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Conserved domains on  [gi|223029386|ref|NP_001138368|]
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CD209 antigen isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 232-355 1.19e-60

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: 191.36  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 311
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 223029386 312 LPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 355
Cdd:cd03590   80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
43-201 5.01e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  43 ISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELpEKSKLQEI 122
Cdd:COG3206  235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAAL-RAQLQQEA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 123 YQELTWLKAAVGELpeKSKMQEIYQELTRLKAAVGELPEKSKQqeiYQELTRlkaavgelpEKSKQQEIYQE-LTRLKAA 201
Cdd:COG3206  312 QRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER---------EVEVARELYESlLQRLEEA 377
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 232-355 1.19e-60

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: 191.36  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 311
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 223029386 312 LPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 355
Cdd:cd03590   80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 232-354 1.52e-37

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: 131.57  E-value: 1.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFTWMGLSDLNQEGTWQWVDGS 309
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 223029386   310 PLLPSFkqYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWICK 354
Cdd:smart00034  81 GPVSYS--NWAPGEPNN-SSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 250-355 1.17e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 102.17  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  250 QRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFkqyWNRGEPNNVGE 329
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 223029386  330 EDCAE--FSGNGWNDDKCNLAKFWICKK 355
Cdd:pfam00059  78 EDCVElsSSSGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 232-356 1.39e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.60  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 311
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 223029386 312 LPSFKQywnrgepnnVGEEDCAEFSGNGWNDDKCNLAKFWICKKS 356
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSKT 201
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 213-368 1.43e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 66.26  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   213 EIYQELTQLKAAVERLCHP-CPWEWTFFQGN--CYFMSNSQRNWHDSITACKE-VGAQLVVIKSAEEQNFLQLQSSRS-N 287
Cdd:TIGR00864  298 DAAWKITAHGEEPAKASHPhCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   288 RFTWMGLSDLN--QEGTWQWVDGSPLLPSfkQYWNRGEPNNVGEEDCAEFSGNGW-NDDKCNLAKFWICKKSAASCSRDE 364
Cdd:TIGR00864  378 RGVWIGFSDVNgaEKGPAHQGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCELNPGGPVPDA 455


                   ....
gi 223029386   365 EQFL 368
Cdd:TIGR00864  456 ENFA 459
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
43-201 5.01e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  43 ISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELpEKSKLQEI 122
Cdd:COG3206  235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAAL-RAQLQQEA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 123 YQELTWLKAAVGELpeKSKMQEIYQELTRLKAAVGELPEKSKQqeiYQELTRlkaavgelpEKSKQQEIYQE-LTRLKAA 201
Cdd:COG3206  312 QRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER---------EVEVARELYESlLQRLEEA 377
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
36-228 1.62e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  36 VSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAA-VGELP 114
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELR 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 115 EKSKLQEIY-QELTWLKAAVGELPEK-SKMQEIYQELTRLKAAVGELPEKskqQEIYQELTRLKAAVGELPEKSKQ---Q 189
Cdd:PRK03918 311 EIEKRLSRLeEEINGIEERIKELEEKeERLEELKKKLKELEKRLEELEER---HELYEEAKAKKEELERLKKRLTGltpE 387

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 223029386 190 EIYQELTRLKAAVGELPEK-----SKQQEIYQELTQLKAAVERL 228
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431
CoV_Spike_S1-S2_S2 cd21698
S1/S2 cleavage region and the S2 fusion subunit of coronavirus spike (S) proteins; This model ...
 9-87 7.74e-03

S1/S2 cleavage region and the S2 fusion subunit of coronavirus spike (S) proteins; This model represents the S1/S2 cleavage region and the S2 subunit of the spike (S) glycoprotein from coronavirus (CoVs), including three highly pathogenic human CoVs, Middle East respiratory syndrome coronavirus (MERS-CoV), Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV), and SARS coronavirus 2 (SARS-CoV-2), also known as a 2019 novel coronavirus (2019-nCoV). The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect S1 and S2. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV, and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP), and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. Notably, SARS-CoV-2 has a functional polybasic (furin) cleavage site through the insertion of PRRAR*SV (* indicates the cleavage site) at the S1/S2 interface, which is absent in SARS-CoV and other SARS-related CoVs. The S1/S2 cleavage region and the S2 fusion subunit play an essential role in viral entry by initiating fusion of the viral and cellular membranes.


Pssm-ID: 411955 [Multi-domain]  Cd Length: 523  Bit Score: 38.17  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   9 LQQLGLLEEEQLRGLGFRQTRGYKSLAVSKVPSSIsqeQSRQDAIYQNLTQLKAAVGELSEK-----SKLQEIYQELTQL 83
Cdd:cd21698  228 LQQNVLLENQKLLANSFNKAIGNISDAFSSTSSAL---QKIQDVVNQQAQALNTLTSQLSNNfgaisSSIQDIYQRLDKL 304


                 ....
gi 223029386  84 KAAV 87
Cdd:cd21698  305 EADV 308
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 232-355 1.19e-60

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: 191.36  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 311
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 223029386 312 LPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 355
Cdd:cd03590   80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 232-354 1.52e-37

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: 131.57  E-value: 1.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFTWMGLSDLNQEGTWQWVDGS 309
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 223029386   310 PLLPSFkqYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWICK 354
Cdd:smart00034  81 GPVSYS--NWAPGEPNN-SSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 242-355 5.29e-36

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: 127.35  E-value: 5.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 242 NCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQ-LQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFkqYWN 320
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYT--NWA 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 223029386 321 RGEPNNVGEEDCAEFSGN---GWNDDKCNLAKFWICKK 355
Cdd:cd00037   79 PGEPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFICEK 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 232-355 1.02e-29

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: 110.88  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 311
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 223029386 312 LPSFKqywnrgEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKK 355
Cdd:cd03593   79 NNLFN------IRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 232-354 9.61e-28

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: 106.29  E-value: 9.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVG-----AQLVVIKSAEEQNFL--QLQSSRSNRFT---WMGLSDLNQEG 301
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVydLFESSRGPDTPyglWIGLHDRTSEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223029386 302 TWQWVDGSPLlpSFkQYWNRGEPNN-VGEEDCAEFSGNG-----WNDDKCNLAKFWICK 354
Cdd:cd03589   81 PFEWTDGSPV--DF-TKWAGGQPDNyGGNEDCVQMWRRGdagqsWNDMPCDAVFPYICK 136
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 250-355 1.17e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 102.17  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  250 QRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFkqyWNRGEPNNVGE 329
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 223029386  330 EDCAE--FSGNGWNDDKCNLAKFWICKK 355
Cdd:pfam00059  78 EDCVElsSSSGKWNDENCNSKNPFVCEK 105
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 244-353 1.56e-22

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 91.20  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 244 YFMSNSQR-NWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLlpSFKQyWNRG 322
Cdd:cd03591    3 IFVTNGEEkNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPL--TYTN-WKPG 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 223029386 323 EPNNVG-EEDCAE-FSGNGWNDDKCNLAKFWIC 353
Cdd:cd03591   80 EPNNAGgGEDCVEmYTSGKWNDVACNLTRLFVC 112
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 244-353 3.71e-19

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: 82.04  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 244 YFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFL-QLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLlpSFKQyWNRG 322
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINNEGTWVDTDKKEL--EYKN-WAPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 223029386 323 EPNNVGEEDCAE----FSGNgWNDDKCNLAKFWIC 353
Cdd:cd03592   80 EPNNGRNENCLEiyikDNGK-WNDEPCSKKKSAIC 113
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 232-355 3.17e-18

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: 79.93  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLqlqSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 311
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 223029386 312 LpsFKQyWNRGEPNN--VGEEDCAEFSGNG---WNDDKCNLAKFWICKK 355
Cdd:cd03588   78 Q--FEN-WRPNQPDNffATGEDCVVMIWHEegeWNDVPCNYHLPFTCKK 123
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 232-354 5.98e-16

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 73.56  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEV--GAQLVVIKSAEEQNFLQ---LQSSRSNRFTWMGLSDLNQEGTWQWV 306
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLHDPQQSRGWEWS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223029386 307 DGSPLLPSfkqYWNRGEPNNVGEEdCAEFSGNG----WNDDKCNLAKFWICK 354
Cdd:cd03594   81 DGSKLDYR---SWDRNPPYARGGY-CAELSRSTgflkWNDANCEERNPFICK 128
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 252-342 8.93e-15

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: 70.15  E-value: 8.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 252 NWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNrFTWMGLSDLNQEGTWQWVDGSPLLPSFkqyWNRGEP------- 324
Cdd:cd03603   11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTN---WGSGEPhnngggn 86

                         90
                 ....*....|....*....
gi 223029386 325 -NNVGEEDCAEFSGnGWND 342
Cdd:cd03603   87 eDYAAINHFPGISG-KWND 104
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 243-353 4.92e-13

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 65.49  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 243 CYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQ---LQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLlpSFKQyW 319
Cdd:cd03596   11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEGKWVDVNGSPI--SYFN-W 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 223029386 320 NR---GEPNNVGEEDCAEFSG--NG-WNDDKCNLAKFWIC 353
Cdd:cd03596   88 EReitAQPDGGKRENCVALSSsaQGkWFDEDCRREKPYVC 127
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 232-356 1.39e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.60  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 311
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 223029386 312 LPSFKQywnrgepnnVGEEDCAEFSGNGWNDDKCNLAKFWICKKS 356
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSKT 201
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 213-368 1.43e-11

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 66.26  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   213 EIYQELTQLKAAVERLCHP-CPWEWTFFQGN--CYFMSNSQRNWHDSITACKE-VGAQLVVIKSAEEQNFLQLQSSRS-N 287
Cdd:TIGR00864  298 DAAWKITAHGEEPAKASHPhCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   288 RFTWMGLSDLN--QEGTWQWVDGSPLLPSfkQYWNRGEPNNVGEEDCAEFSGNGW-NDDKCNLAKFWICKKSAASCSRDE 364
Cdd:TIGR00864  378 RGVWIGFSDVNgaEKGPAHQGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCELNPGGPVPDA 455


                   ....
gi 223029386   365 EQFL 368
Cdd:TIGR00864  456 ENFA 459
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 244-353 1.49e-10

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 57.77  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 244 YFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDlnQEGTWQWVDGSPLLPSfkqYWNRGE 323
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYR--DVDSWRWSDGSESSFR---NWNTFQ 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 223029386 324 PNnvGEEDCAEFSGNG-WNDDKCNLAKFWIC 353
Cdd:cd03602   78 PF--GQGDCATMYSSGrWYAALCSALKPFIC 106
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 232-353 1.40e-08

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 53.33  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNF----LQLQSsrsnrfTWMGLSDLNQEGTWQWVD 307
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFvsryKGGQD------LWIGIEKKKGDDDDREVL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 223029386 308 GSPLLPSfkqywnrgepnnvGEEDCAEFSGNGWNDDKCNLAKFWIC 353
Cdd:PHA03097 120 DKVVKPP-------------KSGKCAYLKDKTIISSNCNATKGWIC 152
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 241-353 1.01e-07

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 50.14  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 241 GNCYFMSNSQRNWHDSITACKEV-GAQLVVIKSAEEQNFLQLQSSRSNR-FTWMGLSDLNQEGTWQ--WVDGSPLLPSfk 316
Cdd:cd03598    1 GRCYRFVKSPRTFRDAQVICRRCyRGNLASIHSFAFNYRVQRLVSTLNQaQVWIGGIITGKGRCRRfsWVDGSVWNYA-- 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 223029386 317 qYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWIC 353
Cdd:cd03598   79 -YWAPGQPGN-RRGHCVELCTRGghWRRAHCKLRRPFIC 115
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 244-354 4.59e-07

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 49.12  E-value: 4.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 244 YFMSNSQR-NWHDSITACKEVGAQLVVIKSAEEQ----NFLQLQSSRSNRFtWMGL---SDLNQEGT-----WQWVDGSP 310
Cdd:cd03595   17 YFQDSRRRlNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDF-WIGLrrsSQYNVTSSacsslYYWLDGSI 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223029386 311 llPSFKQyWNRGEPNnVGEEDCAEF-------SGNG------WNDDKCNLAKFWICK 354
Cdd:cd03595   96 --STFRN-WYVDEPS-CGSEVCVVMyhqpsapAGQGgpylfqWNDDNCNMKNNFICK 148
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
43-201 5.01e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  43 ISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELpEKSKLQEI 122
Cdd:COG3206  235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAAL-RAQLQQEA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 123 YQELTWLKAAVGELpeKSKMQEIYQELTRLKAAVGELPEKSKQqeiYQELTRlkaavgelpEKSKQQEIYQE-LTRLKAA 201
Cdd:COG3206  312 QRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER---------EVEVARELYESlLQRLEEA 377
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
71-220 7.05e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  71 SKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGEL-----PEKSKMQEI 145
Cdd:COG3206  219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytPNHPDVIAL 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 146 YQELTRLKAAVgelpekskQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEKSKQ-----------QEI 214
Cdd:COG3206  297 RAQIAALRAQL--------QQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAElrrlerevevaREL 366


                 ....*.
gi 223029386 215 YQELTQ 220
Cdd:COG3206  367 YESLLQ 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
56-228 2.00e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  56 NLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGElpeksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGE 135
Cdd:COG4717   69 NLKELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 136 LPEksKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELpeKSKQQEIY 215
Cdd:COG4717  144 LPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQ 219

                        170
                 ....*....|...
gi 223029386 216 QELTQLKAAVERL 228
Cdd:COG4717  220 EELEELEEELEQL 232
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 252-355 6.28e-06

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 44.83  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 252 NWHDSITACKEVGAQLVVIKS--AEEQNFLQLQSSRSNRFTWMGLSDL-NQEGTWQWVDGSpLLPSFKQYWNRGEPNN-V 327
Cdd:cd03601   11 NYAKAGAFCRSRGMRLASLAMrdSEMRDAILAFTLVKGHGYWVGADNLqDGEYDFLWNDGV-SLPTDSDLWAPNEPSNpQ 89

                         90       100       110
                 ....*....|....*....|....*....|
gi 223029386 328 GEEDCAE--FSGNGWNDDKCNLAKFWICKK 355
Cdd:cd03601   90 SRQLCVQlwSKYNLLDDEYCGRAKRVICEK 119
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
55-228 1.88e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  55 QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQ 124
Cdd:COG4717  319 EELEELLAALGlppdlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQ 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 125 ELtwlkaavgelpeKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKskQQEIYQELTRLKAAVGE 204
Cdd:COG4717  399 EL------------KEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE--LEELREELAELEAELEQ 464

                        170       180
                 ....*....|....*....|....
gi 223029386 205 LPEKSKQQEIYQELTQLKAAVERL 228
Cdd:COG4717  465 LEEDGELAELLQELEELKAELREL 488
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
43-200 4.27e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  43 ISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPEKSKLQEI 122
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAE 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029386 123 YQELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKA 200
Cdd:COG4717  175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
36-228 1.62e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  36 VSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAA-VGELP 114
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELR 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 115 EKSKLQEIY-QELTWLKAAVGELPEK-SKMQEIYQELTRLKAAVGELPEKskqQEIYQELTRLKAAVGELPEKSKQ---Q 189
Cdd:PRK03918 311 EIEKRLSRLeEEINGIEERIKELEEKeERLEELKKKLKELEKRLEELEER---HELYEEAKAKKEELERLKKRLTGltpE 387

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 223029386 190 EIYQELTRLKAAVGELPEK-----SKQQEIYQELTQLKAAVERL 228
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431
PHA02867 PHA02867
C-type lectin protein; Provisional
 232-279 1.98e-04

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 41.59  E-value: 1.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 223029386 232 CPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFL 279
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 72-226 4.97e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  72 KLQEIYQELTQLKAAVGELPE-----KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTWLKAAVGELPEKSK----- 141
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAelaelEDELAALEARLEAAKTELEDL--EKEIKRLELEIEEVEARIKKYEEQLGnvrnn 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 142 --MQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEK--SKQQEIYQELTRLKAAVGELpeKSKQQEIYQE 217
Cdd:COG1579   89 keYEALQKEIESLKRRISDL--EDEILELMERIEELEEELAELEAElaELEAELEEKKAELDEELAEL--EAELEELEAE 164


                 ....*....
gi 223029386 218 LTQLKAAVE 226
Cdd:COG1579  165 REELAAKIP 173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-228 7.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  32 KSLAVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLK-AAVGELPEKSK-LQEIYQELTRLKAA 109
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE--LAELLKELEELGfESVEELEERLKeLEPFYNEYLELKDA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 110 VGELPEKSKLQEIYQELtwLKAAVGELPE-KSKMQEIYQELTRLKAAVGELPEKSKQQ---EIYQELTRLKAAVGELpeK 185
Cdd:PRK03918 611 EKELEREEKELKKLEEE--LDKAFEELAEtEKRLEELRKELEELEKKYSEEEYEELREeylELSRELAGLRAELEEL--E 686

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 223029386 186 SKQQEIYQELTRLKAAVGELPEKSKqqeiyqELTQLKAAVERL 228
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKK------ELEKLEKALERV 723
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 61-223 2.33e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  61 KAAVGElsEKSKLQEIYQELTQLKAavgELPEKSK-LQEIYQELTRLKAAVGElpEKSKLQEIYQELtwlkaavgelpeK 139
Cdd:PRK00409 508 KKLIGE--DKEKLNELIASLEELER---ELEQKAEeAEALLKEAEKLKEELEE--KKEKLQEEEDKL------------L 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 140 SKMQEIYQEltRLKAAvgelpekskQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEksKQQEIYQELT 219
Cdd:PRK00409 569 EEAEKEAQQ--AIKEA---------KKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK--KKKKQKEKQE 635


                 ....
gi 223029386 220 QLKA 223
Cdd:PRK00409 636 ELKV 639
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-159 3.28e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  51 DAIYQNLTQLKAAVgelSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEksKLQEIYQELTWLK 130
Cdd:COG4717  385 EELRAALEQAEEYQ---ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE--ELEELREELAELE 459

                         90       100
                 ....*....|....*....|....*....
gi 223029386 131 AAVGELPEKSKMQEIYQELTRLKAAVGEL 159
Cdd:COG4717  460 AELEQLEEDGELAELLQELEELKAELREL 488
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
41-228 3.96e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  41 SSISQEQSRQDAIYQNLTQLKAAVGELSEK-----SKLQEIYQELTQLKAAVGELPE-----KSKLQEIYQELTRLKAAV 110
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKrdelnEELKELAEKRDELNAQVKELREeaqelREKRDELNEKVKELKEER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386 111 GELpeKSKLQEIYQELTWLKAAVGEL-----PEKSKMQEIYQELTRLKAAVgeLPeKSKQQEIYQEL----TRLKAAVGE 181
Cdd:COG1340   81 DEL--NEKLNELREELDELRKELAELnkaggSIDKLRKEIERLEWRQQTEV--LS-PEEEKELVEKIkeleKELEKAKKA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223029386 182 LPEKSKQQEIYQELTRLKAAVGELPEK-----SKQQEIYQELTQLKAAVERL 228
Cdd:COG1340  156 LEKNEKLKELRAELKELRKEAEEIHKKikelaEEAQELHEEMIELYKEADEL 207
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-136 5.53e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386  45 QEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPEKSKLQEIYQ 124
Cdd:COG4717  399 ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE--ELEELREELAELEAELEQLEEDGELAELLQ 476

                         90
                 ....*....|..
gi 223029386 125 ELTWLKAAVGEL 136
Cdd:COG4717  477 ELEELKAELREL 488
CoV_Spike_S1-S2_S2 cd21698
S1/S2 cleavage region and the S2 fusion subunit of coronavirus spike (S) proteins; This model ...
 9-87 7.74e-03

S1/S2 cleavage region and the S2 fusion subunit of coronavirus spike (S) proteins; This model represents the S1/S2 cleavage region and the S2 subunit of the spike (S) glycoprotein from coronavirus (CoVs), including three highly pathogenic human CoVs, Middle East respiratory syndrome coronavirus (MERS-CoV), Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV), and SARS coronavirus 2 (SARS-CoV-2), also known as a 2019 novel coronavirus (2019-nCoV). The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-terminal domain (C-domain). S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect S1 and S2. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV, and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP), and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. Notably, SARS-CoV-2 has a functional polybasic (furin) cleavage site through the insertion of PRRAR*SV (* indicates the cleavage site) at the S1/S2 interface, which is absent in SARS-CoV and other SARS-related CoVs. The S1/S2 cleavage region and the S2 fusion subunit play an essential role in viral entry by initiating fusion of the viral and cellular membranes.


Pssm-ID: 411955 [Multi-domain]  Cd Length: 523  Bit Score: 38.17  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029386   9 LQQLGLLEEEQLRGLGFRQTRGYKSLAVSKVPSSIsqeQSRQDAIYQNLTQLKAAVGELSEK-----SKLQEIYQELTQL 83
Cdd:cd21698  228 LQQNVLLENQKLLANSFNKAIGNISDAFSSTSSAL---QKIQDVVNQQAQALNTLTSQLSNNfgaisSSIQDIYQRLDKL 304


                 ....
gi 223029386  84 KAAV 87
Cdd:cd21698  305 EADV 308
 
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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