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Conserved domains on  [gi|1958651166|ref|XP_008758809|]
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attractin-like protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 746-872 9.11e-78

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.


The actual alignment was detected with superfamily member cd03597:

Pssm-ID: 470576  Cd Length: 129  Bit Score: 252.50  E-value: 9.11e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 823
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651166  824 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 872
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-597 6.00e-24

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  302 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 377
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  378 GNVTDELWVFNVRSQSWSTKTPtilghgqqyAVEGHSAHIMELDSGDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 457
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  458 TKGAIVQGGYGHTSVYDEMTKsVYVHGGYKalpgnkyglvddlykYEVNSRTWTILKESGFARYLHSAVLISGAVLVFGG 537
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  538 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 597
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-207 1.39e-16

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 77.07  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGl 165
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958651166  166 ivpevrgNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 207
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1011-1056 2.72e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651166 1011 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDPTNGGQCT 1056
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 887-936 9.31e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 44.24  E-value: 9.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651166  887 PCSLRTSCANCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 936
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
DSL super family cl19567
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 234-280 2.91e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


The actual alignment was detected with superfamily member pfam01414:

Pssm-ID: 473190  Cd Length: 46  Bit Score: 36.83  E-value: 2.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958651166  234 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 280
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
 
Name Accession Description Interval E-value
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 746-872 9.11e-78

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 252.50  E-value: 9.11e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 823
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651166  824 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 872
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-597 6.00e-24

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  302 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 377
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  378 GNVTDELWVFNVRSQSWSTKTPtilghgqqyAVEGHSAHIMELDSGDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 457
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  458 TKGAIVQGGYGHTSVYDEMTKsVYVHGGYKalpgnkyglvddlykYEVNSRTWTILKESGFARYLHSAVLISGAVLVFGG 537
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  538 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 597
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-207 1.39e-16

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 77.07  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGl 165
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958651166  166 ivpevrgNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 207
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 746-848 4.21e-14

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: 70.32  E-value: 4.21e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQQRvSPWVGLRKINISY-WGWEDM 824
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 1958651166   825 SPFTNTSLqWLPGEPNDS-GFCAYL 848
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 764-872 1.46e-12

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.19  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  764 RESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQqrvSPWVGLRKINIS-YWGWEDMSPFTNTSLQWLPGEPNDS 842
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958651166  843 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 872
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CUB pfam00431
CUB domain;
92-205 1.84e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 62.31  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   92 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGL 165
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958651166  166 IVPEVrgnetvpeVVTTSGYALLHFFSDAAYNLTGFNIFY 205
Cdd:pfam00431   79 GIPED--------IVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 109-205 3.18e-11

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 61.25  E-value: 3.18e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   109 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGLIVPEvrgnetvPEVVTTSG 184
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1958651166   185 YALLHFFSDAAYNLTGFNIFY 205
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1011-1056 2.72e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651166 1011 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDPTNGGQCT 1056
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 887-936 9.31e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 44.24  E-value: 9.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651166  887 PCSLRTSCANCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 936
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 351-391 1.48e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 43.32  E-value: 1.48e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958651166  351 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 391
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1012-1055 5.53e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 41.96  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651166 1012 CQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDP-TNGGQC 1055
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1012-1052 2.71e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.99  E-value: 2.71e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958651166  1012 CQCNG----HSTCINNN-VCEqCKNLTTGRQCQDCMPGYYGDPTNG 1052
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
PLN02153 PLN02153
epithiospecifier protein
 453-599 2.72e-04

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 44.98  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  453 WLVPETKGAIVQG---GYGHTSVYDEMtksvYVHGGykALPGNKYgLVDDLYKYEVNSRTWTILKESGFARYLHS----A 525
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958651166  526 VLISGAVLVFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 599
Cdd:PLN02153    82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 234-280 2.91e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


Pssm-ID: 460202  Cd Length: 46  Bit Score: 36.83  E-value: 2.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958651166  234 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 280
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
233-279 3.34e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.34e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958651166   233 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 279
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
 
Name Accession Description Interval E-value
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 746-872 9.11e-78

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 252.50  E-value: 9.11e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 823
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651166  824 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 872
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-597 6.00e-24

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  302 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 377
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  378 GNVTDELWVFNVRSQSWSTKTPtilghgqqyAVEGHSAHIMELDSGDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 457
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  458 TKGAIVQGGYGHTSVYDEMTKsVYVHGGYKalpgnkyglvddlykYEVNSRTWTILKESGFARYLHSAVLISGAVLVFGG 537
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  538 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 597
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
300-541 1.29e-19

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.60  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  300 PSVGRASHKAVLHGKFMWVIGGYTFNYSSFQM---VLNYNLESSIWNVGAVSrgPLQRYGHSLALYQENIFMYGGRmetS 376
Cdd:COG3055     57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPlndVYVYDPATNTWTKLAPM--PTPRGGATALLLDGKIYVVGGW---D 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  377 DGNVTDELWVFNVRSQSWSTKTPTILghgqqyAVEGHSAHImeLDSGdvvMIVIFGysaiyGYTSSIqeyhiSSNTWlvp 456
Cdd:COG3055    132 DGGNVAWVEVYDPATGTWTQLAPLPT------PRDHLAAAV--LPDG---KILVIG-----GRNGSG-----FSNTW--- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  457 ETKGAIVQGGYGHTSVYdeMTKSVYVHGGYkalpgnkYGLVDDLYKYEVNSRTWTILKESGFARYLHSAVLISGAVLVFG 536
Cdd:COG3055    188 TTLAPLPTARAGHAAAV--LGGKILVFGGE-------SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIG 258


                   ....*
gi 1958651166  537 GNTHN 541
Cdd:COG3055    259 GETKP 263
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
351-613 1.16e-17

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 84.82  E-value: 1.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  351 PLQRYGHSLALYQENIFMYGGRmetSDGNVTDELWVFNVRSQSWSTKTPtilghgqqYAVEGHSAHIMELDSGDVvmIVI 430
Cdd:COG3055     10 PTPRSEAAAALLDGKVYVAGGL---SGGSASNSFEVYDPATNTWSELAP--------LPGPPRHHAAAVAQDGKL--YVF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  431 FGYSAIYG---YTSSIQEYHISSNTWlvpETKGAIVQGGYGHTSVYDEmtKSVYVHGGYkalpgNKYGLVDDLYKYEVNS 507
Cdd:COG3055     77 GGFTGANPsstPLNDVYVYDPATNTW---TKLAPMPTPRGGATALLLD--GKIYVVGGW-----DDGGNVAWVEVYDPAT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  508 RTWTILKESGFARYLHSA-VLISGAVLVFGGNthNDTSLSNgakcfsadflaydiacdEWKTLPkpnlHRDVNRFGHSAV 586
Cdd:COG3055    147 GTWTQLAPLPTPRDHLAAaVLPDGKILVIGGR--NGSGFSN-----------------TWTTLA----PLPTARAGHAAA 203

                          250       260
                   ....*....|....*....|....*..
gi 1958651166  587 VINGSMYIFGGFSSVlLNDILVYKPPS 613
Cdd:COG3055    204 VLGGKILVFGGESGF-SDEVEAYDPAT 229
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-207 1.39e-16

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 77.07  E-value: 1.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGl 165
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958651166  166 ivpevrgNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 207
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 756-872 2.63e-15

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: 73.42  E-value: 2.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  756 SCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQQRVspWVGLRKINI-SYWGWEDMSPFTNTSlQW 834
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--WIGLNDLSSeGTWKWSDGSPLVDYT-NW 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958651166  835 LPGEPN--DSGFCAYLERAAVAGLKANPCTSMAdGLVCEK 872
Cdd:cd00037     78 APGEPNpgGSEDCVVLSSSSDGKWNDVSCSSKL-PFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 746-848 4.21e-14

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: 70.32  E-value: 4.21e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQQRvSPWVGLRKINISY-WGWEDM 824
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 1958651166   825 SPFTNTSLqWLPGEPNDS-GFCAYL 848
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 764-872 1.46e-12

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 65.19  E-value: 1.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  764 RESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQqrvSPWVGLRKINIS-YWGWEDMSPFTNTSLQWLPGEPNDS 842
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958651166  843 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 872
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
509-611 3.66e-12

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 68.64  E-value: 3.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  509 TWTILKESGFARYLHSAVLISGAVLVFGGNTHNDTslsngakcfSADFLAYDIACDEWKTLPKPNLHRdvnRFGHSAVVI 588
Cdd:COG3055      2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELAPLPGPP---RHHAAAVAQ 69

                           90       100
                   ....*....|....*....|....*...
gi 1958651166  589 NGSMYIFGGF-----SSVLLNDILVYKP 611
Cdd:COG3055     70 DGKLYVFGGFtganpSSTPLNDVYVYDP 97
CUB pfam00431
CUB domain;
92-205 1.84e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 62.31  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   92 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGL 165
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958651166  166 IVPEVrgnetvpeVVTTSGYALLHFFSDAAYNLTGFNIFY 205
Cdd:pfam00431   79 GIPED--------IVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 109-205 3.18e-11

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 61.25  E-value: 3.18e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166   109 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVLSGLIVPEvrgnetvPEVVTTSG 184
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1958651166   185 YALLHFFSDAAYNLTGFNIFY 205
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 746-848 8.25e-09

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: 55.00  E-value: 8.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFvldeIQKNTQQRVSPWVGLRKINI-SYWGWEDM 824
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETeGEWKWVDG 76

                           90       100
                   ....*....|....*....|....*...
gi 1958651166  825 SPFTNTSLQWLPGEPNDSGF----CAYL 848
Cdd:cd03590     77 TPLNSSKTFWHPGEPNNWGGggedCAEL 104
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1011-1056 2.72e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651166 1011 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDPTNGGQCT 1056
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 746-872 6.68e-07

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: 49.25  E-value: 6.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFvldeIQKNTQQRvSPWVGLRKINISY-WGWEDM 824
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF----LQSQIGSS-SYWIGLSREKSEKpWKWIDG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651166  825 SPFTNtslqWL-PGEPNDSGFCAYLERaavAGLKANPCtSMADGLVCEK 872
Cdd:cd03593     76 SPLNN----LFnIRGSTKSGNCAYLSS---TGIYSEDC-STKKRWICEK 116
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 887-936 9.31e-06

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 44.24  E-value: 9.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651166  887 PCSLRTSCANCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 936
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 351-391 1.48e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 43.32  E-value: 1.48e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958651166  351 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 391
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 746-850 4.94e-05

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 44.91  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGD--SCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVL------DEIQKNTQQRVSPWVGLRKI--- 814
Cdd:cd03599      1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILaqewdfDERVFGRKDQCKFWVGYQYVitn 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958651166  815 -NISYWG-WEdmSPFTNTSLQWLPGEP--------NDSGFCAYLER 850
Cdd:cd03599     81 rNHSLEGrWE--VAYKGSMEVFLPPEPifatgmstNDNVFCAQLQC 124
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1012-1055 5.53e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 41.96  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651166 1012 CQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDP-TNGGQC 1055
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 746-862 9.16e-05

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: 43.89  E-value: 9.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYN-----LSGNLASLTTSKEVGFVLDEIQKNTQQRVSP--WVGL-RKINIS 817
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGPDTPYglWIGLhDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958651166  818 YWGWEDMSPFTNTslQWLPGEPNDSGF---CAYLERAAVAGLKAN--PCT 862
Cdd:cd03589     81 PFEWTDGSPVDFT--KWAGGQPDNYGGnedCVQMWRRGDAGQSWNdmPCD 128
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 746-850 1.01e-04

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: 43.51  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYC--YNLSGNLASLTTSKEVGFVLDEIqKNTQQRVSP-WVGLRKINISY-WGW 821
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLI-SSYQKAYQPvWIGLHDPQQSRgWEW 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958651166  822 EDMSPFTNTSlqWLPGEP-NDSGFCAYLER 850
Cdd:cd03594     80 SDGSKLDYRS--WDRNPPyARGGYCAELSR 107
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1012-1052 2.71e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.99  E-value: 2.71e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958651166  1012 CQCNG----HSTCINNN-VCEqCKNLTTGRQCQDCMPGYYGDPTNG 1052
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
PLN02153 PLN02153
epithiospecifier protein
 453-599 2.72e-04

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 44.98  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  453 WLVPETKGAIVQG---GYGHTSVYDEMtksvYVHGGykALPGNKYgLVDDLYKYEVNSRTWTILKESGFARYLHS----A 525
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958651166  526 VLISGAVLVFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 599
Cdd:PLN02153    82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
PHA03098 PHA03098
kelch-like protein; Provisional
 315-453 6.74e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.99  E-value: 6.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  315 FMWVIGGYTFNYSSFQMVLNYNLESSIWNVGavSRGPLQRYGHSLALYQENIFMYGGRMETSDGNVTDELWVFNVRSQSW 394
Cdd:PHA03098   391 LIYVIGGISKNDELLKTVECFSLNTNKWSKG--SPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVYNIVESYNPVTNKW 468

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958651166  395 STKTPTILGHGqqyaveghsahIMELDSGDVVMIVIFGYSAIYgYTSSIQEYHISSNTW 453
Cdd:PHA03098   469 TELSSLNFPRI-----------NASLCIFNNKIYVVGGDKYEY-YINEIEVYDDKTNTW 515
PHA03098 PHA03098
kelch-like protein; Provisional
 480-609 8.63e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.60  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  480 VYVHGGYkalpgNKYG-LVDDLYKYEVNSRTWTILKESGFARYLHSAVLISGAVLVFGGNTHndtslSNGAKCFSADFLa 558
Cdd:PHA03098   392 IYVIGGI-----SKNDeLLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGISY-----IDNIKVYNIVES- 460

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651166  559 YDIACDEWKTLPKPNLHRdvnrFGHSAVVINGSMYIFGGFS-SVLLNDILVY 609
Cdd:PHA03098   461 YNPVTNKWTELSSLNFPR----INASLCIFNNKIYVVGGDKyEYYINEIEVY 508
Kelch_3 pfam13415
Galactose oxidase, central domain;
477-528 1.37e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 38.04  E-value: 1.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651166  477 TKSVYVHGGYKALPGNKYglvDDLYKYEVNSRTWTILKESGFARYLHSAVLI 528
Cdd:pfam13415    1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 770-848 2.16e-03

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: 39.28  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  770 AKLYCYNLSGNLASLTTSKEvgfvLDEIQKNTQQRVSP-WVGLRKiNISYWGWEDMSPFTntSLQWLPGEPNDSGFCAYL 848
Cdd:cd03602     15 AQQYCRENYTDLATVQNQED----NALLSNLSRVSNSAaWIGLYR-DVDSWRWSDGSESS--FRNWNTFQPFGQGDCATM 87
Kelch_4 pfam13418
Galactose oxidase, central domain;
468-513 2.35e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.21  E-value: 2.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958651166  468 GHTSVYDEmTKSVYVHGGYkalpGNKYGLVDDLYKYEVNSRTWTIL 513
Cdd:pfam13418    4 YHTSTSIP-DDTIYLFGGE----GEDGTLLSDLWVFDLSTNEWTRL 44
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 234-280 2.91e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


Pssm-ID: 460202  Cd Length: 46  Bit Score: 36.83  E-value: 2.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958651166  234 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 280
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
233-279 3.34e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.34e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958651166   233 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 279
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
Kelch_6 pfam13964
Kelch motif;
354-396 4.54e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 36.54  E-value: 4.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958651166  354 RYGHSLALYQENIFMYGGRmeTSDGNVTDELWVFNVRSQSWST 396
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGY--TNASPALNKLEVYNPLTKSWEE 42
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 746-846 6.48e-03

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 38.33  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651166  746 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVldeiqkNTQQRVSPWVGLRKINISY-WGWEDM 824
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV------NNNAQDYQWIGLNDRTIEGdFRWSDG 74

                           90       100
                   ....*....|....*....|....
gi 1958651166  825 SP--FTNtslqWLPGEPnDSGFCA 846
Cdd:cd03588     75 HPlqFEN----WRPNQP-DNFFAT 93
Kelch_4 pfam13418
Galactose oxidase, central domain;
354-396 6.54e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 6.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958651166  354 RYGHSL-ALYQENIFMYGGRMEtsDGNVTDELWVFNVRSQSWST 396
Cdd:pfam13418    2 RAYHTStSIPDDTIYLFGGEGE--DGTLLSDLWVFDLSTNEWTR 43
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 580-613 7.86e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 35.62  E-value: 7.86e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958651166  580 RFGHSAVVINGSMYIFGGFSS---VLLNDILVYKPPS 613
Cdd:pfam13854    4 RYGHCAVTVGDYIYLYGGYTGgegQPSDDVYVLSLPT 40
 
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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