNW-- 97
Cdd:cd03596  12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGnweVWLGINDMVAEGKWVDvNGSPIS--YFNWer 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 20302053  98 -APGEPNNKQRnEDCVeiyIQRPKDSGMWNDERCDKKKLALC 138
Cdd:cd03596  90 eITAQPDGGKR-ENCV---ALSSSAQGKWFDEDCRREKPYVC 127
 
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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