NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21357409|ref|NP_652641|]
View 

lectin-24Db [Drosophila melanogaster]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10034483)

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

CATH:  3.10.100.10
Gene Ontology:  GO:0030246|GO:0120153
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 247-354 3.47e-25

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: 98.46  E-value: 3.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 247 YINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKS---YWLGINDLQSSNTYVSVASGREVEFLNWNAGEP 323
Cdd:cd00037   3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPGEP 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 21357409 324 NHGNeDENCVELIRS---KMNDDPCHRKKHVICQ 354
Cdd:cd00037  83 NPGG-SEDCVVLSSSsdgKWNDVSCSSKLPFICE 115
IFT57 super family cl26417
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 64-215 5.72e-05

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


The actual alignment was detected with superfamily member pfam10498:

Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 44.56  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    64 NTSEALWLNEtqgkLDRIQTQLAAqalsleesaqKVPGDIKD---RLDRMEHLQTTLQES-------LKKMPAELDARLM 133
Cdd:pfam10498 192 NVDAAEWKLE----LERVLPQLKV----------TIKADAKDwraHLEQMKQHKKSIEESlpdtksqLDKLHTDISKTLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   134 KMENQQKTLGDQLENQINLTKEsQQDQLEalknampiNFEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLE-------- 205
Cdd:pfam10498 258 KIESREKYINSQLEPLIQEYRE-AQDELS--------EVQEKYKQLSEGVTERTRELAEITEELEKVKQEMEergssmtd 328

                         170
                  ....*....|....
gi 21357409   206 ----QNQKDELTKL 215
Cdd:pfam10498 329 gsplVKIKQALTKL 342
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 247-354 3.47e-25

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: 98.46  E-value: 3.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 247 YINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKS---YWLGINDLQSSNTYVSVASGREVEFLNWNAGEP 323
Cdd:cd00037   3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPGEP 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 21357409 324 NHGNeDENCVELIRS---KMNDDPCHRKKHVICQ 354
Cdd:cd00037  83 NPGG-SEDCVVLSSSsdgKWNDVSCSSKLPFICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 253-355 6.49e-20

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 83.68  E-value: 6.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   253 AYDWQSAVDFCRDMGGYIAAIKDQEELDAISARL--DDKSYWLGINDLQSSNTYVSVaSGREVEFLNWnAGEPNHGNEDE 330
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWV-DGSPVNYTNW-APEPNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 21357409   331 NCVELIRS--KMNDDPCHRKKHVICQT 355
Cdd:pfam00059  79 DCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 236-354 9.55e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 83.80  E-value: 9.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    236 PKFERIGSRLFYINHkDAYDWQSAVDFCRDMGGYIAAIKDQEELDAI----SARLDDKSYWLGINDLQSSNTYVSVASGR 311
Cdd:smart00034   3 SGWISYGGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 21357409    312 EVEFLNWNAGEPNHGNedENCVELIRS--KMNDDPCHRKKHVICQ 354
Cdd:smart00034  82 PVSYSNWAPGEPNNSS--GDCVVLSTSggKWNDVSCTSKLPFVCE 124
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 258-353 4.03e-05

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  258 SAVDFCRDMGGYIAAIKDQEELDAISARLDDKSYWLGIndlqssnTYVSV-ASGREVeflnwnAGEPNHGNEDENCVELI 336
Cdd:PHA03097  69 LAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGI-------EKKKGdDDDREV------LDKVVKPPKSGKCAYLK 135

                         90
                 ....*....|....*..
gi 21357409  337 RSKMNDDPCHRKKHVIC 353
Cdd:PHA03097 136 DKTIISSNCNATKGWIC 152
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 64-215 5.72e-05

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 44.56  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    64 NTSEALWLNEtqgkLDRIQTQLAAqalsleesaqKVPGDIKD---RLDRMEHLQTTLQES-------LKKMPAELDARLM 133
Cdd:pfam10498 192 NVDAAEWKLE----LERVLPQLKV----------TIKADAKDwraHLEQMKQHKKSIEESlpdtksqLDKLHTDISKTLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   134 KMENQQKTLGDQLENQINLTKEsQQDQLEalknampiNFEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLE-------- 205
Cdd:pfam10498 258 KIESREKYINSQLEPLIQEYRE-AQDELS--------EVQEKYKQLSEGVTERTRELAEITEELEKVKQEMEergssmtd 328

                         170
                  ....*....|....
gi 21357409   206 ----QNQKDELTKL 215
Cdd:pfam10498 329 gsplVKIKQALTKL 342
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 71-229 1.01e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  71 LNETQGKLDRIQTQLAAQALSLEESAQKVpGDIKDRLDRMEHLQTTLQESLKKMPAELDARLMKMENQ------------ 138
Cdd:COG3883  25 LSELQAELEAAQAELDALQAELEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvs 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 139 -------QKTLGDQLENQINLTK--ESQQDQLEALKNAMpINFEMRLAQIEEQQKLLQETLKKIpEDFERKLQKLEQNQK 209
Cdd:COG3883 104 yldvllgSESFSDFLDRLSALSKiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAEL-EAAKAELEAQQAEQE 181

                       170       180
                ....*....|....*....|
gi 21357409 210 DELTKLGAQQSANQVTLKEI 229
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAEL 201
PRK11281 PRK11281
mechanosensitive channel MscK;
71-229 1.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    71 LNETQGKLDRIQTQLAaQALSLEESAQKVPGDIKD---RLDRM-EHLQTTLQESLKKMP-AELDARLMKMENQQKTLGDQ 145
Cdd:PRK11281   65 LEQTLALLDKIDRQKE-ETEQLKQQLAQAPAKLRQaqaELEALkDDNDEETRETLSTLSlRQLESRLAQTLDQLQNAQND 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   146 LeNQINLTKESQQDQLEALKNAMPINfEMRLAQIE---------------EQQKLLQETLKKIPE--DFERK-------L 201
Cdd:PRK11281  144 L-AEYNSQLVSLQTQPERAQAALYAN-SQRLQQIRnllkggkvggkalrpSQRVLLQAEQALLNAqnDLQRKslegntqL 221

                         170       180
                  ....*....|....*....|....*...
gi 21357409   202 QKLEQNQKDELTKLGAQQSANQVTLKEI 229
Cdd:PRK11281  222 QDLLQKQRDYLTARIQRLEHQLQLLQEA 249
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-229 1.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409     52 LLDHIVKHQEQWNTSEALwLNETQGKLDRIQTQLAAQALSLEE-------------SAQKVPGDIKDRLDRMEHlqttlq 118
Cdd:TIGR02168  230 LVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEElrlevseleeeieELQKELYALANEISRLEQ------ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    119 eslkkMPAELDARLMKMENQQKTLGDQLENQinltkESQQDQLEALKNAMPINFEMRLAQIEEQQKLLQEtLKKIPEDFE 198
Cdd:TIGR02168  303 -----QKQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELKEELESLEAELEE-LEAELEELE 371

                          170       180       190
                   ....*....|....*....|....*....|....
gi 21357409    199 RKLQKLE---QNQKDELTKLGAQQSANQVTLKEI 229
Cdd:TIGR02168  372 SRLEELEeqlETLRSKVAQLELQIASLNNEIERL 405
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 247-354 3.47e-25

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: 98.46  E-value: 3.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 247 YINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKS---YWLGINDLQSSNTYVSVASGREVEFLNWNAGEP 323
Cdd:cd00037   3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPGEP 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 21357409 324 NHGNeDENCVELIRS---KMNDDPCHRKKHVICQ 354
Cdd:cd00037  83 NPGG-SEDCVVLSSSsdgKWNDVSCSSKLPFICE 115
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 247-355 9.98e-22

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: 88.97  E-value: 9.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 247 YINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAI---SARLDDKSYWLGINDLQSSNTYVSvASGREVEFLNWNAGEP 323
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLngfALKYNLGYYWIDGNDINNEGTWVD-TDKKELEYKNWAPGEP 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21357409 324 NhGNEDENCVELIRS---KMNDDPCHRKKHVICQT 355
Cdd:cd03592  82 N-NGRNENCLEIYIKdngKWNDEPCSKKKSAICYT 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 253-355 6.49e-20

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 83.68  E-value: 6.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   253 AYDWQSAVDFCRDMGGYIAAIKDQEELDAISARL--DDKSYWLGINDLQSSNTYVSVaSGREVEFLNWnAGEPNHGNEDE 330
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWV-DGSPVNYTNW-APEPNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 21357409   331 NCVELIRS--KMNDDPCHRKKHVICQT 355
Cdd:pfam00059  79 DCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 236-354 9.55e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 83.80  E-value: 9.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    236 PKFERIGSRLFYINHkDAYDWQSAVDFCRDMGGYIAAIKDQEELDAI----SARLDDKSYWLGINDLQSSNTYVSVASGR 311
Cdd:smart00034   3 SGWISYGGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 21357409    312 EVEFLNWNAGEPNHGNedENCVELIRS--KMNDDPCHRKKHVICQ 354
Cdd:smart00034  82 PVSYSNWAPGEPNNSS--GDCVVLSTSggKWNDVSCTSKLPFVCE 124
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 246-354 9.58e-20

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: 83.50  E-value: 9.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 246 FYINHKDaYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKSY--WLGINDLQSSNTYVSVaSGREVEFLNWNAGEP 323
Cdd:cd03591   4 FVTNGEE-KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTyaFIGITDLETEGQFVYL-DGGPLTYTNWKPGEP 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 21357409 324 NHGNEDENCVELIRS-KMNDDPCHRKKHVICQ 354
Cdd:cd03591  82 NNAGGGEDCVEMYTSgKWNDVACNLTRLFVCE 113
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 235-355 1.78e-19

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: 83.12  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 235 WPKFeriGSRLFYINhKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLD-DKSYWLGINDLQSSNTYVSV-ASGRE 312
Cdd:cd03590   5 WKSF---QSSCYFFS-TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSgNRSYWIGLSDEETEGEWKWVdGTPLN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21357409 313 VEFLNWNAGEP-NHGNEDENCVELIRSKM--NDDPCHRKKHVICQT 355
Cdd:cd03590  81 SSKTFWHPGEPnNWGGGGEDCAELVYDSGgwNDVPCNLEYRWICEK 126
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 256-355 2.01e-10

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: 58.14  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 256 WQSAVDFCRDMG-----GYIAAIKDQEELDAI-----SARLDDKSY--WLGINDLQSSNTYVSvASGREVEFLNWNAGEP 323
Cdd:cd03589  22 WEEAELRCRSFSipgliAHLVSIHSQEENDFVydlfeSSRGPDTPYglWIGLHDRTSEGPFEW-TDGSPVDFTKWAGGQP 100

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 21357409 324 NHGNEDENCVELIR-----SKMNDDPCHRKKHVICQT 355
Cdd:cd03589 101 DNYGGNEDCVQMWRrgdagQSWNDMPCDAVFPYICKM 137
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 256-354 2.94e-09

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: 54.69  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 256 WQSAVDFCRDM--GGYIAAIKDQEELDAISA-----RLDDKSYWLGINDLQSSNTYVSVaSGREVEFLNWNAGEPNHGNE 328
Cdd:cd03594  22 WSDAELFCQKYgpGAHLASIHSPAEAAAIASlissyQKAYQPVWIGLHDPQQSRGWEWS-DGSKLDYRSWDRNPPYARGG 100

                        90       100       110
                ....*....|....*....|....*....|
gi 21357409 329 deNCVELIRS----KMNDDPCHRKKHVICQ 354
Cdd:cd03594 101 --YCAELSRStgflKWNDANCEERNPFICK 128
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 247-354 5.06e-09

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: 53.93  E-value: 5.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 247 YINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAIsARLDDKS------YWLGINDLQSSNTYVSVaSGREVEFLNWN- 319
Cdd:cd03596  12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDAL-RDYVKASvpgnweVWLGINDMVAEGKWVDV-NGSPISYFNWEr 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21357409 320 --AGEPNhGNEDENCVELIRS---KMNDDPCHRKKHVICQ 354
Cdd:cd03596  90 eiTAQPD-GGKRENCVALSSSaqgKWFDEDCRREKPYVCE 128
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 246-331 7.16e-09

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 53.20  E-value: 7.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 246 FYINHKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDD-KSYWLGINDLQSSNTYVSvASGREVEFLNWNAGEP- 323
Cdd:cd03603   2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGyGASWIGASDAATEGTWKW-SDGEESTYTNWGSGEPh 80


                ....*...
gi 21357409 324 NHGNEDEN 331
Cdd:cd03603  81 NNGGGNED 88
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 235-354 1.47e-07

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: 49.50  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 235 WPKFERIGSRLFyinhKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKSyWLGINDLQSSNTYvSVASGREVE 314
Cdd:cd03588   5 WDKFQGHCYRHF----PDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-WIGLNDRTIEGDF-RWSDGHPLQ 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21357409 315 FLNWNAGEP-NHGNEDENCVELI---RSKMNDDPCHRKKHVICQ 354
Cdd:cd03588  79 FENWRPNQPdNFFATGEDCVVMIwheEGEWNDVPCNYHLPFTCK 122
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 255-354 2.69e-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: 48.87  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 255 DWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKSYWLGINDLQSSNTYVSVASGrevEFLNWNagEPNHGNEDENCVE 334
Cdd:cd03593  21 TWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGS---PLNNLF--NIRGSTKSGNCAY 95

                        90       100
                ....*....|....*....|
gi 21357409 335 LIRSKMNDDPCHRKKHVICQ 354
Cdd:cd03593  96 LSSTGIYSEDCSTKKRWICE 115
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 259-354 1.70e-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: 46.37  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 259 AVDFCRDMGGYIAAI--KDQEELDAISARLDDK--SYWLGINDLQSSNTYVSVASGREV--EFLNWNAGEPNHGNEDENC 332
Cdd:cd03601  15 AGAFCRSRGMRLASLamRDSEMRDAILAFTLVKghGYWVGADNLQDGEYDFLWNDGVSLptDSDLWAPNEPSNPQSRQLC 94

                        90       100
                ....*....|....*....|....
gi 21357409 333 VELI--RSKMNDDPCHRKKHVICQ 354
Cdd:cd03601  95 VQLWskYNLLDDEYCGRAKRVICE 118
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 258-353 4.03e-05

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  258 SAVDFCRDMGGYIAAIKDQEELDAISARLDDKSYWLGIndlqssnTYVSV-ASGREVeflnwnAGEPNHGNEDENCVELI 336
Cdd:PHA03097  69 LAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGI-------EKKKGdDDDREV------LDKVVKPPKSGKCAYLK 135

                         90
                 ....*....|....*..
gi 21357409  337 RSKMNDDPCHRKKHVIC 353
Cdd:PHA03097 136 DKTIISSNCNATKGWIC 152
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 64-215 5.72e-05

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 44.56  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    64 NTSEALWLNEtqgkLDRIQTQLAAqalsleesaqKVPGDIKD---RLDRMEHLQTTLQES-------LKKMPAELDARLM 133
Cdd:pfam10498 192 NVDAAEWKLE----LERVLPQLKV----------TIKADAKDwraHLEQMKQHKKSIEESlpdtksqLDKLHTDISKTLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   134 KMENQQKTLGDQLENQINLTKEsQQDQLEalknampiNFEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLE-------- 205
Cdd:pfam10498 258 KIESREKYINSQLEPLIQEYRE-AQDELS--------EVQEKYKQLSEGVTERTRELAEITEELEKVKQEMEergssmtd 328

                         170
                  ....*....|....
gi 21357409   206 ----QNQKDELTKL 215
Cdd:pfam10498 329 gsplVKIKQALTKL 342
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 71-229 1.01e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  71 LNETQGKLDRIQTQLAAQALSLEESAQKVpGDIKDRLDRMEHLQTTLQESLKKMPAELDARLMKMENQ------------ 138
Cdd:COG3883  25 LSELQAELEAAQAELDALQAELEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvs 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 139 -------QKTLGDQLENQINLTK--ESQQDQLEALKNAMpINFEMRLAQIEEQQKLLQETLKKIpEDFERKLQKLEQNQK 209
Cdd:COG3883 104 yldvllgSESFSDFLDRLSALSKiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAEL-EAAKAELEAQQAEQE 181

                       170       180
                ....*....|....*....|
gi 21357409 210 DELTKLGAQQSANQVTLKEI 229
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAEL 201
PRK11281 PRK11281
mechanosensitive channel MscK;
71-229 1.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    71 LNETQGKLDRIQTQLAaQALSLEESAQKVPGDIKD---RLDRM-EHLQTTLQESLKKMP-AELDARLMKMENQQKTLGDQ 145
Cdd:PRK11281   65 LEQTLALLDKIDRQKE-ETEQLKQQLAQAPAKLRQaqaELEALkDDNDEETRETLSTLSlRQLESRLAQTLDQLQNAQND 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   146 LeNQINLTKESQQDQLEALKNAMPINfEMRLAQIE---------------EQQKLLQETLKKIPE--DFERK-------L 201
Cdd:PRK11281  144 L-AEYNSQLVSLQTQPERAQAALYAN-SQRLQQIRnllkggkvggkalrpSQRVLLQAEQALLNAqnDLQRKslegntqL 221

                         170       180
                  ....*....|....*....|....*...
gi 21357409   202 QKLEQNQKDELTKLGAQQSANQVTLKEI 229
Cdd:PRK11281  222 QDLLQKQRDYLTARIQRLEHQLQLLQEA 249
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
50-209 1.35e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  50 QPLLDHIVKHQEQWNTSEALwLNETQGKLDRIQTQLAAQALSLEESAQKvpGDIKDRLDRMEHLQTTLQESLKKMPAElD 129
Cdd:COG3206 215 KLLLQQLSELESQLAEARAE-LAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPN-H 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 130 ARLMKMENQQKTLGDQLENQINLTKESQQDQLEALKNampinfemRLAQIEEQQKLLQETLKKIPEDfERKLQKLEQNQK 209
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA--------REASLQAQLAQLEARLAELPEL-EAELRRLEREVE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-229 1.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409     52 LLDHIVKHQEQWNTSEALwLNETQGKLDRIQTQLAAQALSLEE-------------SAQKVPGDIKDRLDRMEHlqttlq 118
Cdd:TIGR02168  230 LVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEElrlevseleeeieELQKELYALANEISRLEQ------ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    119 eslkkMPAELDARLMKMENQQKTLGDQLENQinltkESQQDQLEALKNAMPINFEMRLAQIEEQQKLLQEtLKKIPEDFE 198
Cdd:TIGR02168  303 -----QKQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELKEELESLEAELEE-LEAELEELE 371

                          170       180       190
                   ....*....|....*....|....*....|....
gi 21357409    199 RKLQKLE---QNQKDELTKLGAQQSANQVTLKEI 229
Cdd:TIGR02168  372 SRLEELEeqlETLRSKVAQLELQIASLNNEIERL 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-219 3.15e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409     73 ETQGKLDRIQTQLAAQALSLEESAQKvPGDIKDRLDRMEHLQTTLQESLKKMPAELDARLMKMENqqktlgdqLENQInl 152
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------LESRL-- 374

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    153 tkESQQDQLEALKNAmpinfemrLAQIEEQQKLLQETLKKIP---EDFERKLQKLEQNQKDELTKLGAQQ 219
Cdd:TIGR02168  375 --EELEEQLETLRSK--------VAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAE 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 71-229 3.35e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409     71 LNETQGKLDRIQTQLAAQALSLEesaqKVPGDIKDRLDRMEHLQTTLQE---SLKKMPAELDARLMKMENQQKTLGDQLE 147
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409    148 NQINLTKESQQDQLEALknampiNFEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLEQNQKDeLTKLGAQQSANQVTLK 227
Cdd:TIGR02169  407 ELDRLQEELQRLSEELA------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD-LSKYEQELYDLKEEYD 479


                   ..
gi 21357409    228 EI 229
Cdd:TIGR02169  480 RV 481
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 70-228 3.44e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 3.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  70 WLNETQGKLDRIQTQLAAQALSLEESAQKVP------GDIKDRLDRMEHLQTTLQESLKKMPAELDARL---MKMENQ-- 138
Cdd:COG4942  42 ELAALKKEEKALLKQLAALERRIAALARRIRaleqelAALEAELAELEKEIAELRAELEAQKEELAELLralYRLGRQpp 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 139 ------QKTLGDQLENQINLTK--ESQQDQLEALKNAMPiNFEMRLAQIEEQQKLLQETLKKIpEDFERKLQKLEQNQKD 210
Cdd:COG4942 122 lalllsPEDFLDAVRRLQYLKYlaPARREQAEELRADLA-ELAALRAELEAERAELEALLAEL-EEERAALEALKAERQK 199

                       170
                ....*....|....*...
gi 21357409 211 ELTKLGAQQSANQVTLKE 228
Cdd:COG4942 200 LLARLEKELAELAAELAE 217
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 71-225 3.47e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  71 LNETQGKLDRIQTQLAAQALSLEESAQKVP--------GDIKDRLDRMEHLQTtLQESLKKMPAELDARLMKMENQQKTL 142
Cdd:COG3883  74 IAEAEAEIEERREELGERARALYRSGGSVSyldvllgsESFSDFLDRLSALSK-IADADADLLEELKADKAELEAKKAEL 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 143 GDQLENQinltkESQQDQLEALKNAMpinfemrLAQIEEQQKLLQEtLKKIPEDFERKLQKLEQNQKDELTKLGAQQSAN 222
Cdd:COG3883 153 EAKLAEL-----EALKAELEAAKAEL-------EAQQAEQEALLAQ-LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219


                ...
gi 21357409 223 QVT 225
Cdd:COG3883 220 AAA 222
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 218-302 5.50e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 40.87  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  218 QQSANQVTLKEIYTKVFWPKFeriGSRLFYINhKDAYDWQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKSYWLGIND 297
Cdd:PHA02642  75 KSDTQEPTIKYVTCPKGWIGF---GYKCFYFS-EDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNR 150


                 ....*
gi 21357409  298 lQSSN 302
Cdd:PHA02642 151 -ESSN 154
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
73-229 1.08e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  73 ETQGKLDRIQTQLAAQALSLEESAQKV------------PGDIKDRLDRMEHLQTTLQESLKKMpAELDARLMKMENQ-- 138
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALeefrqknglvdlSEEAKLLLQQLSELESQLAEARAEL-AEAEARLAALRAQlg 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 139 --QKTLGDQLENQINLTKESQQDQLEALKNAMPINF-----EMR--LAQIEEQQKLLQETLKKIPEDFERKLQKLE---- 205
Cdd:COG3206 251 sgPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpDVIalRAQIAALRAQLQQEAQRILASLEAELEALQarea 330

                       170       180
                ....*....|....*....|....*.
gi 21357409 206 --QNQKDELTKLGAQQSANQVTLKEI 229
Cdd:COG3206 331 slQAQLAQLEARLAELPELEAELRRL 356
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 78-216 1.29e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409     78 LDRIQTQLAAQALSLEESAQKVPGDiKDRLDR----MEHLQTTLQESLKKMPAELDARLMKMENQQKtlgdQLENQINLT 153
Cdd:pfam12128  627 LVQANGELEKASREETFARTALKNA-RLDLRRlfdeKQSEKDKKNKALAERKDSANERLNSLEAQLK----QLDKKHQAW 701

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357409    154 KESQQDQLEALKNAMPINFEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLEQNQKDELTKLG 216
Cdd:pfam12128  702 LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 256-323 1.31e-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: 38.12  E-value: 1.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 256 WQSAVDFCRDMGGYIAAIKDQEELDAISARLDDKS--YWLGINDLQSSntyVSVASGREVEFLNWNAGEP 323
Cdd:cd03602  12 WSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNsaAWIGLYRDVDS---WRWSDGSESSFRNWNTFQP 78
PRK15471 PRK15471
chain length determinant protein WzzB; Provisional
 66-190 2.02e-03

chain length determinant protein WzzB; Provisional


Pssm-ID: 185368 [Multi-domain]  Cd Length: 325  Bit Score: 39.73  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   66 SEALWLNETQGKLDrIQTQLAAQALSLE--------ESAQKvpgdikdrldrmeHLQTTLQESLKKMPAELDARL-MKME 136
Cdd:PRK15471 107 AETLDNQEEPEKLT-IEPSVKGQALPLSvsyvgqtaEGAQK-------------KLAQYIQQVDDQVAKELEKDLkDNIA 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21357409  137 NQQKTLGDQLENQINLTKEsQQD----QL-EALKNAMPINfeMRLAQIEEQQKLLQETL 190
Cdd:PRK15471 173 LRTKTLQDSLETQEVVAQE-QKDlrikQIqEALQYANQAN--ITKPQIQQTQDVTQDTL 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 52-223 2.87e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  52 LLDHIVKHQEQWNTSEALwLNETQGKLDRIQTQLAAQALSLEEsaqkvpgdIKDRLDRMEHLQTTLQESLkkmpAELDAR 131
Cdd:COG1196 230 LLLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEE--------LRLELEELELELEEAQAEE----YELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 132 LMKMENQQKtlgDQLENQINLTKESQQDQLEALKNampinfEMRLAQIEEQQKLLQETLKKIPEDFERKLQKLEQNQKDE 211
Cdd:COG1196 297 LARLEQDIA---RLEERRRELEERLEELEEELAEL------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                       170
                ....*....|..
gi 21357409 212 LTKLGAQQSANQ 223
Cdd:COG1196 368 LEAEAELAEAEE 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
71-224 6.73e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 6.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  71 LNETQGKLDRIQTQLAAQALSLEESAQKVpgdikDRLDRMEHLQTTLQE--SLKKMPAELDARLMKMENQQKTLGDQLEN 148
Cdd:COG4717  90 YAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQEleALEAELAELPERLEELEERLEELRELEEE 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409 149 QINLTKE--SQQDQLEALKNAMPINFEMRLAQIEEQQKLLQETLKKIPEDF---ERKLQKLEQNQKDELTKLGAQQSANQ 223
Cdd:COG4717 165 LEELEAElaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELeeaQEELEELEEELEQLENELEAAALEER 244


                .
gi 21357409 224 V 224
Cdd:COG4717 245 L 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-229 7.12e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409   48 VLQPLLDHIVKHQEQWNTsealwLNETQGKLDRIQTQLAAQALSLEESAQKvpgDIKDRLDRMEHLQTTLQESLKkmpaE 127
Cdd:COG4913  253 LLEPIRELAERYAAARER-----LAELEYLRAALRLWFAQRRLELLEAELE---ELRAELARLEAELERLEARLD----A 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357409  128 LDARLMKMENQQKTLG----DQLENQI---NLTKESQQDQLEALKNAMpINFEMRLAQIEEQQKLLQETLKKIPEDFERK 200
Cdd:COG4913  321 LREELDELEAQIRGNGgdrlEQLEREIerlERELEERERRRARLEALL-AALGLPLPASAEEFAALRAEAAALLEALEEE 399

                        170       180
                 ....*....|....*....|....*....
gi 21357409  201 LQKLEQNQKDELTKLGAQQSANQVTLKEI 229
Cdd:COG4913  400 LEALEEALAEAEAALRDLRRELRELEAEI 428
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH