NCBI Conserved Domain Search

Conserved domains on [gi|46395874|sp|Q8HY01|]

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RecName: Full=CD209 antigen; AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 1; Short=DC-SIGN1; AltName: CD_antigen=CD209

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132480)

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

CATH: 3.10.100.10

Gene Ontology: GO:0030246

PubMed: 16336259|10508765

SCOP: 4002453

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

CLECT_DC-SIGN_like

cd03590

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...

256-379

3.14e-60

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 191.36 E-value: 3.14e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFAWMGLSDLNQEGTWQWVDGSPL 335
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395874 336 SPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 379
Cdd:cd03590  80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

GumC super family

cl34566

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

71-244

6.83e-08

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

The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.83e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  71 QSKQDAIYQNLTQLKAAVGEL-SEKSKLQEIYQEL-TQLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQ-QEIY 147
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEArAELAEAEARLAALrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNH 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 148 QELTQLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEKSKQqeiYQELTRlkaavg 227
Cdd:COG3206 291 PDVIALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER------ 358

                       170
                ....*....|....*..
gi 46395874 228 elpEKSKQQEIYQELTQ 244
Cdd:COG3206 359 ---EVEVARELYESLLQ 372

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 ...

256-379

3.14e-60

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 191.36 E-value: 3.14e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFAWMGLSDLNQEGTWQWVDGSPL 335
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395874 336 SPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 379
Cdd:cd03590  80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

CLECT

smart00034

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...

256-378

3.48e-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: 133.88 E-value: 3.48e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFAWMGLSDLNQEGTWQWVDGS 333
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395874    334 PLSPSFkqYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWICK 378
Cdd:smart00034  81 GPVSYS--NWAPGEPNN-SSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124

Lectin_C

pfam00059

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

274-379

1.54e-27

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 104.87 E-value: 1.54e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   274 QRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLSPSFkqyWNRGEPNNVGE 353
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395874   354 EDCAE--FSGNGWNDDKCNLAKFWICKK 379
Cdd:pfam00059  78 EDCVElsSSSGKWNDENCNSKNPFVCEK 105

PHA02642

C-type lectin-like protein; Provisional

256-380

7.45e-12

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 64.37 E-value: 7.45e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRfaWMGLSDLNQEGTWQWVDGSPL 335
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 46395874  336 SPSFKQywnrgepnnVGEEDCAEFSGNGWNDDKCNLAKFWICKKS 380
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSKT 201

PCC

TIGR00864

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...

237-392

1.71e-11

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 66.26 E-value: 1.71e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    237 EIYQELTQLKAAVERLCRP-CPWEWTFFQGN--CYFMSNSQRDWHDSVTACQE-VGAQLVVIKSAEEQNFLQLQSSRS-N 311
Cdd:TIGR00864  298 DAAWKITAHGEEPAKASHPhCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    312 RFAWMGLSDLN--QEGTWQWVDGSPLSPSfkQYWNRGEPNNVGEEDCAEFSGNGW-NDDKCNLAKFWICKKSAASCSRDE 388
Cdd:TIGR00864  378 RGVWIGFSDVNgaEKGPAHQGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCELNPGGPVPDA 455


                   ....
gi 46395874    389 EQFL 392
Cdd:TIGR00864  456 ENFA 459

GumC

COG3206

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

71-244

6.83e-08

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.83e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  71 QSKQDAIYQNLTQLKAAVGEL-SEKSKLQEIYQEL-TQLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQ-QEIY 147
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEArAELAEAEARLAALrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNH 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 148 QELTQLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEKSKQqeiYQELTRlkaavg 227
Cdd:COG3206 291 PDVIALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER------ 358

                       170
                ....*....|....*..
gi 46395874 228 elpEKSKQQEIYQELTQ 244
Cdd:COG3206 359 ---EVEVARELYESLLQ 372

PRK03918

DNA double-strand break repair ATPase Rad50;

65-252

6.35e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 6.35e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   65 SSISQEQSKQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAA-VGELPEKSKQ 143
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELREIEKR 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  144 QEIY-QELTQLKAAVGELPEKSKQ-QEIYQELTRLKAAVGELPEKsqqQEIYQELTQLKAAVGELPEKSKQ---QEIYQE 218
Cdd:PRK03918 316 LSRLeEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEER---HELYEEAKAKKEELERLKKRLTGltpEKLEKE 392

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 46395874  219 LTRLKAAVGELPEK-----SKQQEIYQELTQLKAAVERL 252
Cdd:PRK03918 393 LEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

65-252

2.09e-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: 43.52 E-value: 2.09e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874     65 SSISQEQSKQD-AIYQNLTQLKAAVGELSEKSK-LQEIYQELTQLKAAVGELPEK--SKQQEIYQELTQLKAAVGELPEK 140
Cdd:TIGR02169  691 SSLQSELRRIEnRLDELSQELSDASRKIGEIEKeIEQLEQEEEKLKERLEELEEDlsSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    141 SKQQEIYQE-LTQLKAAVGELP------EKSKQQEIYQEL-TRLKAAVGELPEKSQQQEIYQELTQ-LKAAVGELpeKSK 211
Cdd:TIGR02169  771 EEDLHKLEEaLNDLEARLSHSRipeiqaELSKLEEEVSRIeARLREIEQKLNRLTLEKEYLEKEIQeLQEQRIDL--KEQ 848

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 46395874    212 QQEIYQELTRLKAAVGELPE--KSKQQEIYQ---ELTQLKAAVERL 252
Cdd:TIGR02169  849 IKSIEKEIENLNGKKEELEEelEELEAALRDlesRLGDLKKERDEL 894

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 ...

256-379

3.14e-60

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 191.36 E-value: 3.14e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFAWMGLSDLNQEGTWQWVDGSPL 335
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395874 336 SPSfKQYWNRGEPNNVG--EEDCAEFSGN--GWNDDKCNLAKFWICKK 379
Cdd:cd03590  80 NSS-KTFWHPGEPNNWGggGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

CLECT

smart00034

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...

256-378

3.48e-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: 133.88 E-value: 3.48e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFAWMGLSDLNQEGTWQWVDGS 333
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395874    334 PLSPSFkqYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWICK 378
Cdd:smart00034  81 GPVSYS--NWAPGEPNN-SSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124

CLECT

cd00037

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...

266-379

1.55e-36

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

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 129.28 E-value: 1.55e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 266 NCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQ-LQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLSPSFkqYWN 344
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYT--NWA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 46395874 345 RGEPNNVGEEDCAEFSGN---GWNDDKCNLAKFWICKK 379
Cdd:cd00037  79 PGEPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFICEK 116

CLECT_NK_receptors_like

cd03593

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...

256-379

1.12e-31

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: 116.28 E-value: 1.12e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRfaWMGLSDLNQEGTWQWVDGSPL 335
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46395874 336 SPSFKqywnrgEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKK 379
Cdd:cd03593  79 NNLFN------IRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116

CLECT_CEL-1_like

cd03589

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...

256-378

6.45e-28

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 107.06 E-value: 6.45e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVG-----AQLVVIKSAEEQNFL--QLQSSRSNRF---AWMGLSDLNQEG 325
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVydLFESSRGPDTpygLWIGLHDRTSEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46395874 326 TWQWVDGSPLSPSfkqYWNRGEPNN-VGEEDCAEFSGNG-----WNDDKCNLAKFWICK 378
Cdd:cd03589  81 PFEWTDGSPVDFT---KWAGGQPDNyGGNEDCVQMWRRGdagqsWNDMPCDAVFPYICK 136

Lectin_C

pfam00059

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

274-379

1.54e-27

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 104.87 E-value: 1.54e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   274 QRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLSPSFkqyWNRGEPNNVGE 353
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395874   354 EDCAE--FSGNGWNDDKCNLAKFWICKK 379
Cdd:pfam00059  78 EDCVElsSSSGKWNDENCNSKNPFVCEK 105

CLECT_collectin_like

cd03591

C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...

268-377

1.72e-23

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: 94.29 E-value: 1.72e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 268 YFMSNSQR-DWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLSPSfkqYWNRG 346
Cdd:cd03591   3 IFVTNGEEkNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYT---NWKPG 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 46395874 347 EPNNVG-EEDCAE-FSGNGWNDDKCNLAKFWIC 377
Cdd:cd03591  80 EPNNAGgGEDCVEmYTSGKWNDVACNLTRLFVC 112

CLECT_selectins_like

cd03592

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...

268-377

3.93e-19

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 82.42 E-value: 3.93e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 268 YFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFL-QLQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLspSFKQyWNRG 346
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINNEGTWVDTDKKEL--EYKN-WAPG 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 46395874 347 EPNNVGEEDCAE----FSGNgWNDDKCNLAKFWIC 377
Cdd:cd03592  80 EPNNGRNENCLEiyikDNGK-WNDEPCSKKKSAIC 113

CLECT_CSPGs

cd03588

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...

256-379

6.50e-18

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

Pssm-ID: 153058 Cd Length: 124 Bit Score: 79.16 E-value: 6.50e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLqlqSSRSNRFAWMGLSDLNQEGTWQWVDGSPL 335
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46395874 336 spSFKQyWNRGEPNN--VGEEDCAEFSGNG---WNDDKCNLAKFWICKK 379
Cdd:cd03588  78 --QFEN-WRPNQPDNffATGEDCVVMIWHEegeWNDVPCNYHLPFTCKK 123

CLECT_REG-1_like

cd03594

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...

256-378

2.10e-16

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

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 75.10 E-value: 2.10e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEV--GAQLVVIKSAEEQNFLQ---LQSSRSNRFAWMGLSDLNQEGTWQWV 330
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLHDPQQSRGWEWS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 46395874 331 DGSplSPSFKQyWNRGEPNNVGEEdCAEFSGNG----WNDDKCNLAKFWICK 378
Cdd:cd03594  81 DGS--KLDYRS-WDRNPPYARGGY-CAELSRSTgflkWNDANCEERNPFICK 128

CLECT_VCBS

cd03603

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...

277-366

1.20e-15

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

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 72.84 E-value: 1.20e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 277 WHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNrFAWMGLSDLNQEGTWQWVDGSPLSPSFkqyWNRGEP-------- 348
Cdd:cd03603  12 WEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTN---WGSGEPhnngggne 87

                        90
                ....*....|....*...
gi 46395874 349 NNVGEEDCAEFSGnGWND 366
Cdd:cd03603  88 DYAAINHFPGISG-KWND 104

CLECT_tetranectin_like

cd03596

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...

267-377

1.10e-13

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

Pssm-ID: 153066 Cd Length: 129 Bit Score: 67.41 E-value: 1.10e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 267 CYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQ---LQSSRSNRFAWMGLSDLNQEGTWQWVDGSPLspSFKQyW 343
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEGKWVDVNGSPI--SYFN-W 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 46395874 344 NR---GEPNNVGEEDCAEFSG--NG-WNDDKCNLAKFWIC 377
Cdd:cd03596  88 EReitAQPDGGKRENCVALSSsaQGkWFDEDCRREKPYVC 127

PHA02642

C-type lectin-like protein; Provisional

256-380

7.45e-12

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 64.37 E-value: 7.45e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRfaWMGLSDLNQEGTWQWVDGSPL 335
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 46395874  336 SPSFKQywnrgepnnVGEEDCAEFSGNGWNDDKCNLAKFWICKKS 380
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSKT 201

CLECT_1

cd03602

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...

268-377

1.28e-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: 60.85 E-value: 1.28e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 268 YFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFAWMGLSDlnQEGTWQWVDGSPLSPSfkqYWNRGE 347
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYR--DVDSWRWSDGSESSFR---NWNTFQ 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 46395874 348 PNnvGEEDCAEFSGNG-WNDDKCNLAKFWIC 377
Cdd:cd03602  78 PF--GQGDCATMYSSGrWYAALCSALKPFIC 106

PCC

TIGR00864

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...

237-392

1.71e-11

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 66.26 E-value: 1.71e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    237 EIYQELTQLKAAVERLCRP-CPWEWTFFQGN--CYFMSNSQRDWHDSVTACQE-VGAQLVVIKSAEEQNFLQLQSSRS-N 311
Cdd:TIGR00864  298 DAAWKITAHGEEPAKASHPhCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    312 RFAWMGLSDLN--QEGTWQWVDGSPLSPSfkQYWNRGEPNNVGEEDCAEFSGNGW-NDDKCNLAKFWICKKSAASCSRDE 388
Cdd:TIGR00864  378 RGVWIGFSDVNgaEKGPAHQGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCELNPGGPVPDA 455


                   ....
gi 46395874    389 EQFL 392
Cdd:TIGR00864  456 ENFA 459

GumC

COG3206

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

71-244

6.83e-08

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.83e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  71 QSKQDAIYQNLTQLKAAVGEL-SEKSKLQEIYQEL-TQLKAAVGELPEKSKQQEIYQELTQLKAAVGELPEKSKQ-QEIY 147
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEArAELAEAEARLAALrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNH 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 148 QELTQLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEKSKQqeiYQELTRlkaavg 227
Cdd:COG3206 291 PDVIALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELPELEAE---LRRLER------ 358

                       170
                ....*....|....*..
gi 46395874 228 elpEKSKQQEIYQELTQ 244
Cdd:COG3206 359 ---EVEVARELYESLLQ 372

CLECT_EMBP_like

cd03598

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...

265-377

1.17e-07

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

Pssm-ID: 153068 Cd Length: 117 Bit Score: 49.76 E-value: 1.17e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 265 GNCYFMSNSQRDWHDSVTACQEV-GAQLVVIKSAEEQNFLQLQSSRSN--RFaWMGLSDLNQEGTWQ--WVDGSPLSPSf 339
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVICRRCyRGNLASIHSFAFNYRVQRLVSTLNqaQV-WIGGIITGKGRCRRfsWVDGSVWNYA- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 46395874 340 kqYWNRGEPNNvGEEDCAEFSGNG--WNDDKCNLAKFWIC 377
Cdd:cd03598  79 --YWAPGQPGN-RRGHCVELCTRGghWRRAHCKLRRPFIC 115

PHA03097

C-type lectin-like protein; Provisional

256-377

3.92e-07

C-type lectin-like protein; Provisional

Pssm-ID: 222982 [Multi-domain] Cd Length: 157 Bit Score: 49.48 E-value: 3.92e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNF----LQLQSsrsnrfAWMGLSDLNQEGTWQWVD 331
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFvsryKGGQD------LWIGIEKKKGDDDDREVL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46395874  332 GSPLSPSfkqywnrgepnnvGEEDCAEFSGNGWNDDKCNLAKFWIC 377
Cdd:PHA03097 120 DKVVKPP-------------KSGKCAYLKDKTIISSNCNATKGWIC 152

YhaN

COG4717

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

80-252

8.68e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 8.68e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  80 NLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGElpeksKQQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAAVGE 159
Cdd:COG4717  69 NLKELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 160 LPEksKQQEIYQELTRLKAAVGELPEKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELpeKSKQQEIY 239
Cdd:COG4717 144 LPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQ 219

                       170
                ....*....|...
gi 46395874 240 QELTQLKAAVERL 252
Cdd:COG4717 220 EELEELEEELEQL 232

YhaN

COG4717

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

41-254

1.22e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.22e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  41 GALVLQLLSFTLLAGLLIQVSKFPSSISQEQSKQDAIYQNLTQ-----LKAAVG-----ELSEKSKLQEIYQELTQLKAA 110
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleeLLAALGlppdlSPEELLELLDRIEELQELLRE 355

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 111 VGELPEKSKQQEIYQELTQLKAAVG-----ELPEKSKQQEIYQELTQlkaavgelpeksKQQEIYQELTRLKAAVGELPE 185
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLE 423

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395874 186 KSQQQEIYQELTQLKAAVGELPEKskQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCR 254
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490

CLECT_chondrolectin_like

cd03595

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...

268-378

1.86e-06

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: 47.19 E-value: 1.86e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 268 YFMSNSQR-DWHDSVTACQEVGAQLVVIKSAEEQ----NFLQLQSSRSNRFaWMGL---SDLNQEGT-----WQWVDGSP 334
Cdd:cd03595  17 YFQDSRRRlNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDF-WIGLrrsSQYNVTSSacsslYYWLDGSI 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46395874 335 lsPSFKQyWNRGEPNnVGEEDCAEF-------SGNG------WNDDKCNLAKFWICK 378
Cdd:cd03595  96 --STFRN-WYVDEPS-CGSEVCVVMyhqpsapAGQGgpylfqWNDDNCNMKNNFICK 148

GumC

COG3206

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

68-252

7.00e-06

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 7.00e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  68 SQEQSKQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAAVGELpeKSKQQEIY 147
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPEL--RKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEA--RAELAEAE 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 148 QELTQLKAAVG----ELPEKSKQQEIYQELTRLKAAVGELPEKSQQ-QEIYQELTQLKAAVGELpEKSKQQEIYQELTRL 222
Cdd:COG3206 240 ARLAALRAQLGsgpdALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAAL-RAQLQQEAQRILASL 318

                       170       180       190
                ....*....|....*....|....*....|
gi 46395874 223 KAAVGELpeKSKQQEIYQELTQLKAAVERL 252
Cdd:COG3206 319 EAELEAL--QAREASLQAQLAQLEARLAEL 346

CLECT_TC14_like

cd03601

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...

315-379

7.44e-06

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 44.83 E-value: 7.44e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395874 315 WMGLSDL-NQEGTWQWVDGSPLsPSFKQYWNRGEPNN-VGEEDCAE--FSGNGWNDDKCNLAKFWICKK 379
Cdd:cd03601  52 WVGADNLqDGEYDFLWNDGVSL-PTDSDLWAPNEPSNpQSRQLCVQlwSKYNLLDDEYCGRAKRVICEK 119

YhaN

COG4717

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

67-224

2.31e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 2.31e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  67 ISQEQSKQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKQQEIYQELTQLKAAVGELPEKSKQQEI 146
Cdd:COG4717  97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAE 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46395874 147 YQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKA 224
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250

COG1340

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

56-252

2.56e-05

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 2.56e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  56 LLIQVSKFPSSISQEQSKQDAIYQNLTQLKAAVGELSEksKLQEIYQELTQLKAAVGEL-----PEKSKQQEIYQELTQL 130
Cdd:COG1340  48 LNAQVKELREEAQELREKRDELNEKVKELKEERDELNE--KLNELREELDELRKELAELnkaggSIDKLRKEIERLEWRQ 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 131 KAAVgeLPeKSKQQEIYQELTQLKAavgELPEKSKQQEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELpeKS 210
Cdd:COG1340 126 QTEV--LS-PEEEKELVEKIKELEK---ELEKAKKALEKNEKLKELRAELKEL--RKEAEEIHKKIKELAEEAQEL--HE 195

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 46395874 211 KQQEIYQELTRLKAAVGELPEK--SKQQEIYQELTQLKAAVERL 252
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEivEAQEKADELHEEIIELQKEL 239

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

96-250

2.90e-05

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: 44.92 E-value: 2.90e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  96 KLQEIYQELTQLKAAVGELPE-----KSKQQEIYQELTQLKAAVGELpeKSKQQEIYQELTQLKAAVGELPEKSKQ---- 166
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAelaelEDELAALEARLEAAKTELEDL--EKEIKRLELEIEEVEARIKKYEEQLGNvrnn 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 167 ---QEIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEK--SKQQEIYQELTRLKAAVGELpeKSKQQEIYQE 241
Cdd:COG1579  89 keyEALQKEIESLKRRISDL--EDEILELMERIEELEEELAELEAElaELEAELEEKKAELDEELAEL--EAELEELEAE 164


                ....*....
gi 46395874 242 LTQLKAAVE 250
Cdd:COG1579 165 REELAAKIP 173

PRK03918

DNA double-strand break repair ATPase Rad50;

65-252

6.35e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 6.35e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   65 SSISQEQSKQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKQQEIYQELTQLKAA-VGELPEKSKQ 143
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELREIEKR 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  144 QEIY-QELTQLKAAVGELPEKSKQ-QEIYQELTRLKAAVGELPEKsqqQEIYQELTQLKAAVGELPEKSKQ---QEIYQE 218
Cdd:PRK03918 316 LSRLeEEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEER---HELYEEAKAKKEELERLKKRLTGltpEKLEKE 392

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 46395874  219 LTRLKAAVGELPEK-----SKQQEIYQELTQLKAAVERL 252
Cdd:PRK03918 393 LEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431

PRK10929

putative mechanosensitive channel protein; Provisional

81-252

7.42e-05

putative mechanosensitive channel protein; Provisional

Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 7.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    81 LTQLKAAVgeLSEKSKLQEIY---------QELTQLKAavgELPEKsKQQEIYQELTQLKAAVGELpeksKQQEIYQELT 151
Cdd:PRK10929  175 LTALQAES--AALKALVDELElaqlsannrQELARLRS---ELAKK-RSQQLDAYLQALRNQLNSQ----RQREAERALE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   152 ---QLKAAVGELPEK-SKQQEIYQELTR-LKAAVGELPE-KSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTR-LKA 224
Cdd:PRK10929  245 steLLAEQSGDLPKSiVAQFKINRELSQaLNQQAQRMDLiASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGEaLRA 324

                         170       180
                  ....*....|....*....|....*...
gi 46395874   225 AVGELPEKSKQQEIYQELTQLKaaVERL 252
Cdd:PRK10929  325 QVARLPEMPKPQQLDTEMAQLR--VQRL 350

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

65-252

2.09e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 2.09e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874     65 SSISQEQSKQD-AIYQNLTQLKAAVGELSEKSK-LQEIYQELTQLKAAVGELPEK--SKQQEIYQELTQLKAAVGELPEK 140
Cdd:TIGR02169  691 SSLQSELRRIEnRLDELSQELSDASRKIGEIEKeIEQLEQEEEKLKERLEELEEDlsSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    141 SKQQEIYQE-LTQLKAAVGELP------EKSKQQEIYQEL-TRLKAAVGELPEKSQQQEIYQELTQ-LKAAVGELpeKSK 211
Cdd:TIGR02169  771 EEDLHKLEEaLNDLEARLSHSRipeiqaELSKLEEEVSRIeARLREIEQKLNRLTLEKEYLEKEIQeLQEQRIDL--KEQ 848

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 46395874    212 QQEIYQELTRLKAAVGELPE--KSKQQEIYQ---ELTQLKAAVERL 252
Cdd:TIGR02169  849 IKSIEKEIENLNGKKEELEEelEELEAALRDlesRLGDLKKERDEL 894

PHA02867

C-type lectin protein; Provisional

256-303

3.61e-04

C-type lectin protein; Provisional

Pssm-ID: 165201 Cd Length: 167 Bit Score: 40.82 E-value: 3.61e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 46395874  256 CPWEWTFFQGNCYFMSNSQRDWHDSVTACQEVGAQLVVIKSAEEQNFL 303
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96

PRK03918

DNA double-strand break repair ATPase Rad50;

88-246

6.10e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 6.10e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   88 VGELSEKSK-LQEIYQELTQLKAAVGELPEKSKQQEIYQEltQLKAAVGELPEKSKQ-QEIYQELTQLKAAVGELPEKSK 165
Cdd:PRK03918 587 VEELEERLKeLEPFYNEYLELKDAEKELEREEKELKKLEE--ELDKAFEELAETEKRlEELRKELEELEKKYSEEEYEEL 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  166 QQ---EIYQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQ----ELTRLKAAVGELPEKSKQQ-- 236
Cdd:PRK03918 665 REeylELSRELAGLRAELEEL--EKRREEIKKTLEKLKEELEEREKAKKELEKLEkaleRVEELREKVKKYKALLKERal 742

                        170
                 ....*....|....*...
gi 46395874  237 --------EIYQELTQLK 246
Cdd:PRK03918 743 skvgeiasEIFEELTEGK 760

COG1340

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

65-252

1.25e-03

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 1.25e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  65 SSISQEQSKQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAavgelpeksKQQEIYQELTQLKAAVGELpeKSKQQ 144
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEEL--KEKRDELNEELKELAE---------KRDELNAQVKELREEAQEL--REKRD 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 145 EIYQELTQLKAAVGELPEKSKqqEIYQELTRLKAAVGEL-----PEKSQQQEIYQELTQLKAAVgeLPeKSKQQEIYQEL 219
Cdd:COG1340  68 ELNEKVKELKEERDELNEKLN--ELREELDELRKELAELnkaggSIDKLRKEIERLEWRQQTEV--LS-PEEEKELVEKI 142

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 46395874 220 ----TRLKAAVGELPEKSKQQEIYQELTQLKAAVERL 252
Cdd:COG1340 143 keleKELEKAKKALEKNEKLKELRAELKELRKEAEEI 179

PRK10929

putative mechanosensitive channel protein; Provisional

43-246

1.48e-03

putative mechanosensitive channel protein; Provisional

Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 1.48e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    43 LVLQLLSFTLLAGLLIQVSKFPSSISQEQSKQDAIYQNLTQ-LKAAVGELSEKSK------------------LQEIYQE 103
Cdd:PRK10929    8 LMAWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEaLQSALNWLEERKGslerakqyqqvidnfpklSAELRQQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   104 LTQLKAAVGELPEKSKQQEIYQELTQLKAavgELPEKSKQQEIYQELT-QLKAAVGELPEksKQQEIYQELTRLKAAVGE 182
Cdd:PRK10929   88 LNNERDEPRSVPPNMSTDALEQEILQVSS---QLLEKSRQAQQEQDRArEISDSLSQLPQ--QQTEARRQLNEIERRLQT 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   183 LP------EKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAavgELPEKsKQQEIYQELTQLK 246
Cdd:PRK10929  163 LGtpntplAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRS---ELAKK-RSQQLDAYLQALR 228

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

85-247

3.60e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 3.60e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   85 KAAVGElsEKSKLQEIYQELTQLKAavgELPEKSKQ-QEIYQELTQLKAAVGElpEKSKQQEIYQELtqlkaavgelpeK 163
Cdd:PRK00409 508 KKLIGE--DKEKLNELIASLEELER---ELEQKAEEaEALLKEAEKLKEELEE--KKEKLQEEEDKL------------L 568

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  164 SKQQEIYQEltRLKAAvgelpeksqQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEksKQQEIYQELT 243
Cdd:PRK00409 569 EEAEKEAQQ--AIKEA---------KKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK--KKKKQKEKQE 635


                 ....
gi 46395874  244 QLKA 247
Cdd:PRK00409 636 ELKV 639

Smc

COG1196

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

69-252

4.18e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.18e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  69 QEQSKQDAIYQNLTQLKAAVGELS--------EKSKLQEIYQELTQLKAAVGELpekskQQEIYQELTQLKAAVGELpeK 140
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIArleerrreLEERLEELEEELAELEEELEEL-----EEELEELEEELEEAEEEL--E 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 141 SKQQEIYQELTQLKAAVGELpeKSKQQEIYQELTRLKAAVGElpEKSQQQEIYQELTQLKAAVGELpEKSKQQEIYQELT 220
Cdd:COG1196 355 EAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRA--AAELAAQLEELEEAEEALLERL-ERLEEELEELEEA 429

                       170       180       190
                ....*....|....*....|....*....|..
gi 46395874 221 RLKAAVGELPEKSKQQEIYQELTQLKAAVERL 252
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

PTZ00121

MAEBL; Provisional

70-254

5.36e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 5.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874    70 EQSKQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKQQEIYQEltQLKaavgelpeksKQQEIYQE 149
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--ELK----------KAEEEKKK 1634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   150 LTQLKAAVGELPEKSKQQEIYQELTRLKAAV---GELPEKSQQQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAv 226
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE- 1713

                         170       180
                  ....*....|....*....|....*...
gi 46395874   227 gelpEKSKQQEIYQELTQLKAAVERLCR 254
Cdd:PTZ00121 1714 ----EKKKAEELKKAEEENKIKAEEAKK 1737

COG4913

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

71-253

5.78e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 5.78e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   71 QSKQDAIYQNLTQLKAAVGEL-SEKSKLQEIYQELTQLKAAVGelpekskqqeiYQELTQLKAAVGELpeKSKQQEIYQE 149
Cdd:COG4913  294 EAELEELRAELARLEAELERLeARLDALREELDELEAQIRGNG-----------GDRLEQLEREIERL--ERELEERERR 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  150 LTQLKAAVGELPEKSKQQEiyQELTRLKAAVGELPE--KSQQQEIYQELTQLKAAVGELpeKSKQQEIYQELTRLKAAVG 227
Cdd:COG4913  361 RARLEALLAALGLPLPASA--EEFAALRAEAAALLEalEEELEALEEALAEAEAALRDL--RRELRELEAEIASLERRKS 436

                        170       180
                 ....*....|....*....|....*.
gi 46395874  228 ELPekskqqeiyQELTQLKAAVERLC 253
Cdd:COG4913  437 NIP---------ARLLALRDALAEAL 453

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

92-252

6.36e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 6.36e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  92 SEKSKLQEIYQELTQLKAAVGELpeKSKQQEIYQELTQLKAAVGELpeKSKQQEIYQELTQLKAAVGELpeKSKQQEIYQ 171
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAAL--KKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAEL--EKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874 172 ELTRLKAAVGELPEKSQQQEIYQELTQLKAAvGELPEKSKQQEIYQELTR-LKAAVGELpeKSKQQEIYQELTQLKAAVE 250
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSP-EDFLDAVRRLQYLKYLAPaRREQAEEL--RADLAELAALRAELEAERA 174


                ..
gi 46395874 251 RL 252
Cdd:COG4942 175 EL 176

COG4913

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

67-230

6.75e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 6.75e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874   67 ISQEQSKQDAIYQNLTQLKAAVGELsEKSKLQEIYQELTQLKAAVGELpeKSKQQEIYQELTQLKAAVG--ELPEKSKQQ 144
Cdd:COG4913  304 LARLEAELERLEARLDALREELDEL-EAQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAalGLPLPASAE 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395874  145 EIYQELTQLKAAVGELPEKSKQQEiyQELTRLKAAVGELpeKSQQQEIYQELTQLKAAVGELPEksKQQEIYQEL-TRLK 223
Cdd:COG4913  381 EFAALRAEAAALLEALEEELEALE--EALAEAEAALRDL--RRELRELEAEIASLERRKSNIPA--RLLALRDALaEALG 454


                 ....*..
gi 46395874  224 AAVGELP 230
Cdd:COG4913  455 LDEAELP 461

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