NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|334085205|ref|NP_001193948|]
View 

low affinity immunoglobulin epsilon Fc receptor isoform b [Homo sapiens]

Protein Classification

CENP-F_leu_zip and CLECT_DC-SIGN_like domain-containing protein( domain architecture ID 11794892)

CENP-F_leu_zip and CLECT_DC-SIGN_like domain-containing protein

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 smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-281 1.32e-38

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: 133.11  E-value: 1.32e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS----WIGLRNLDLKGEFIWVDGS 237
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 334085205   238 -HVDYSNWAPGEPTSRsqGEDCV-MMRGSGRWNDAFCDRKLGaWVC 281
Cdd:smart00034  81 gPVSYSNWAPGEPNNS--SGDCVvLSTSGGKWNDVSCTSKLP-FVC 123
CENP-F_leu_zip super family cl25924
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 47-147 5.29e-06

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


The actual alignment was detected with superfamily member pfam10473:

Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 45.37  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   47 DTTQSLKQLE-----ERAARNVSQVSKNLESHHgdQMAQKSQSTQISqELEELRAEQQRLKSQDLELSWNLNGLQADLSS 121
Cdd:pfam10473   1 DEKKQLHVLEklkesERKADSLKDKVENLEREL--EMSEENQELAIL-EAENSKAEVETLKAEIEEMAQNLRDLELDLVT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 334085205  122 FKS------QELNERNEASDLLERLREEVTKL 147
Cdd:pfam10473  78 LRSekenltKELQKKQERVSELESLNSSLENL 109
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-281 1.32e-38

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: 133.11  E-value: 1.32e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS----WIGLRNLDLKGEFIWVDGS 237
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 334085205   238 -HVDYSNWAPGEPTSRsqGEDCV-MMRGSGRWNDAFCDRKLGaWVC 281
Cdd:smart00034  81 gPVSYSNWAPGEPNNS--SGDCVvLSTSGGKWNDVSCTSKLP-FVC 123
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 162-281 2.53e-36

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: 127.04  E-value: 2.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS-WIGLRNLDLKGEFIWVDGS--H 238
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTplN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 334085205 239 VDYSNWAPGEPTS-RSQGEDCVMMRG-SGRWNDAFCDRKLgAWVC 281
Cdd:cd03590   81 SSKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCNLEY-RWIC 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 180-283 3.54e-30

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.26  E-value: 3.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  180 TKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS--WIGLRNLDLKGEFIWVDGSHVDYSNWAPgEPTSRSQGED 257
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 334085205  258 CVMM-RGSGRWNDAFCDRKLGaWVCDR 283
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKNP-FVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 161-242 6.56e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.98  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 161 TCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVD 240
Cdd:PHA02642  87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSNYN 166


                 ..
gi 334085205 241 YS 242
Cdd:PHA02642 167 AS 168
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 47-147 5.29e-06

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 45.37  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   47 DTTQSLKQLE-----ERAARNVSQVSKNLESHHgdQMAQKSQSTQISqELEELRAEQQRLKSQDLELSWNLNGLQADLSS 121
Cdd:pfam10473   1 DEKKQLHVLEklkesERKADSLKDKVENLEREL--EMSEENQELAIL-EAENSKAEVETLKAEIEEMAQNLRDLELDLVT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 334085205  122 FKS------QELNERNEASDLLERLREEVTKL 147
Cdd:pfam10473  78 LRSekenltKELQKKQERVSELESLNSSLENL 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
52-152 8.48e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  52 LKQLEERaarnVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERN 131
Cdd:COG4372   75 LEQLEEE----LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150

                         90       100
                 ....*....|....*....|....
gi 334085205 132 EASDL---LERLREEVTKLRMELQ 152
Cdd:COG4372  151 ELKELeeqLESLQEELAALEQELQ 174
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-151 4.13e-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: 41.98  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205    48 TTQSLKQLEERaarnVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLEL--------------SWNLN 113
Cdd:TIGR02169  383 TRDELKDYREK----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeeekedkaleikkqEWKLE 458

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 334085205   114 GLQADLSSFKSQELNERNEasdlLERLREEVTKLRMEL 151
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEE----YDRVEKELSKLQREL 492
46 PHA02562
endonuclease subunit; Provisional
 47-152 2.87e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  47 DTTQSLKQLEERAAR---NVSQVSKNLESHH--------------GDQMAQK--SQSTQISQELEEL---RAEQQRLKSQ 104
Cdd:PHA02562 252 DPSAALNKLNTAAAKiksKIEQFQKVIKMYEkggvcptctqqiseGPDRITKikDKLKELQHSLEKLdtaIDELEEIMDE 331

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334085205 105 DLELSWNLNGLQADLSSFKSQELNERNEASDL---LERL-------REEVTKLRMELQ 152
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVkaaIEELqaefvdnAEELAKLQDELD 389
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-281 1.32e-38

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: 133.11  E-value: 1.32e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS----WIGLRNLDLKGEFIWVDGS 237
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 334085205   238 -HVDYSNWAPGEPTSRsqGEDCV-MMRGSGRWNDAFCDRKLGaWVC 281
Cdd:smart00034  81 gPVSYSNWAPGEPNNS--SGDCVvLSTSGGKWNDVSCTSKLP-FVC 123
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 162-281 2.53e-36

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: 127.04  E-value: 2.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS-WIGLRNLDLKGEFIWVDGS--H 238
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTplN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 334085205 239 VDYSNWAPGEPTS-RSQGEDCVMMRG-SGRWNDAFCDRKLgAWVC 281
Cdd:cd03590   81 SSKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCNLEY-RWIC 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 172-281 3.93e-34

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: 121.19  E-value: 3.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 172 KCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS---WIGLRNLDLKGEFIWVDGS-HVDYSNWAPG 247
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvWIGLNDLSSEGTWKWSDGSpLVDYTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334085205 248 EPTSrSQGEDCVMMRGS--GRWNDAFCDRKLGaWVC 281
Cdd:cd00037   81 EPNP-GGSEDCVVLSSSsdGKWNDVSCSSKLP-FIC 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 180-283 3.54e-30

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.26  E-value: 3.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  180 TKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS--WIGLRNLDLKGEFIWVDGSHVDYSNWAPgEPTSRSQGED 257
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 334085205  258 CVMM-RGSGRWNDAFCDRKLGaWVCDR 283
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKNP-FVCEK 105
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 162-281 1.14e-27

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: 104.75  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCY-YFGKGtKQWVHAR-----YACDDMEGQLVSIHSPEEQDFLT-------KHASHTGSWIGLRNLDLK 228
Cdd:cd03589    1 CPTFWTAFGGYCYrFFGDR-LTWEEAElrcrsFSIPGLIAHLVSIHSQEENDFVYdlfessrGPDTPYGLWIGLHDRTSE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334085205 229 GEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMR----GSGRWNDAFCDRKLgAWVC 281
Cdd:cd03589   80 GPFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWrrgdAGQSWNDMPCDAVF-PYIC 135
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 162-276 4.04e-24

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: 94.95  E-value: 4.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHAsHTGSWIGLRNLDLKGEFIWVDGSHVDY 241
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNA-QDYQWIGLNDRTIEGDFRWSDGHPLQF 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 334085205 242 SNWAPGEPTSR-SQGEDCVMMRG--SGRWNDAFCDRKL 276
Cdd:cd03588   80 ENWRPNQPDNFfATGEDCVVMIWheEGEWNDVPCNYHL 117
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 162-281 4.39e-21

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: 86.62  E-value: 4.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGShvDY 241
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGS--PL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 334085205 242 SNWapGEPTSRSQGEDCVMMrGSGRWNDAFCDRKLGaWVC 281
Cdd:cd03593   79 NNL--FNIRGSTKSGNCAYL-SSTGIYSEDCSTKKR-WIC 114
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 174-269 3.29e-19

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: 81.70  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 174 YYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASH-TGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTS- 251
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGyGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNn 82

                         90       100
                 ....*....|....*....|..
gi 334085205 252 RSQGEDCVMMRG----SGRWND 269
Cdd:cd03603   83 GGGNEDYAAINHfpgiSGKWND 104
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 174-283 8.57e-18

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: 77.80  E-value: 8.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 174 YYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHA-SHTGS--WIGLRnlDLKGEFIWVD--GSHVDYSNWAPGE 248
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlKYNLGyyWIDGN--DINNEGTWVDtdKKELEYKNWAPGE 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334085205 249 PTSRsQGEDCVMM--RGSGRWNDAFCDRKLGAwVCDR 283
Cdd:cd03592   81 PNNG-RNENCLEIyiKDNGKWNDEPCSKKKSA-ICYT 115
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 172-287 7.81e-16

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: 72.33  E-value: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 172 KCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS--WIGLRNLDLKGEFIWVDGSHVDYSNWAPGEP 249
Cdd:cd03591    2 KIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTyaFIGITDLETEGQFVYLDGGPLTYTNWKPGEP 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 334085205 250 TSRSQGEDCVMMRGSGRWNDAFCDRKlgawvcdRLATC 287
Cdd:cd03591   82 NNAGGGEDCVEMYTSGKWNDVACNLT-------RLFVC 112
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 162-281 1.30e-15

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: 72.02  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCY-YFGKgTKQWVHARYACDDME--GQLVSIHSPEEQDFLTKH--ASHTGS---WIGLRNLDLKGEFIW 233
Cdd:cd03594    1 CPKGWLPYKGNCYgYFRQ-PLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLisSYQKAYqpvWIGLHDPQQSRGWEW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334085205 234 VDGSHVDYSNWAPGEPTSRsqGEDCVMMRGSG---RWNDAFCDRKLgAWVC 281
Cdd:cd03594   80 SDGSKLDYRSWDRNPPYAR--GGYCAELSRSTgflKWNDANCEERN-PFIC 127
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 172-281 3.51e-15

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 70.56  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 172 KCYYFGKGTKQWVHARYACDDM-EGQLVSIHSPEEQDFLTKHAS---HTGSWIGLRnLDLKG---EFIWVDGSHVDYSNW 244
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRCyRGNLASIHSFAFNYRVQRLVStlnQAQVWIGGI-ITGKGrcrRFSWVDGSVWNYAYW 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334085205 245 APGEPtsRSQGEDCVMM--RGsGRWNDAFCDRKLgAWVC 281
Cdd:cd03598   81 APGQP--GNRRGHCVELctRG-GHWRRAHCKLRR-PFIC 115
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 161-242 6.56e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.98  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 161 TCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVD 240
Cdd:PHA02642  87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSNYN 166


                 ..
gi 334085205 241 YS 242
Cdd:PHA02642 167 AS 168
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 174-272 3.88e-11

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: 59.31  E-value: 3.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 174 YYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTK--HASHTGSWIGLRnlDLKGEFIWVDGSHVDYSNWAPGEPTs 251
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNlsRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNTFQPF- 79

                         90       100
                 ....*....|....*....|.
gi 334085205 252 rsQGEDCVMMRGSGRWNDAFC 272
Cdd:cd03602   80 --GQGDCATMYSSGRWYAALC 98
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 175-282 5.87e-11

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: 59.08  E-value: 5.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 175 YFGKGTKQWVHARYACDDMEGQLVSIHSPE---EQDFLTKHA-SHTGSWIGLRNL-DLKGEFIWVDGSHV--DYSNWAPG 247
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLASLAMRDsemRDAILAFTLvKGHGYWVGADNLqDGEYDFLWNDGVSLptDSDLWAPN 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334085205 248 EPTSRSQGEDCVMM-RGSGRWNDAFCDRKLGAwVCD 282
Cdd:cd03601   84 EPSNPQSRQLCVQLwSKYNLLDDEYCGRAKRV-ICE 118
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 169-275 5.71e-09

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 54.13  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 169 FQRKCY---YFGKGTKQ--WVHARYACDDMEGQLVSIHSPEEQDFLTK-----HASHTGSWIGLR--------NLDLKGE 230
Cdd:cd03595    8 TEKPCYkiaYFQDSRRRlnFEEARQACREDGGELLSIESENEQKLIERfiqtlRASDGDFWIGLRrssqynvtSSACSSL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334085205 231 FIWVDGSHVDYSNWAPGEPTSRSqgEDCVMM-------RGSG-----RWNDAFCDRK 275
Cdd:cd03595   88 YYWLDGSISTFRNWYVDEPSCGS--EVCVVMyhqpsapAGQGgpylfQWNDDNCNMK 142
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 171-281 5.82e-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: 53.55  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 171 RKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLT---KHASHTGS--WIGLRNLDLKGEFIWVDGSHVDYSNW- 244
Cdd:cd03596    9 KKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWevWLGINDMVAEGKWVDVNGSPISYFNWe 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 334085205 245 --APGEPTSRSQgEDCVMMRGS--GRWNDAFCDRKLgAWVC 281
Cdd:cd03596   89 reITAQPDGGKR-ENCVALSSSaqGKWFDEDCRREK-PYVC 127
PHA02867 PHA02867
C-type lectin protein; Provisional
 162-220 1.24e-07

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 50.84  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHAShTGSWI 220
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRYGK-GSYWI 106
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 173-281 1.51e-07

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 49.74  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 173 CYYFGKGTKQWVHARYACDDMEGQLVSIHSPEE---------QDFLTKHASHTGSWIGLR---------NLDLKGeFIWV 234
Cdd:cd03600    6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEadvvslllaAGPGRHGRGSLRLWIGLQreprqcsdpSLPLRG-FSWV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334085205 235 DG-SHVDYSNWaPGEPTSRSQGEDCVMMRGSG------RWNDAFCDRKLGAWVC 281
Cdd:cd03600   85 TGdQDTDFSNW-LQEPAGTCTSPRCVALSAAGstpdnlKWKDGPCSARADGYLC 137
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 162-281 1.20e-06

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 47.55  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLkgefiWVDGSHVdy 241
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKG-----DDDDREV-- 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 334085205 242 snwaPGEPTSRSQGEDCVMMRGSGrWNDAFCDRKLGaWVC 281
Cdd:PHA03097 119 ----LDKVVKPPKSGKCAYLKDKT-IISSNCNATKG-WIC 152
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 47-147 5.29e-06

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 45.37  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   47 DTTQSLKQLE-----ERAARNVSQVSKNLESHHgdQMAQKSQSTQISqELEELRAEQQRLKSQDLELSWNLNGLQADLSS 121
Cdd:pfam10473   1 DEKKQLHVLEklkesERKADSLKDKVENLEREL--EMSEENQELAIL-EAENSKAEVETLKAEIEEMAQNLRDLELDLVT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 334085205  122 FKS------QELNERNEASDLLERLREEVTKL 147
Cdd:pfam10473  78 LRSekenltKELQKKQERVSELESLNSSLENL 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
52-152 8.48e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  52 LKQLEERaarnVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERN 131
Cdd:COG4372   75 LEQLEEE----LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150

                         90       100
                 ....*....|....*....|....
gi 334085205 132 EASDL---LERLREEVTKLRMELQ 152
Cdd:COG4372  151 ELKELeeqLESLQEELAALEQELQ 174
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-151 4.13e-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: 41.98  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205    48 TTQSLKQLEERaarnVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLEL--------------SWNLN 113
Cdd:TIGR02169  383 TRDELKDYREK----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeeekedkaleikkqEWKLE 458

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 334085205   114 GLQADLSSFKSQELNERNEasdlLERLREEVTKLRMEL 151
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEE----YDRVEKELSKLQREL 492
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
47-152 7.58e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  47 DTTQSLKQLEERAAR---NVSQVSKNLE---SHHGDqMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLS 120
Cdd:COG3206  172 EARKALEFLEEQLPElrkELEEAEAALEefrQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334085205 121 SfKSQELNERNEaSDLLERLREEVTKLRMELQ 152
Cdd:COG3206  251 S-GPDALPELLQ-SPVIQQLRAQLAELEAELA 280
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
50-152 1.24e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  50 QSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLssfksQEL-N 128
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-----EELqK 122

                         90       100
                 ....*....|....*....|....
gi 334085205 129 ERNEASDLLERLREEVTKLRMELQ 152
Cdd:COG4372  123 ERQDLEQQRKQLEAQIAELQSEIA 146
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
51-152 2.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  51 SLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQ---EL 127
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQ 93

                         90       100
                 ....*....|....*....|....*
gi 334085205 128 NERNEASDLLERLREEVTKLRMELQ 152
Cdd:COG4372   94 AELAQAQEELESLQEEAEELQEELE 118
46 PHA02562
endonuclease subunit; Provisional
 47-152 2.87e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205  47 DTTQSLKQLEERAAR---NVSQVSKNLESHH--------------GDQMAQK--SQSTQISQELEEL---RAEQQRLKSQ 104
Cdd:PHA02562 252 DPSAALNKLNTAAAKiksKIEQFQKVIKMYEkggvcptctqqiseGPDRITKikDKLKELQHSLEKLdtaIDELEEIMDE 331

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334085205 105 DLELSWNLNGLQADLSSFKSQELNERNEASDL---LERL-------REEVTKLRMELQ 152
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVkaaIEELqaefvdnAEELAKLQDELD 389
Adeno_E3_15_3 pfam03307
Adenovirus 15.3kD protein in E3 region;
125-181 3.11e-03

Adenovirus 15.3kD protein in E3 region;


Pssm-ID: 460880  Cd Length: 117  Bit Score: 37.06  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 334085205  125 QELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCpekwinfQRKCYYFGKGTK 181
Cdd:pfam03307   7 LELDEINKAARELERLKAASEDERLKHECEDGIFCHQC-------KAGIFCEKKQAG 56
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 50-148 3.68e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.85  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   50 QSLKQLEERAARNVSQVSKNLESHHgdQMAQKSQS---------TQISQELEELRAEQQRLKSQdlelswnLNGLQADLS 120
Cdd:pfam07926  11 KRLKEEAADAEAQLQKLQEDLEKQA--EIAREAQQnyerelvlhAEDIKALQALREELNELKAE-------IAELKAEAE 81

                          90       100
                  ....*....|....*....|....*...
gi 334085205  121 SFKSQELNERNEASDLLERLREEVTKLR 148
Cdd:pfam07926  82 SAKAELEESEESWEEQKKELEKELSELE 109
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-144 6.65e-03

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: 38.11  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205    52 LKQLEERAARNVSQVSKNLESHHGDQM-AQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKsQELNER 130
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-RELAQL 487

                           90
                   ....*....|....
gi 334085205   131 NEASDLLERLREEV 144
Cdd:TIGR02168  488 QARLDSLERLQENL 501
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
47-152 7.08e-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: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   47 DTTQSLKQLEERAARnvsqvsknLESHHGDQMAQKSQSTQISQELEELRAEQQRLksqdLELSW---NLNGLQADLSSfK 123
Cdd:COG4913   607 DNRAKLAALEAELAE--------LEEELAEAEERLEALEAELDALQERREALQRL----AEYSWdeiDVASAEREIAE-L 673

                          90       100
                  ....*....|....*....|....*....
gi 334085205  124 SQELNERNEASDLLERLREEVTKLRMELQ 152
Cdd:COG4913   674 EAELERLDASSDDLAALEEQLEELEAELE 702
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 162-250 7.36e-03

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: 36.02  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205 162 CPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGS-------WIGLRNLDLKgEFIWV 234
Cdd:cd03597    1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMtkqkltpWVGLRKINVS-YWCWE 79

                         90
                 ....*....|....*...
gi 334085205 235 DGSHVDYS--NWAPGEPT 250
Cdd:cd03597   80 DMSPFTNTtlQWLPGEPS 97
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 49-152 8.66e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 36.97  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334085205   49 TQSLKQLEERAARNVSQVSKNLESHHGdqmAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQE-L 127
Cdd:pfam04012  74 QAALTKGNEELAREALAEKKSLEKQAE---ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEaV 150

                          90       100       110
                  ....*....|....*....|....*....|.
gi 334085205  128 NER------NEASDLLERLREEVtkLRMELQ 152
Cdd:pfam04012 151 QTSlgslstSSATDSFERIEEKI--EEREAR 179
 
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