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Conserved domains on  [gi|17533687|ref|NP_496745|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10844887)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
13-200 1.09e-89

VWA F09G8.8 type: 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


:

Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 268.14  E-value: 1.09e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  13 SPTLSVSDRRCGTNANKLWLDVVFVIDNCKIGS---MNLVYQTISSLFSKQLQIGTGYDDPRSTRVGFITYNWNATDVAD 89
Cdd:cd01477   1 SPAAAYTDRECGSDIKNLWLDIVFVVDNSKGMTqggLWQVRATISSLFGSSSQIGTDYDDPRSTRVGLVTYNSNATVVAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  90 FYKLQSWADLNSQIQRlQYTPQSSSPASRMDTGLNAAIGMIDAT-AGFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKS 168
Cdd:cd01477  81 LNDLQSFDDLYSQIQG-SLTDVSSTNASYLDTGLQAAEQMLAAGkRTSRENYKKVVIVFASDYNDEGSNDPRPIAARLKS 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 17533687 169 RGIPVVTVNTGS--SSDTQAYLKQIASDNMSFAI 200
Cdd:cd01477 160 TGIAIITVAFTQdeSSNLLDKLGKIASPGMNFTS 193
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
220-359 4.23e-09

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: 54.14  E-value: 4.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    220 CEQGWVQYNypwnnlqnryGTCLYTDTTDYSsRDGAKSKCRQYSpkSYLVNELDQQKRDFNFNLVNSDStkPVNAFYNGL 299
Cdd:smart00034   1 CPSGWISYG----------GKCYKFSTEKKT-WEDAQAFCQSLG--GHLASIHSEAENDFVASLLKNSG--SSDYYWIGL 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533687    300 --LNLNGNWYWDqpnDRSPIPLDPN--SGAPPTRNA-CVAdMKYSDGTtaWTPVSCANNFRFICE 359
Cdd:smart00034  66 sdPDSNGSWQWS---DGSGPVSYSNwaPGEPNNSSGdCVV-LSTSGGK--WNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
13-200 1.09e-89

VWA F09G8.8 type: 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 268.14  E-value: 1.09e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  13 SPTLSVSDRRCGTNANKLWLDVVFVIDNCKIGS---MNLVYQTISSLFSKQLQIGTGYDDPRSTRVGFITYNWNATDVAD 89
Cdd:cd01477   1 SPAAAYTDRECGSDIKNLWLDIVFVVDNSKGMTqggLWQVRATISSLFGSSSQIGTDYDDPRSTRVGLVTYNSNATVVAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  90 FYKLQSWADLNSQIQRlQYTPQSSSPASRMDTGLNAAIGMIDAT-AGFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKS 168
Cdd:cd01477  81 LNDLQSFDDLYSQIQG-SLTDVSSTNASYLDTGLQAAEQMLAAGkRTSRENYKKVVIVFASDYNDEGSNDPRPIAARLKS 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 17533687 169 RGIPVVTVNTGS--SSDTQAYLKQIASDNMSFAI 200
Cdd:cd01477 160 TGIAIITVAFTQdeSSNLLDKLGKIASPGMNFTS 193
VWA pfam00092
von Willebrand factor type A domain;
33-212 4.32e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.23  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    33 DVVFVIDNCkiGSM-----NLVYQTISSLFSkQLQIGtgyddPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQ 107
Cdd:pfam00092   1 DIVFLLDGS--GSIggdnfEKVKEFLKKLVE-SLDIG-----PDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687   108 YtpqSSSPASRMDTGLNAAIG-MIDATAGFRDNYKKIVIVFTSvhGSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDTQa 186
Cdd:pfam00092  73 Y---LGGGTTNTGKALKYALEnLFSSAAGARPGAPKVVVLLTD--GRSQDGDPEEVARELKSAGVTVFAVGVGNADDEE- 146
                         170       180
                  ....*....|....*....|....*....
gi 17533687   187 yLKQIASDN---MSFAIADGNVTQEILKA 212
Cdd:pfam00092 147 -LRKIASEPgegHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
33-213 5.89e-29

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: 110.62  E-value: 5.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687     33 DVVFVIDNckIGSMNLVYQTISSLFSKQLqIGTGYDDPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQYTPQS 112
Cdd:smart00327   1 DVVFLLDG--SGSMGGNRFELAKEFVLKL-VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    113 SSPasrMDTGLNAAIGMI-DATAGFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDtQAYLKQI 191
Cdd:smart00327  78 GTN---LGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD-EEELKKL 153
                          170       180
                   ....*....|....*....|..
gi 17533687    192 ASDNMSFAIADGNVTQEILKAM 213
Cdd:smart00327 154 ASAPGGVYVFLPELLDLLIDLL 175
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
220-359 4.23e-09

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: 54.14  E-value: 4.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    220 CEQGWVQYNypwnnlqnryGTCLYTDTTDYSsRDGAKSKCRQYSpkSYLVNELDQQKRDFNFNLVNSDStkPVNAFYNGL 299
Cdd:smart00034   1 CPSGWISYG----------GKCYKFSTEKKT-WEDAQAFCQSLG--GHLASIHSEAENDFVASLLKNSG--SSDYYWIGL 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533687    300 --LNLNGNWYWDqpnDRSPIPLDPN--SGAPPTRNA-CVAdMKYSDGTtaWTPVSCANNFRFICE 359
Cdd:smart00034  66 sdPDSNGSWQWS---DGSGPVSYSNwaPGEPNNSSGdCVV-LSTSGGK--WNDVSCTSKLPFVCE 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
32-192 1.04e-08

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 55.71  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDnckI-GSM------NLVYQTISSLFSkqlqigtgyDDPRSTRVGFITYNWNATDVADFykLQSWADLNSQIQ 104
Cdd:COG1240  93 RDVVLVVD---AsGSMaaenrlEAAKGALLDFLD---------DYRPRDRVGLVAFGGEAEVLLPL--TRDREALKRALD 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 105 RLQ---YTPqssspasrMDTGLNAAIGMIDAtagFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKSRGIPVVTVNTGSS 181
Cdd:COG1240 159 ELPpggGTP--------LGDALALALELLKR---ADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE 227
                       170
                ....*....|.
gi 17533687 182 SDTQAYLKQIA 192
Cdd:COG1240 228 AVDEGLLREIA 238
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
247-360 6.24e-05

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: 41.84  E-value: 6.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 247 TDYSSRDGAKSKCRQYSpkSYLVNELDQQKRDFNFNLVNSDSTKPvnaFYNGL--LNLNGNWYWDqpnDRSPIP----LD 320
Cdd:cd00037   7 TEKLTWEEAQEYCRSLG--GHLASIHSEEENDFLASLLKKSSSSD---VWIGLndLSSEGTWKWS---DGSPLVdytnWA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17533687 321 PNSGAPPTRNACVADMKYSDGTtaWTPVSCANNFRFICEQ 360
Cdd:cd00037  79 PGEPNPGGSEDCVVLSSSSDGK--WNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
253-360 1.19e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 38.23  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687   253 DGAKSKCRQYSpkSYLVNELDQQKRDFnfnlVNSDSTKPVNAFYNGL--LNLNGNWYWDQPNDRSPIPLDPNSGAPPTRN 330
Cdd:pfam00059   5 DEAREACRKLG--GHLVSINSAEELDF----LSSTLKKSNKYFWIGLtdRKNEGTWKWVDGSPVNYTNWAPEPNNNGENE 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 17533687   331 ACVAdMKYSDGTtaWTPVSCANNFRFICEQ 360
Cdd:pfam00059  79 DCVE-LSSSSGK--WNDENCNSKNPFVCEK 105
 
Name Accession Description Interval E-value
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
13-200 1.09e-89

VWA F09G8.8 type: 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 268.14  E-value: 1.09e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  13 SPTLSVSDRRCGTNANKLWLDVVFVIDNCKIGS---MNLVYQTISSLFSKQLQIGTGYDDPRSTRVGFITYNWNATDVAD 89
Cdd:cd01477   1 SPAAAYTDRECGSDIKNLWLDIVFVVDNSKGMTqggLWQVRATISSLFGSSSQIGTDYDDPRSTRVGLVTYNSNATVVAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  90 FYKLQSWADLNSQIQRlQYTPQSSSPASRMDTGLNAAIGMIDAT-AGFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKS 168
Cdd:cd01477  81 LNDLQSFDDLYSQIQG-SLTDVSSTNASYLDTGLQAAEQMLAAGkRTSRENYKKVVIVFASDYNDEGSNDPRPIAARLKS 159
                       170       180       190
                ....*....|....*....|....*....|....
gi 17533687 169 RGIPVVTVNTGS--SSDTQAYLKQIASDNMSFAI 200
Cdd:cd01477 160 TGIAIITVAFTQdeSSNLLDKLGKIASPGMNFTS 193
VWA pfam00092
von Willebrand factor type A domain;
33-212 4.32e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 121.23  E-value: 4.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    33 DVVFVIDNCkiGSM-----NLVYQTISSLFSkQLQIGtgyddPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQ 107
Cdd:pfam00092   1 DIVFLLDGS--GSIggdnfEKVKEFLKKLVE-SLDIG-----PDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687   108 YtpqSSSPASRMDTGLNAAIG-MIDATAGFRDNYKKIVIVFTSvhGSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDTQa 186
Cdd:pfam00092  73 Y---LGGGTTNTGKALKYALEnLFSSAAGARPGAPKVVVLLTD--GRSQDGDPEEVARELKSAGVTVFAVGVGNADDEE- 146
                         170       180
                  ....*....|....*....|....*....
gi 17533687   187 yLKQIASDN---MSFAIADGNVTQEILKA 212
Cdd:pfam00092 147 -LRKIASEPgegHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
32-194 1.39e-29

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: 111.61  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDNCK-IGS--MNLVYQTISSLFSKqLQIGtgyddPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQY 108
Cdd:cd01450   1 LDIVFLLDGSEsVGPenFEKVKDFIEKLVEK-LDIG-----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 109 tpqSSSPASRMDTGLNAAIGMIDATAGFRDNYKKIVIVFTSVHgSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDTQayL 188
Cdd:cd01450  75 ---LGGGGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGR-SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEE--L 148

                ....*.
gi 17533687 189 KQIASD 194
Cdd:cd01450 149 REIASC 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
33-213 5.89e-29

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: 110.62  E-value: 5.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687     33 DVVFVIDNckIGSMNLVYQTISSLFSKQLqIGTGYDDPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQYTPQS 112
Cdd:smart00327   1 DVVFLLDG--SGSMGGNRFELAKEFVLKL-VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    113 SSPasrMDTGLNAAIGMI-DATAGFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDtQAYLKQI 191
Cdd:smart00327  78 GTN---LGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVD-EEELKKL 153
                          170       180
                   ....*....|....*....|..
gi 17533687    192 ASDNMSFAIADGNVTQEILKAM 213
Cdd:smart00327 154 ASAPGGVYVFLPELLDLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
32-200 1.61e-16

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: 76.07  E-value: 1.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDNCkiGSM-----NLVYQTISSLFSkQLQIGtgyddPRSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRL 106
Cdd:cd00198   1 ADIVFLLDVS--GSMggeklDKAKEALKALVS-SLSAS-----PPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 107 QYTPQSSSpasRMDTGLNAAIGMIDATAgfRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKSRGIPVVTVNTGSSSDTQA 186
Cdd:cd00198  73 KKGLGGGT---NIGAALRLALELLKSAK--RPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDE 147
                       170
                ....*....|....
gi 17533687 187 yLKQIASDNMSFAI 200
Cdd:cd00198 148 -LKEIADKTTGGAV 160
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
220-359 4.23e-09

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: 54.14  E-value: 4.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687    220 CEQGWVQYNypwnnlqnryGTCLYTDTTDYSsRDGAKSKCRQYSpkSYLVNELDQQKRDFNFNLVNSDStkPVNAFYNGL 299
Cdd:smart00034   1 CPSGWISYG----------GKCYKFSTEKKT-WEDAQAFCQSLG--GHLASIHSEAENDFVASLLKNSG--SSDYYWIGL 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17533687    300 --LNLNGNWYWDqpnDRSPIPLDPN--SGAPPTRNA-CVAdMKYSDGTtaWTPVSCANNFRFICE 359
Cdd:smart00034  66 sdPDSNGSWQWS---DGSGPVSYSNwaPGEPNNSSGdCVV-LSTSGGK--WNDVSCTSKLPFVCE 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
32-192 1.04e-08

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 55.71  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDnckI-GSM------NLVYQTISSLFSkqlqigtgyDDPRSTRVGFITYNWNATDVADFykLQSWADLNSQIQ 104
Cdd:COG1240  93 RDVVLVVD---AsGSMaaenrlEAAKGALLDFLD---------DYRPRDRVGLVAFGGEAEVLLPL--TRDREALKRALD 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 105 RLQ---YTPqssspasrMDTGLNAAIGMIDAtagFRDNYKKIVIVFTSVHGSYKSNQPRDVSKILKSRGIPVVTVNTGSS 181
Cdd:COG1240 159 ELPpggGTP--------LGDALALALELLKR---ADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE 227
                       170
                ....*....|.
gi 17533687 182 SDTQAYLKQIA 192
Cdd:COG1240 228 AVDEGLLREIA 238
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
32-179 6.00e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 45.85  E-value: 6.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDNCkiGSMNLVYQ---TISSLFSKQLQIGtgyddPRSTRVGFITYNWNATDVADFyKLQSWADLNSQIQRLQY 108
Cdd:cd01476   1 LDLLFVLDSS--GSVRGKFEkykKYIERIVEGLEIG-----PTATRVALITYSGRGRQRVRF-NLPKHNDGEELLEKVDN 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17533687 109 TPqSSSPASRMDTGLNAAIGMIDATAGFRDNYKKIVIVFTSVHgSYKSnqPRDVSKILKSR-GIPVVTVNTG 179
Cdd:cd01476  73 LR-FIGGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGR-SHDD--PEKQARILRAVpNIETFAVGTG 140
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
247-360 6.24e-05

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: 41.84  E-value: 6.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 247 TDYSSRDGAKSKCRQYSpkSYLVNELDQQKRDFNFNLVNSDSTKPvnaFYNGL--LNLNGNWYWDqpnDRSPIP----LD 320
Cdd:cd00037   7 TEKLTWEEAQEYCRSLG--GHLASIHSEEENDFLASLLKKSSSSD---VWIGLndLSSEGTWKWS---DGSPLVdytnWA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17533687 321 PNSGAPPTRNACVADMKYSDGTtaWTPVSCANNFRFICEQ 360
Cdd:cd00037  79 PGEPNPGGSEDCVVLSSSSDGK--WNDVSCSSKLPFICEK 116
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
32-222 9.95e-05

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 43.14  E-value: 9.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDNCK-IGSMN--LVYQTISSLFSKqLQIGtgyddPRSTRVGFITYnwnATDVADFYKLQSW---ADLNSQIQR 105
Cdd:cd01475   3 TDLVFLIDSSRsVRPENfeLVKQFLNQIIDS-LDVG-----PDATRVGLVQY---SSTVKQEFPLGRFkskADLKRAVRR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 106 LQYTPQSSspasrMdTGL------NAAIGMIDATAGFRDNYKKIVIVFTSvhGSYKSNQpRDVSKILKSRGIPVVTVNTG 179
Cdd:cd01475  74 MEYLETGT-----M-TGLaiqyamNNAFSEAEGARPGSERVPRVGIVVTD--GRPQDDV-SEVAAKARALGIEMFAVGVG 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 17533687 180 SSSDTQayLKQIASDNMS---FAIADGNVTQEILKAMtdTNCFCEQ 222
Cdd:cd01475 145 RADEEE--LREIASEPLAdhvFYVEDFSTIEELTKKF--QGKICVV 186
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
33-194 4.11e-04

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: 40.67  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  33 DVVFVIDNC-KIGSMNlvYQTISSLFSK---QLQIGTGyddprSTRVGFITYNWNATDVADFYKLQSWADLNSQIQRLQY 108
Cdd:cd01472   2 DIVFLVDGSeSIGLSN--FNLVKDFVKRvveRLDIGPD-----GVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687 109 TpqssspASRMDTG--LNAAIG-MIDATAGFRDNYKKIVIVFTSVHGSYKSNQPrdvSKILKSRGIPVVTVNTGSSSDTQ 185
Cdd:cd01472  75 I------GGGTNTGkaLKYVREnLFTEASGSREGVPKVLVVITDGKSQDDVEEP---AVELKQAGIEVFAVGVKNADEEE 145

                ....*....
gi 17533687 186 ayLKQIASD 194
Cdd:cd01472 146 --LKQIASD 152
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
32-180 5.00e-04

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 40.83  E-value: 5.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687  32 LDVVFVIDNC-KIGSMNLVYQTISSL--FSKQLQIGtgyddPRSTRVGFITYnwnATDVADFYKLQSWADLNSQ-----I 103
Cdd:cd01471   1 LDLYLLVDGSgSIGYSNWVTHVVPFLhtFVQNLNIS-----PDEINLYLVTF---STNAKELIRLSSPNSTNKDlalnaI 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17533687 104 QRLQYTPqssSPASRMDT--GLNAAIGMIDATAGFRDNYKKIVIVFTSVHGSYKSnQPRDVSKILKSRGIPVVTVNTGS 180
Cdd:cd01471  73 RALLSLY---YPNGSTNTtsALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKF-RTLKEARKLRERGVIIAVLGVGQ 147
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
253-360 1.19e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 38.23  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533687   253 DGAKSKCRQYSpkSYLVNELDQQKRDFnfnlVNSDSTKPVNAFYNGL--LNLNGNWYWDQPNDRSPIPLDPNSGAPPTRN 330
Cdd:pfam00059   5 DEAREACRKLG--GHLVSINSAEELDF----LSSTLKKSNKYFWIGLtdRKNEGTWKWVDGSPVNYTNWAPEPNNNGENE 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 17533687   331 ACVAdMKYSDGTtaWTPVSCANNFRFICEQ 360
Cdd:pfam00059  79 DCVE-LSSSSGK--WNDENCNSKNPFVCEK 105
 
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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