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Conserved domains on  [gi|223278353|ref|NP_001138383|]
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C-type lectin domain family 4 member M isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 240-284 5.12e-17

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


The actual alignment was detected with superfamily member cd03590:

Pssm-ID: 470576 [Multi-domain]  Cd Length: 126  Bit Score: 75.42  E-value: 5.12e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQ 45
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-208 2.31e-05

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  51 LSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPEKSKLQEI 130
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAE 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223278353 131 YQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKA 208
Cdd:COG4717  175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 240-284 5.12e-17

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: 75.42  E-value: 5.12e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQ 45
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 240-284 6.01e-12

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: 61.85  E-value: 6.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 223278353   240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEN 45
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-208 2.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  51 LSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPEKSKLQEI 130
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAE 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223278353 131 YQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKA 208
Cdd:COG4717  175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
PHA02867 PHA02867
C-type lectin protein; Provisional
 233-276 6.23e-05

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 42.75  E-value: 6.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 223278353 233 FERLCRHCPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLV 276
Cdd:PHA02867  42 FPYFSKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLI 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-233 4.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  43 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpEKSKLQEIYQELTRLKAAVGELp 122
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKL- 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 123 eKSKLQEIYQELTRLKAAVGELPE-KSKLQEIYQELTRLKAAVGELPEKS---------KLQEIYQELTELKAAVGELPE 192
Cdd:PRK03918 538 -KGEIKSLKKELEKLEELKKKLAElEKKLDELEEELAELLKELEELGFESveeleerlkELEPFYNEYLELKDAEKELER 616

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223278353 193 KSKLQEIYQEltQLKAAVGELPDQSKQ-QQIYQELTDLKTAF 233
Cdd:PRK03918 617 EEKELKKLEE--ELDKAFEELAETEKRlEELRKELEELEKKY 656
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 240-284 5.12e-17

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: 75.42  E-value: 5.12e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQ 45
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 240-284 6.01e-12

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: 61.85  E-value: 6.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 223278353   240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEN 45
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 240-284 7.28e-11

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: 58.50  E-value: 7.28e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEEL 45
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 250-284 8.25e-07

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: 46.84  E-value: 8.25e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 223278353 250 NCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQ 284
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEEN 35
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 240-284 3.66e-06

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: 45.81  E-value: 3.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQE-----VRAQLVVIKTAEEQ 284
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEEN 50
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 240-285 8.10e-06

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: 44.49  E-value: 8.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQL 285
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQE 46
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-208 2.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  51 LSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPEKSKLQEI 130
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAE 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223278353 131 YQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKA 208
Cdd:COG4717  175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
64-236 2.37e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  64 NLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGElpeksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGE 143
Cdd:COG4717   69 NLKELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 144 LPEksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKAAVGELpdQSKQQQIY 223
Cdd:COG4717  144 LPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQ 219

                        170
                 ....*....|...
gi 223278353 224 QELTDLKTAFERL 236
Cdd:COG4717  220 EELEELEEELEQL 232
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
79-224 4.37e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  79 SKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELT 158
Cdd:COG3206  219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223278353 159 RLKAAVGELpEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELPDQSKQQQIYQ 224
Cdd:COG3206  295 ALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAELRRLE 357
PHA02867 PHA02867
C-type lectin protein; Provisional
 233-276 6.23e-05

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 42.75  E-value: 6.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 223278353 233 FERLCRHCPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLV 276
Cdd:PHA02867  42 FPYFSKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLI 85
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 240-283 8.09e-05

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: 41.59  E-value: 8.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVR--AQLVVIKTAEE 283
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAE 46
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
30-238 8.38e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  30 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 97
Cdd:COG4717  279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  98 LPEKSKLQEIYQELTRL--KAAVGELPEKSKLQEIYQELTRLKAavgelpeksKLQEIYQELTRLKAAVGELPEKSKLQE 175
Cdd:COG4717  359 LEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEEYQELKE---------ELEELEEQLEELLGELEELLEALDEEE 429

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223278353 176 IYQELTELKAAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCR 238
Cdd:COG4717  430 LEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 240-283 2.01e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 41.64  E-value: 2.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEE 283
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEE 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-233 4.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  43 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpEKSKLQEIYQELTRLKAAVGELp 122
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKL- 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 123 eKSKLQEIYQELTRLKAAVGELPE-KSKLQEIYQELTRLKAAVGELPEKS---------KLQEIYQELTELKAAVGELPE 192
Cdd:PRK03918 538 -KGEIKSLKKELEKLEELKKKLAElEKKLDELEEELAELLKELEELGFESveeleerlkELEPFYNEYLELKDAEKELER 616

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223278353 193 KSKLQEIYQEltQLKAAVGELPDQSKQ-QQIYQELTDLKTAF 233
Cdd:PRK03918 617 EEKELKKLEE--ELDKAFEELAETEKRlEELRKELEELEKKY 656
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-236 4.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  43 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVgelp 122
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY---- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 123 eKSKLQEIYQELTRLKAAVGELPE--------KSKLQEIYQELTRLKAAVGELPEKSKLqeiYQELTELKAAVGELPEKS 194
Cdd:PRK03918 306 -LDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRL 381

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 223278353 195 K---LQEIYQELTQLKAAVGELPDQ-----SKQQQIYQELTDLKTAFERL 236
Cdd:PRK03918 382 TgltPEKLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 80-243 9.79e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  80 KLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSK---------- 149
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPA--ELAELEDELAALEARLEAA--KTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 150 ----LQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVgelpdQSKQQQIYQE 225
Cdd:COG1579   87 nnkeYEALQKEIESLKRRISDL--EDEILELMERIEELEEELAEL--EAELAELEAELEEKKAEL-----DEELAELEAE 157

                        170
                 ....*....|....*...
gi 223278353 226 LTDLKTAFERLCRHCPKD 243
Cdd:COG1579  158 LEELEAEREELAAKIPPE 175
46 PHA02562
endonuclease subunit; Provisional
 78-234 3.54e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  78 KSKLQEIYQELTQLKAAVGELPEKSKLQEIYQE---------LTRLKAAVGELPEKSKlqEIYQELTRLKAAVGELPEK- 147
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEeqrkkngenIARKQNKYDELVEEAK--TIKAEIEELTDELLNLVMDi 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353 148 ----SKLQEIYQELTRLKAAVGELpekSKLQEIY----------QELTELKAAVGELpeKSKLQEIYQELTQLKAAVGEL 213
Cdd:PHA02562 251 edpsAALNKLNTAAAKIKSKIEQF---QKVIKMYekggvcptctQQISEGPDRITKI--KDKLKELQHSLEKLDTAIDEL 325

                        170       180
                 ....*....|....*....|..
gi 223278353 214 PDQSKQ-QQIYQELTDLKTAFE 234
Cdd:PHA02562 326 EEIMDEfNEQSKKLLELKNKIS 347
COG5022 COG5022
Myosin heavy chain [General function prediction only];
53-230 4.16e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 38.91  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353   53 QEQSEQDAIYQNLTQLKAAVGELSE-KSKLQEIYQELTQLKAAVGELP-EKSKLQEiyQELTRLKaavgELPEKSKLQEI 130
Cdd:COG5022   872 QSAQRVELAERQLQELKIDVKSISSlKLVNLELESEIIELKKSLSSDLiENLEFKT--ELIARLK----KLLNNIDLEEG 945

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  131 YQ-ELTRLKAAVGELPEKSKLQEIYQELTRL----KAAVGEL-PEKSKLQEIYQELTELKAAVGELPEKSK-LQEIYQEL 203
Cdd:COG5022   946 PSiEYVKLPELNKLHEVESKLKETSEEYEDLlkksTILVREGnKANSELKNFKKELAELSKQYGALQESTKqLKELPVEV 1025

                         170       180
                  ....*....|....*....|....*..
gi 223278353  204 TQLKAAVGELPDQSKQQQIYQELTDLK 230
Cdd:COG5022  1026 AELQSASKIISSESTELSILKPLQKLK 1052
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-214 6.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353   51 LSQEQSEQDAIYQNLTQLKAAVGELsEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEi 130
Cdd:COG4913   304 LARLEAELERLEARLDALREELDEL-EAQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAALGLPLPASA- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223278353  131 yQELTRLKAAVGELPE--KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEksKLQEIYQEL-TQLK 207
Cdd:COG4913   380 -EEFAALRAEAAALLEalEEELEALEEALAEAEAALRDL--RRELRELEAEIASLERRKSNIPA--RLLALRDALaEALG 454


                  ....*..
gi 223278353  208 AAVGELP 214
Cdd:COG4913   455 LDEAELP 461
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 240-285 7.14e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 36.38  E-value: 7.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 223278353 240 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQL 285
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVL 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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