NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|193211092|ref|NP_509919|]
View 

C-type LECtin [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MD smart00604
MD domain;
1262-1401 5.04e-37

MD domain;


:

Pssm-ID: 214741  Cd Length: 145  Bit Score: 136.92  E-value: 5.04e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1262 VNIVPGGLWKVTVQSN-SGSCEIQARSQSDIQVFFGFVTDPRNDKPSTYANIQSNS--NYLIAYPTGVLpytpDTKPSME 1338
Cdd:smart00604    1 YAHLPPGTWTITVRANgSNSCTISVRSQSSLQVVLGFTTDIQNDRPSHYPNKFANSttNSLIVYHAGGL----DNENAIQ 76

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1339 GKL-NYAVL-SSNRTITNSLPlGNRACTYATISAPFSCPVTDGSLSDFS-----IKFTGIDQYGYAFERY 1401
Cdd:smart00604   77 AILtEYATNhYSNRTPMETRF-CTYAPVLERLSLTDGCAYEFVSTSDFScdyfvVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
153-285 4.64e-29

MD domain;


:

Pssm-ID: 214741  Cd Length: 145  Bit Score: 114.20  E-value: 4.64e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092    153 YADLPSGGYTLSIDNQgvPTSECIIEVNGDpSGLKAVDGFVYSPQSDDP-PYG----ESAINGVPMYMAAHVDNSPAQ-- 225
Cdd:smart00604    1 YAHLPPGTWTITVRAN--GSNSCTISVRSQ-SSLQVVLGFTTDIQNDRPsHYPnkfaNSTTNSLIVYHAGGLDNENAIqa 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092    226 --VQSITIRQGNSL---------APVYRAaLTRRYQCGYEYYAG-QWQCQlgnAYFYHIDGVDANGFNFRRT 285
Cdd:smart00604   78 ilTEYATNHYSNRTpmetrfctyAPVLER-LSLTDGCAYEFVSTsDFSCD---YFVVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
1757-1887 1.69e-23

MD domain;


:

Pssm-ID: 214741  Cd Length: 145  Bit Score: 98.40  E-value: 1.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1757 AGTYRILLTGTGGNNCFATVRGRSNLELFLGFVdsssdghNGATNDATHYAPVNLENNT----IVVHANGL------GAG 1826
Cdd:smart00604    6 PGTWTITVRANGSNSCTISVRSQSSLQVVLGFT-------TDIQNDRPSHYPNKFANSTtnslIVYHAGGLdnenaiQAI 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092   1827 IVRYVQI-VMPRFG----------LLHTTEMRkrdSACSYEWYATTPFSFDYdqYYVIIYGSSEFGSNWKRN 1887
Cdd:smart00604   79 LTEYATNhYSNRTPmetrfctyapVLERLSLT---DGCAYEFVSTSDFSCDY--FVVLIDGVDENGYNFRRT 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1914-2070 7.84e-21

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


:

Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 91.20  E-value: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAgENSFDRVSELIYNMQYIGIDGQ 1993
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND-YKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193211092 1994 NVTAGLQYALDYYDLPSQgyrTGSDVRHLLVYVTQTNPTDA-DPSELLRTIKRSGlYEVVVVALDMQPSDKLTNMVNP 2070
Cdd:cd01450    81 NTGKALQYALEQLFSESN---ARENVPKVIIVLTDGRSDDGgDPKEAAAKLKDEG-IKVFVVGVGPADEEELREIASC 154
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1126-1236 2.77e-18

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: 82.65  E-value: 2.77e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1126 SFWNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI----GSYRVWIGLAF--NNGQWYWDvpDGN 1199
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDpdSNGSWQWS--DGS 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 193211092   1200 faqPLTGYTNWAPNVdPTNPAYNHAVIN-SNGKWEPAD 1236
Cdd:smart00034   81 ---GPVSYSNWAPGE-PNNSSGDCVVLStSGGKWNDVS 114
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1484-1660 1.93e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


:

Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 44.09  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1484 LVLMLETSYNMGSSIFQLKKN-LKASLDSINNDPTTqgwfTNFVLYPFDstSNKDSWYPPTISRNSDDIVTALKNISTMS 1562
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEaLKALVSSLSASPPG----DRVGLVTFG--SNARVVLPLTTDTDKADLLEAIDALKKGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1563 CPGSAPCSSqcprpiVSVLSSILDMNALAAPNSVIVVITRSSPEDYLQ-VGQISQKLQTKKAYINFVfpAIDSpcgegwn 1641
Cdd:cd00198    77 GGGTNIGAA------LRLALELLKSAKRPNARRVIILLTDGEPNDGPElLAEAARELRKLGITVYTI--GIGD------- 141

                         170
                  ....*....|....*....
gi 193211092 1642 SPNTDALFQIISYSQGNTF 1660
Cdd:cd00198   142 DANEDELKEIADKTTGGAV 160
 
Name Accession Description Interval E-value
MD smart00604
MD domain;
1262-1401 5.04e-37

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 136.92  E-value: 5.04e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1262 VNIVPGGLWKVTVQSN-SGSCEIQARSQSDIQVFFGFVTDPRNDKPSTYANIQSNS--NYLIAYPTGVLpytpDTKPSME 1338
Cdd:smart00604    1 YAHLPPGTWTITVRANgSNSCTISVRSQSSLQVVLGFTTDIQNDRPSHYPNKFANSttNSLIVYHAGGL----DNENAIQ 76

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1339 GKL-NYAVL-SSNRTITNSLPlGNRACTYATISAPFSCPVTDGSLSDFS-----IKFTGIDQYGYAFERY 1401
Cdd:smart00604   77 AILtEYATNhYSNRTPMETRF-CTYAPVLERLSLTDGCAYEFVSTSDFScdyfvVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
153-285 4.64e-29

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 114.20  E-value: 4.64e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092    153 YADLPSGGYTLSIDNQgvPTSECIIEVNGDpSGLKAVDGFVYSPQSDDP-PYG----ESAINGVPMYMAAHVDNSPAQ-- 225
Cdd:smart00604    1 YAHLPPGTWTITVRAN--GSNSCTISVRSQ-SSLQVVLGFTTDIQNDRPsHYPnkfaNSTTNSLIVYHAGGLDNENAIqa 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092    226 --VQSITIRQGNSL---------APVYRAaLTRRYQCGYEYYAG-QWQCQlgnAYFYHIDGVDANGFNFRRT 285
Cdd:smart00604   78 ilTEYATNHYSNRTpmetrfctyAPVLER-LSLTDGCAYEFVSTsDFSCD---YFVVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
1757-1887 1.69e-23

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 98.40  E-value: 1.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1757 AGTYRILLTGTGGNNCFATVRGRSNLELFLGFVdsssdghNGATNDATHYAPVNLENNT----IVVHANGL------GAG 1826
Cdd:smart00604    6 PGTWTITVRANGSNSCTISVRSQSSLQVVLGFT-------TDIQNDRPSHYPNKFANSTtnslIVYHAGGLdnenaiQAI 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092   1827 IVRYVQI-VMPRFG----------LLHTTEMRkrdSACSYEWYATTPFSFDYdqYYVIIYGSSEFGSNWKRN 1887
Cdd:smart00604   79 LTEYATNhYSNRTPmetrfctyapVLERLSLT---DGCAYEFVSTSDFSCDY--FVVLIDGVDENGYNFRRT 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1914-2070 7.84e-21

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 91.20  E-value: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAgENSFDRVSELIYNMQYIGIDGQ 1993
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND-YKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193211092 1994 NVTAGLQYALDYYDLPSQgyrTGSDVRHLLVYVTQTNPTDA-DPSELLRTIKRSGlYEVVVVALDMQPSDKLTNMVNP 2070
Cdd:cd01450    81 NTGKALQYALEQLFSESN---ARENVPKVIIVLTDGRSDDGgDPKEAAAKLKDEG-IKVFVVGVGPADEEELREIASC 154
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1126-1236 2.77e-18

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: 82.65  E-value: 2.77e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1126 SFWNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI----GSYRVWIGLAF--NNGQWYWDvpDGN 1199
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDpdSNGSWQWS--DGS 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 193211092   1200 faqPLTGYTNWAPNVdPTNPAYNHAVIN-SNGKWEPAD 1236
Cdd:smart00034   81 ---GPVSYSNWAPGE-PNNSSGDCVVLStSGGKWNDVS 114
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1914-2082 1.06e-16

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 79.81  E-value: 1.06e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNaGENSFDRVSELIYNMQYIGIDGQ 1993
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN-DSRSKDALLEALASLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1994 NVTAGLQYALDYYDLPSQGYRtgSDVRHLLVYVTQTNPTDA--DPSELLRTIKRSGLyEVVVVAL----DMQPSDKLTNM 2067
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGpkDLLKAAKELKRSGV-KVFVVGVgndvDEEELKKLASA 156

                           170
                    ....*....|....*
gi 193211092   2068 VNPRCFYLAQDFHDL 2082
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1134-1249 6.57e-16

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: 75.73  E-value: 6.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1134 NCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI---GSYRVWIGLAFN--NGQWYWDvpDGNfaqPLTGYT 1208
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLssEGTWKWS--DGS---PLVDYT 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193211092 1209 NWAPNVDPTNPAYNHAVINSN--GKWEPADPNDaaNNFAACMK 1249
Cdd:cd00037    76 NWAPGEPNPGGSEDCVVLSSSsdGKWNDVSCSS--KLPFICEK 116
VWA pfam00092
von Willebrand factor type A domain;
1914-2079 1.25e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 65.37  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1914 DTLFLIDSSlkdSNVT---FRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAGENSfDRVSELIYNMQYIGI 1990
Cdd:pfam00092    1 DIVFLLDGS---GSIGgdnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSK-EELLSAVDNLRYLGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1991 DGQNVTAGLQYALDYYDLPSQGYRTGsdVRHLLVYVTQTNPTDADPSELLRTIKRSGlYEVVVVALDMQPSDKLTNMV-- 2068
Cdd:pfam00092   77 GTTNTGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDGDPEEVARELKSAG-VTVFAVGVGNADDEELRKIAse 153

                          170
                   ....*....|..
gi 193211092  2069 -NPRCFYLAQDF 2079
Cdd:pfam00092  154 pGEGHVFTVSDF 165
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1142-1233 5.09e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 58.64  E-value: 5.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1142 KLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSYRV--WIGLAF--NNGQWYWDvpDGNfaqPLTgYTNWAPNVDPT 1217
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfWIGLTDrkNEGTWKWV--DGS---PVN-YTNWAPEPNNN 74

                           90
                   ....*....|....*..
gi 193211092  1218 NPAYNHAVIN-SNGKWE 1233
Cdd:pfam00059   75 GENEDCVELSsSSGKWN 91
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1484-1660 1.93e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 44.09  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1484 LVLMLETSYNMGSSIFQLKKN-LKASLDSINNDPTTqgwfTNFVLYPFDstSNKDSWYPPTISRNSDDIVTALKNISTMS 1562
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEaLKALVSSLSASPPG----DRVGLVTFG--SNARVVLPLTTDTDKADLLEAIDALKKGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1563 CPGSAPCSSqcprpiVSVLSSILDMNALAAPNSVIVVITRSSPEDYLQ-VGQISQKLQTKKAYINFVfpAIDSpcgegwn 1641
Cdd:cd00198    77 GGGTNIGAA------LRLALELLKSAKRPNARRVIILLTDGEPNDGPElLAEAARELRKLGITVYTI--GIGD------- 141

                         170
                  ....*....|....*....
gi 193211092 1642 SPNTDALFQIISYSQGNTF 1660
Cdd:cd00198   142 DANEDELKEIADKTTGGAV 160
 
Name Accession Description Interval E-value
MD smart00604
MD domain;
1262-1401 5.04e-37

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 136.92  E-value: 5.04e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1262 VNIVPGGLWKVTVQSN-SGSCEIQARSQSDIQVFFGFVTDPRNDKPSTYANIQSNS--NYLIAYPTGVLpytpDTKPSME 1338
Cdd:smart00604    1 YAHLPPGTWTITVRANgSNSCTISVRSQSSLQVVLGFTTDIQNDRPSHYPNKFANSttNSLIVYHAGGL----DNENAIQ 76

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1339 GKL-NYAVL-SSNRTITNSLPlGNRACTYATISAPFSCPVTDGSLSDFS-----IKFTGIDQYGYAFERY 1401
Cdd:smart00604   77 AILtEYATNhYSNRTPMETRF-CTYAPVLERLSLTDGCAYEFVSTSDFScdyfvVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
153-285 4.64e-29

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 114.20  E-value: 4.64e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092    153 YADLPSGGYTLSIDNQgvPTSECIIEVNGDpSGLKAVDGFVYSPQSDDP-PYG----ESAINGVPMYMAAHVDNSPAQ-- 225
Cdd:smart00604    1 YAHLPPGTWTITVRAN--GSNSCTISVRSQ-SSLQVVLGFTTDIQNDRPsHYPnkfaNSTTNSLIVYHAGGLDNENAIqa 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092    226 --VQSITIRQGNSL---------APVYRAaLTRRYQCGYEYYAG-QWQCQlgnAYFYHIDGVDANGFNFRRT 285
Cdd:smart00604   78 ilTEYATNHYSNRTpmetrfctyAPVLER-LSLTDGCAYEFVSTsDFSCD---YFVVLIDGVDENGYNFRRT 145
MD smart00604
MD domain;
1757-1887 1.69e-23

MD domain;


Pssm-ID: 214741  Cd Length: 145  Bit Score: 98.40  E-value: 1.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1757 AGTYRILLTGTGGNNCFATVRGRSNLELFLGFVdsssdghNGATNDATHYAPVNLENNT----IVVHANGL------GAG 1826
Cdd:smart00604    6 PGTWTITVRANGSNSCTISVRSQSSLQVVLGFT-------TDIQNDRPSHYPNKFANSTtnslIVYHAGGLdnenaiQAI 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193211092   1827 IVRYVQI-VMPRFG----------LLHTTEMRkrdSACSYEWYATTPFSFDYdqYYVIIYGSSEFGSNWKRN 1887
Cdd:smart00604   79 LTEYATNhYSNRTPmetrfctyapVLERLSLT---DGCAYEFVSTSDFSCDY--FVVLIDGVDENGYNFRRT 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1914-2070 7.84e-21

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 91.20  E-value: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAgENSFDRVSELIYNMQYIGIDGQ 1993
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND-YKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193211092 1994 NVTAGLQYALDYYDLPSQgyrTGSDVRHLLVYVTQTNPTDA-DPSELLRTIKRSGlYEVVVVALDMQPSDKLTNMVNP 2070
Cdd:cd01450    81 NTGKALQYALEQLFSESN---ARENVPKVIIVLTDGRSDDGgDPKEAAAKLKDEG-IKVFVVGVGPADEEELREIASC 154
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1126-1236 2.77e-18

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: 82.65  E-value: 2.77e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1126 SFWNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI----GSYRVWIGLAF--NNGQWYWDvpDGN 1199
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDpdSNGSWQWS--DGS 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 193211092   1200 faqPLTGYTNWAPNVdPTNPAYNHAVIN-SNGKWEPAD 1236
Cdd:smart00034   81 ---GPVSYSNWAPGE-PNNSSGDCVVLStSGGKWNDVS 114
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1914-2082 1.06e-16

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 79.81  E-value: 1.06e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNaGENSFDRVSELIYNMQYIGIDGQ 1993
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN-DSRSKDALLEALASLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092   1994 NVTAGLQYALDYYDLPSQGYRtgSDVRHLLVYVTQTNPTDA--DPSELLRTIKRSGLyEVVVVAL----DMQPSDKLTNM 2067
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGpkDLLKAAKELKRSGV-KVFVVGVgndvDEEELKKLASA 156

                           170
                    ....*....|....*
gi 193211092   2068 VNPRCFYLAQDFHDL 2082
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1134-1249 6.57e-16

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: 75.73  E-value: 6.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1134 NCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI---GSYRVWIGLAFN--NGQWYWDvpDGNfaqPLTGYT 1208
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLssEGTWKWS--DGS---PLVDYT 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193211092 1209 NWAPNVDPTNPAYNHAVINSN--GKWEPADPNDaaNNFAACMK 1249
Cdd:cd00037    76 NWAPGEPNPGGSEDCVVLSSSsdGKWNDVSCSS--KLPFICEK 116
VWA pfam00092
von Willebrand factor type A domain;
1914-2079 1.25e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 65.37  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1914 DTLFLIDSSlkdSNVT---FRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAGENSfDRVSELIYNMQYIGI 1990
Cdd:pfam00092    1 DIVFLLDGS---GSIGgdnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSK-EELLSAVDNLRYLGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1991 DGQNVTAGLQYALDYYDLPSQGYRTGsdVRHLLVYVTQTNPTDADPSELLRTIKRSGlYEVVVVALDMQPSDKLTNMV-- 2068
Cdd:pfam00092   77 GTTNTGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDGDPEEVARELKSAG-VTVFAVGVGNADDEELRKIAse 153

                          170
                   ....*....|..
gi 193211092  2069 -NPRCFYLAQDF 2079
Cdd:pfam00092  154 pGEGHVFTVSDF 165
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1142-1233 5.09e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 58.64  E-value: 5.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092  1142 KLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSYRV--WIGLAF--NNGQWYWDvpDGNfaqPLTgYTNWAPNVDPT 1217
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfWIGLTDrkNEGTWKWV--DGS---PVN-YTNWAPEPNNN 74

                           90
                   ....*....|....*..
gi 193211092  1218 NPAYNHAVIN-SNGKWE 1233
Cdd:pfam00059   75 GENEDCVELSsSSGKWN 91
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1128-1193 1.94e-09

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: 57.34  E-value: 1.94e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193211092 1128 WNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSYRVWIGLAFN--NGQWYW 1193
Cdd:cd03593     5 WICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREksEKPWKW 72
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1136-1243 2.09e-09

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: 57.05  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1136 FTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSY-RVWIGL--AFNNGQWYWDvpDGnfaqPLTGYTNWAP 1212
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYgASWIGAsdAATEGTWKWS--DG----EESTYTNWGS 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 193211092 1213 NVDPTNP------AYNHAVINSNGKWepadpNDAANN 1243
Cdd:cd03603    77 GEPHNNGggnedyAAINHFPGISGKW-----NDLANS 108
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1127-1213 7.36e-07

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: 50.43  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1127 FWNHRQQNCFTFTADKLSWLDTWDMCH-----AQKAYLLHIDSQATNDYV-------ASQIGSYRVWIGL--AFNNGQWY 1192
Cdd:cd03589     4 FWTAFGGYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVydlfessRGPDTPYGLWIGLhdRTSEGPFE 83

                          90       100
                  ....*....|....*....|.
gi 193211092 1193 WDvpDGNfaqPLtGYTNWAPN 1213
Cdd:cd03589    84 WT--DGS---PV-DFTKWAGG 98
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1128-1245 1.16e-06

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: 49.61  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1128 WNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQI-GSYRVWIGL--AFNNGQWYWdVpDGnfaQPL 1204
Cdd:cd03590     5 WKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLsdEETEGEWKW-V-DG---TPL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 193211092 1205 -TGYTNWAPNvDPTNpaYNH-----AVINSN-GKWepadpNDAANNFA 1245
Cdd:cd03590    80 nSSKTFWHPG-EPNN--WGGggedcAELVYDsGGW-----NDVPCNLE 119
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1138-1247 5.33e-05

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: 44.29  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1138 FTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSYRV---WIGLAFNNGQWYWDVPDGNfaqPLTgYTNWAPNv 1214
Cdd:cd03592     5 YSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKK---ELE-YKNWAPG- 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 193211092 1215 DPTNPAYNHAV---INSNGKWEpaDPNDAANNFAAC 1247
Cdd:cd03592    80 EPNNGRNENCLeiyIKDNGKWN--DEPCSKKKSAIC 113
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1484-1660 1.93e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 44.09  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1484 LVLMLETSYNMGSSIFQLKKN-LKASLDSINNDPTTqgwfTNFVLYPFDstSNKDSWYPPTISRNSDDIVTALKNISTMS 1562
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEaLKALVSSLSASPPG----DRVGLVTFG--SNARVVLPLTTDTDKADLLEAIDALKKGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1563 CPGSAPCSSqcprpiVSVLSSILDMNALAAPNSVIVVITRSSPEDYLQ-VGQISQKLQTKKAYINFVfpAIDSpcgegwn 1641
Cdd:cd00198    77 GGGTNIGAA------LRLALELLKSAKRPNARRVIILLTDGEPNDGPElLAEAARELRKLGITVYTI--GIGD------- 141

                         170
                  ....*....|....*....
gi 193211092 1642 SPNTDALFQIISYSQGNTF 1660
Cdd:cd00198   142 DANEDELKEIADKTTGGAV 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1914-2064 3.14e-03

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 40.29  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1914 DTLFLIDSS--LKDSNvtFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAgENSFDRVSELIYNMQYIGiD 1991
Cdd:cd01472     2 DIVFLVDGSesIGLSN--FNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNT-YRSKDDVLEAVKNLRYIG-G 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193211092 1992 GQNVTAGLQYALDYYDLPSQGYRTGsdVRHLLVYVTQTNPTDaDPSELLRTIKRSGlYEVVVVALDMQPSDKL 2064
Cdd:cd01472    78 GTNTGKALKYVRENLFTEASGSREG--VPKVLVVITDGKSQD-DVEEPAVELKQAG-IEVFAVGVKNADEEEL 146
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1128-1213 4.15e-03

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 39.48  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1128 WNHRQQNCFTFTADKLSWLDTWDMCHAQKAYLLHIDSQATNDYVASQIGSYRvWIGLAFN--NGQWYWDvpDGNFAQplt 1205
Cdd:cd03588     5 WDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-WIGLNDRtiEGDFRWS--DGHPLQ--- 78


                  ....*...
gi 193211092 1206 gYTNWAPN 1213
Cdd:cd03588    79 -FENWRPN 85
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1914-2079 4.22e-03

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 40.00  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1914 DTLFLIDSSLKDSNVTFRILQQFAVQAVQPFNYVSGLGQVAALRVADKAYGGFSYNAGENSFDrVSELIYNMQYIGIDGQ 1993
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKAD-VLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211092 1994 NVTAGLQYALDYYDLPSQGYRTGSDVRHLLVYVTQTNPTDaDPSELLRTIKRSGLYEVVVVALDMQPSDKLTNMVNPRCF 2073
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQD-DVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFV 159


                  ....*.
gi 193211092 2074 YLAQDF 2079
Cdd:cd01481   160 FQVSDF 165
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH