NCBI Conserved Domain Search

Conserved domains on [gi|46395990|sp|Q9H2X3|]

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RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; AltName: Full=DC-SIGN-related protein; Short=DC-SIGNR; AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 2; Short=DC-SIGN2; AltName: Full=Liver/lymph node-specific ICAM-3-grabbing non-integrin; Short=L-SIGN; AltName: CD_antigen=CD299

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 ...

268-391

5.19e-58

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: 185.20 E-value: 5.19e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395990 348 SPSfQRYWNSGEPNN--SGNEDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:cd03590  80 NSS-KTFWHPGEPNNwgGGGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

YhaN super family

cl34808

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

58-266

2.82e-08

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: 55.54 E-value: 2.82e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395990 201 LQEIYQELTELKAAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCR 266
Cdd:COG4717 427 EEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490

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 ...

268-391

5.19e-58

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 185.20 E-value: 5.19e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395990 348 SPSfQRYWNSGEPNN--SGNEDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:cd03590  80 NSS-KTFWHPGEPNNwgGGGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

CLECT

smart00034

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

268-390

8.80e-39

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: 135.42 E-value: 8.80e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSRSNRFSWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395990    346 PLSPSFqrYWNSGEPNNsGNEDCAEFSGSG--WNDNRCDVDNYWICK 390
Cdd:smart00034  81 GPVSYS--NWAPGEPNN-SSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124

Lectin_C

pfam00059

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

286-391

3.94e-31

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 114.50 E-value: 3.94e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   286 QRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqryWNSGEPNNSGN 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395990   366 EDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:pfam00059  78 EDCVELSSSsgKWNDENCNSKNPFVCEK 105

PHA02642

C-type lectin-like protein; Provisional

268-391

5.02e-14

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 70.53 E-value: 5.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRfsWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 46395990  348 SPSFQRywnsgepnnSGNEDCAEFSGSGWNDNRCDVDNYWICKK 391
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSK 200

PCC

TIGR00864

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

267-390

8.44e-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: 63.95 E-value: 8.44e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    267 HCPKDWTFFQGN--CYFMSNSQRNWHDSVTACQE-VRAQLVVIKTAEEQNFLQLQTSRS-NRFSWMGLSDLN--QEGTWQ 340
Cdd:TIGR00864  317 HCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 46395990    341 WVDGSPLSPSfqRYWNSGEPNNSGNEDCAEFSGSGW-NDNRCDVDNYWICK 390
Cdd:TIGR00864  397 QGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCE 445

YhaN

COG4717

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

58-266

2.82e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.82e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395990 201 LQEIYQELTELKAAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCR 266
Cdd:COG4717 427 EEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490

PRK03918

DNA double-strand break repair ATPase Rad50;

71-264

1.03e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.03e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVgelp 150
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY---- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  151 eKSKLQEIYQELTRLKAAVGELPE--------KSKLQEIYQELTRLKAAVGELPEKSKLqeiYQELTELKAAVGELPEKS 222
Cdd:PRK03918 306 -LDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRL 381

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 46395990  223 K---LQEIYQELTQLKAAVGELPDQ-----SKQQQIYQELTDLKTAFERL 264
Cdd:PRK03918 382 TgltPEKLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

152-268

3.32e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 3.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    152 KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEK--SKLQEIYQELTELKAAVgeLPEKSKLQEIYQ 229
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKL--RDRKDALEEELRQLKQLEDELEDCdpTELDRAKEKLKKLLQEI--MIKVKKLEELEE 232

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 46395990    230 ELTQLKAAVGELpdQSKQQQIYQELTDLKTAFERlCRHC 268
Cdd:smart00787 233 ELQELESKIEDL--TNKKSELNTEIAEAEKKLEQ-CRGF 268

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 ...

268-391

5.19e-58

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 185.20 E-value: 5.19e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395990 348 SPSfQRYWNSGEPNN--SGNEDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:cd03590  80 NSS-KTFWHPGEPNNwgGGGEDCAELVYDsgGWNDVPCNLEYRWICEK 126

CLECT

smart00034

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

268-390

8.80e-39

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: 135.42 E-value: 8.80e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSRSNRFSWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395990    346 PLSPSFqrYWNSGEPNNsGNEDCAEFSGSG--WNDNRCDVDNYWICK 390
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 ...

278-391

1.76e-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: 128.89 E-value: 1.76e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 278 NCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSR-SNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqrYWN 356
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKsSSSDVWIGLNDLSSEGTWKWSDGSPLVDYT--NWA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 46395990 357 SGEPNNSGNEDCAEFSGS---GWNDNRCDVDNYWICKK 391
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); ...

268-391

1.19e-33

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: 121.67 E-value: 1.19e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSnrFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEKPWKWIDGSPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46395990 348 SPSFQRywnsgePNNSGNEDCAEFSGSGWNDNRCDVDNYWICKK 391
Cdd:cd03593  79 NNLFNI------RGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116

CLECT_CEL-1_like

cd03589

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

268-390

1.10e-31

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: 117.07 E-value: 1.10e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQE-----VRAQLVVIKTAEEQNFL--QLQTSRSNRFS---WMGLSDLNQEG 337
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydLFESSRGPDTPyglWIGLHDRTSEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46395990 338 TWQWVDGSPLSPSfqrYWNSGEPNNS-GNEDCAEF-----SGSGWNDNRCDVDNYWICK 390
Cdd:cd03589  81 PFEWTDGSPVDFT---KWAGGQPDNYgGNEDCVQMwrrgdAGQSWNDMPCDAVFPYICK 136

Lectin_C

pfam00059

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

286-391

3.94e-31

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 114.50 E-value: 3.94e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   286 QRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqryWNSGEPNNSGN 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395990   366 EDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:pfam00059  78 EDCVELSSSsgKWNDENCNSKNPFVCEK 105

CLECT_collectin_like

cd03591

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

280-389

6.70e-22

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: 89.66 E-value: 6.70e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 280 YFMSNSQR-NWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSfqrYWNSG 358
Cdd:cd03591   3 IFVTNGEEkNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYT---NWKPG 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 46395990 359 EPNNSG-NEDCAE-FSGSGWNDNRCDVDNYWIC 389
Cdd:cd03591  80 EPNNAGgGEDCVEmYTSGKWNDVACNLTRLFVC 112

CLECT_REG-1_like

cd03594

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

268-390

9.30e-20

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: 84.35 E-value: 9.30e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVR--AQLVVIKTAEEQNFL-----QLQTSRSNrfSWMGLSDLNQEGTWQ 340
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIaslisSYQKAYQP--VWIGLHDPQQSRGWE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46395990 341 WVDGSplSPSFqRYWNSGEPNNSGnEDCAEFSGSG----WNDNRCDVDNYWICK 390
Cdd:cd03594  79 WSDGS--KLDY-RSWDRNPPYARG-GYCAELSRSTgflkWNDANCEERNPFICK 128

CLECT_CSPGs

cd03588

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

268-391

2.17e-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: 80.70 E-value: 2.17e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLqlqTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46395990 348 spSFQRyWNSGEPNN--SGNEDCAEFSG--SG-WNDNRCDVDNYWICKK 391
Cdd:cd03588  78 --QFEN-WRPNQPDNffATGEDCVVMIWheEGeWNDVPCNYHLPFTCKK 123

CLECT_selectins_like

cd03592

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

280-389

4.32e-18

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

Pssm-ID: 153062 Cd Length: 115 Bit Score: 79.34 E-value: 4.32e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 280 YFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL-QLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSpsfQRYWNSG 358
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINNEGTWVDTDKKELE---YKNWAPG 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 46395990 359 EPNNSGNEDCAE--FSGSG-WNDNRCDVDNYWIC 389
Cdd:cd03592  80 EPNNGRNENCLEiyIKDNGkWNDEPCSKKKSAIC 113

CLECT_VCBS

cd03603

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

288-378

4.24e-16

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: 74.00 E-value: 4.24e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 288 NWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNrFSWMGLSDLNQEGTWQWVDGsplSPSFQRYWNSGEP--NNSGN 365
Cdd:cd03603  11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDG---EESTYTNWGSGEPhnNGGGN 86

                        90
                ....*....|....*...
gi 46395990 366 EDCA---EFSGS--GWND 378
Cdd:cd03603  87 EDYAainHFPGIsgKWND 104

PHA02642

C-type lectin-like protein; Provisional

268-391

5.02e-14

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 70.53 E-value: 5.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRfsWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 46395990  348 SPSFQRywnsgepnnSGNEDCAEFSGSGWNDNRCDVDNYWICKK 391
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSK 200

CLECT_1

cd03602

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

280-389

2.21e-13

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: 65.86 E-value: 2.21e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 280 YFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDlnQEGTWQWVDGSPLSPsfqRYWNSGE 359
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYR--DVDSWRWSDGSESSF---RNWNTFQ 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 46395990 360 PnnSGNEDCAEFSGSG-WNDNRCDVDNYWIC 389
Cdd:cd03602  78 P--FGQGDCATMYSSGrWYAALCSALKPFIC 106

CLECT_tetranectin_like

cd03596

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

279-389

2.31e-11

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: 60.87 E-value: 2.31e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 279 CYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ---LQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFQRYW 355
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWERE 90

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 46395990 356 NSGEPNNSGNEDCAEFSGSG---WNDNRCDVDNYWIC 389
Cdd:cd03596  91 ITAQPDGGKRENCVALSSSAqgkWFDEDCRREKPYVC 127

PCC

TIGR00864

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

267-390

8.44e-11

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 63.95 E-value: 8.44e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    267 HCPKDWTFFQGN--CYFMSNSQRNWHDSVTACQE-VRAQLVVIKTAEEQNFLQLQTSRS-NRFSWMGLSDLN--QEGTWQ 340
Cdd:TIGR00864  317 HCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 46395990    341 WVDGSPLSPSfqRYWNSGEPNNSGNEDCAEFSGSGW-NDNRCDVDNYWICK 390
Cdd:TIGR00864  397 QGEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCE 445

YhaN

COG4717

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

58-266

2.82e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.82e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395990 201 LQEIYQELTELKAAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCR 266
Cdd:COG4717 427 EEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490

YhaN

COG4717

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

92-264

4.50e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.50e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  92 NLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGElpeksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGE 171
Cdd:COG4717  69 NLKELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 172 LPEksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKAAVGELpdQSKQQQIY 251
Cdd:COG4717 144 LPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQ 219

                       170
                ....*....|...
gi 46395990 252 QELTDLKTAFERL 264
Cdd:COG4717 220 EELEELEEELEQL 232

YhaN

COG4717

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

79-236

8.76e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.76e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  79 LSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPE-KSKLQE 157
Cdd:COG4717  97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEElEAELAE 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46395990 158 IYQELTRLKAAVGeLPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKA 236
Cdd:COG4717 175 LQEELEELLEQLS-LATEEELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250

CLECT_chondrolectin_like

cd03595

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

280-390

9.38e-08

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: 51.04 E-value: 9.38e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 280 YFMSNSQR-NWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSR-SNRFSWMGL---SDLNQEGT-----WQWVDGSPl 347
Cdd:cd03595  17 YFQDSRRRlNFEEARQACREDGGELLSIESENEQKLIErfIQTLRaSDGDFWIGLrrsSQYNVTSSacsslYYWLDGSI- 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46395990 348 spSFQRYWNSGEPNnSGNEDCAEF-------SGSG------WNDNRCDVDNYWICK 390
Cdd:cd03595  96 --STFRNWYVDEPS-CGSEVCVVMyhqpsapAGQGgpylfqWNDDNCNMKNNFICK 148

GumC

COG3206

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

107-260

1.09e-07

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.09e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 107 SKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELT 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395990 187 RLKAAVGELpEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELPdqsKQQQIYQELT-DLKTA 260
Cdd:COG3206 295 ALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELP---ELEAELRRLErEVEVA 363

DR0291

COG1579

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

108-271

1.88e-07

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: 51.46 E-value: 1.88e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 108 KLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSK---------- 177
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPA--ELAELEDELAALEARLEAA--KTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 178 ----LQEIYQELTRLKAAVGELpEKsKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVgelpdQSKQQQIYQE 253
Cdd:COG1579  87 nnkeYEALQKEIESLKRRISDL-ED-EILELMERIEELEEELAEL--EAELAELEAELEEKKAEL-----DEELAELEAE 157

                       170
                ....*....|....*...
gi 46395990 254 LTDLKTAFERLCRHCPKD 271
Cdd:COG1579 158 LEELEAEREELAAKIPPE 175

COG1340

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

71-253

5.98e-07

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 5.98e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEksKLQEIYQELTQLKAAVGEL----PEKSKLQEIYQEL------- 139
Cdd:COG1340  51 QVKELREEAQELREKRDELNEKVKELKEERDELNE--KLNELREELDELRKELAELnkagGSIDKLRKEIERLewrqqte 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 140 ------------------TRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELpeKSKL 201
Cdd:COG1340 129 vlspeeekelvekikeleKELEKAKKALEKNEKLKELRAELKELRKEAEEI--HKKIKELAEEAQELHEEMIEL--YKEA 204

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 46395990 202 QEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELPDQSKQQQIYQE 253
Cdd:COG1340 205 DELRKEADELHKEIVEA--QEKADELHEEIIELQKELRELRKELKKLRKKQR 254

PRK03918

DNA double-strand break repair ATPase Rad50;

71-264

1.03e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.03e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVgelp 150
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY---- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  151 eKSKLQEIYQELTRLKAAVGELPE--------KSKLQEIYQELTRLKAAVGELPEKSKLqeiYQELTELKAAVGELPEKS 222
Cdd:PRK03918 306 -LDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRL 381

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 46395990  223 K---LQEIYQELTQLKAAVGELPDQ-----SKQQQIYQELTDLKTAFERL 264
Cdd:PRK03918 382 TgltPEKLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431

COG1340

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

77-241

1.36e-06

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.36e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  77 SSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLK-------AAVGELPE-----KSKLQEIYQELTRLKA 144
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEEL--KEKRDELNEELKELAekrdelnAQVKELREeaqelREKRDELNEKVKELKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 145 AVGELpeKSKLQEIYQELTRLKAAVGEL----PEKSKLQEIYQEL-------------------------TRLKAAVGEL 195
Cdd:COG1340  79 ERDEL--NEKLNELREELDELRKELAELnkagGSIDKLRKEIERLewrqqtevlspeeekelvekikeleKELEKAKKAL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46395990 196 PEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGEL 241
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEI--HKKIKELAEEAQELHEEMIEL 200

PRK03918

DNA double-strand break repair ATPase Rad50;

71-261

1.44e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.44e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpEKSKLQEIYQELTRLKAAVGELp 150
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKL- 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  151 eKSKLQEIYQELTRLKAAVGELPE-KSKLQEIYQELTRLKAAVGELPEKS---------KLQEIYQELTELKAAVGELPE 220
Cdd:PRK03918 538 -KGEIKSLKKELEKLEELKKKLAElEKKLDELEEELAELLKELEELGFESveeleerlkELEPFYNEYLELKDAEKELER 616

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 46395990  221 KSKLQEIYQEltQLKAAVGELPDQSKQ-QQIYQELTDLKTAF 261
Cdd:PRK03918 617 EEKELKKLEE--ELDKAFEELAETEKRlEELRKELEELEKKY 656

PHA03097

C-type lectin-like protein; Provisional

268-389

3.85e-06

C-type lectin-like protein; Provisional

Pssm-ID: 222982 [Multi-domain] Cd Length: 157 Bit Score: 46.40 E-value: 3.85e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNF----LQLQTsrsnrfSWMGLSDLNQEGTWQWVD 343
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFvsryKGGQD------LWIGIEKKKGDDDDREVL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46395990  344 GSPLSPsfqrywnsgepnnSGNEDCAEFSGSGWNDNRCDVDNYWIC 389
Cdd:PHA03097 120 DKVVKP-------------PKSGKCAYLKDKTIISSNCNATKGWIC 152

PRK03918

DNA double-strand break repair ATPase Rad50;

77-258

2.56e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.56e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   77 SSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLK-AAVGELPEKSK-LQEIYQELTRLKAAVGELP---- 150
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEE--LAELLKELEELGfESVEELEERLKeLEPFYNEYLELKDAEKELEreek 619

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  151 ----EKSKLQEIYQELTRLKAAVGELPEK-SKLQEIY----------------QELTRLKAAVGELpeKSKLQEIYQELT 209
Cdd:PRK03918 620 elkkLEEELDKAFEELAETEKRLEELRKElEELEKKYseeeyeelreeylelsRELAGLRAELEEL--EKRREEIKKTLE 697

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46395990  210 ELKAAVGELPEK-----------SKLQEIYQELTQLKAAVGELPDQSKQQ---QIYQELTDLK 258
Cdd:PRK03918 698 KLKEELEEREKAkkeleklekalERVEELREKVKKYKALLKERALSKVGEiasEIFEELTEGK 760

CLECT_attractin_like

cd03597

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...

268-364

2.61e-05

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

Pssm-ID: 153067 Cd Length: 129 Bit Score: 43.34 E-value: 2.61e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL--QLQTSRSNRFS---WMGLSDLNQEgTWQWV 342
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVlkELQKHQMTKQKltpWVGLRKINVS-YWCWE 79

                        90       100
                ....*....|....*....|..
gi 46395990 343 DGSPLSPSFQRyWNSGEPNNSG 364
Cdd:cd03597  80 DMSPFTNTTLQ-WLPGEPSDAG 100

EnvC

COG4942

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

55-263

2.89e-05

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: 45.91 E-value: 2.89e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  55 LLSFMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELpeKSKLQE 134
Cdd:COG4942   5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRAL--EQELAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 135 IYQELTRLKAAVGEL-PEKSKLQEIYQELTRLKAAVGELPEKSKL------QEIYQELTRLKAAVGELpeKSKLQEIYQE 207
Cdd:COG4942  81 LEAELAELEKEIAELrAELEAQKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPAR--REQAEELRAD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46395990 208 LTELKAAVGELP-EKSKLQEIYQELTQLKAAVGELpdQSKQQQIYQELTDLKTAFER 263
Cdd:COG4942 159 LAELAALRAELEaERAELEALLAELEEERAALEAL--KAERQKLLARLEKELAELAA 213

PHA02867

C-type lectin protein; Provisional

261-315

8.87e-05

C-type lectin protein; Provisional

Pssm-ID: 165201 Cd Length: 167 Bit Score: 42.75 E-value: 8.87e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46395990  261 FERLCRHCPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL 315
Cdd:PHA02867  42 FPYFSKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

70-277

1.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.70e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  70 VQVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELPEKskLQEIYQELTRLKAAVGEL 149
Cdd:COG4372  24 ILIAALSEQLRKALFELDKLQEELEQLREELEQA--REELEQLEEELEQARSELEQLEEE--LEELNEQLQAAQAELAQA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 150 peKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEiyQELTELKaavgelpekSKLQEIYQ 229
Cdd:COG4372 100 --QEELESLQEEAEELQEELEEL--QKERQDLEQQRKQLEAQIAELQSEIAERE--EELKELE---------EQLESLQE 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 46395990 230 ELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCRHCPKDWTFFQG 277
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212

GumC

COG3206

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

102-264

2.09e-04

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.09e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 102 ELSEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVG--ELPEKSK-----LQEIYQELTRLKAAVGELpe 174
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPEL--RKELEEAEAALEEFRQKNGlvDLSEEAKlllqqLSELESQLAEARAELAEA-- 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 175 KSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELpDQSKQQQIYQEL 254
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAAL-RAQLQQEAQRIL 315

                       170
                ....*....|
gi 46395990 255 TDLKTAFERL 264
Cdd:COG3206 316 ASLEAELEAL 325

PRK03918

DNA double-strand break repair ATPase Rad50;

108-235

3.29e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  108 KLQEIYQELTQLKAAVGELPEKS-----KLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPE-KSKLQEI 181
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTenieeLIKEKEKELEEVLREINEI--SSELPELREELEKLEKEVKELEElKEEIEEL 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 46395990  182 YQELTRLKAAVGELPEK-----SKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLK 235
Cdd:PRK03918 244 EKELESLEGSKRKLEEKireleERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY 302

COG4913

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

79-242

4.83e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.83e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   79 LSQEQSEQDAIYQNLTQLKAAVGELsEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGEL-----PEKS 153
Cdd:COG4913  304 LARLEAELERLEARLDALREELDEL-EAQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAALglplpASAE 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  154 KLQEIYQELTRLKAAVGELpekskLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEksKLQEIYQEL-T 232
Cdd:COG4913  381 EFAALRAEAAALLEALEEE-----LEALEEALAEAEAALRDL--RRELRELEAEIASLERRKSNIPA--RLLALRDALaE 451

                        170
                 ....*....|
gi 46395990  233 QLKAAVGELP 242
Cdd:COG4913  452 ALGLDEAELP 461

PHA02562

endonuclease subunit; Provisional

106-264

6.24e-04

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 6.24e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  106 KSKLQEIYQELTQLKAAVGELPEKSKLQEIYQE---------LTRLKAAVGELPEKSKlqEIYQELTRLKAAVGELPEK- 175
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEeqrkkngenIARKQNKYDELVEEAK--TIKAEIEELTDELLNLVMDi 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  176 ----SKLQEIYQELTRLKAAVGELpekSKLQEIY----------QELTELKAAVGELpeKSKLQEIYQELTQLKAAVGEL 241
Cdd:PHA02562 251 edpsAALNKLNTAAAKIKSKIEQF---QKVIKMYekggvcptctQQISEGPDRITKI--KDKLKELQHSLEKLDTAIDEL 325

                        170       180
                 ....*....|....*....|...
gi 46395990  242 pdqskqQQIYQELTDLKTAFERL 264
Cdd:PHA02562 326 ------EEIMDEFNEQSKKLLEL 342

PRK11281

mechanosensitive channel MscK;

50-260

7.55e-04

mechanosensitive channel MscK;

Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 7.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    50 ALVLQLLSFMLLAGVLVAILVQVSKVPSSL------SQEQSEQDAIYQNLTQlkaavgELSEKSKLQEIYQELTQLKAAV 123
Cdd:PRK11281   16 LFLLLCLSSAFARAASNGDLPTEADVQAQLdalnkqKLLEAEDKLVQQDLEQ------TLALLDKIDRQKEETEQLKQQL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   124 GELPEksKLQEIYQELTRLKAAVGELPEK-----------SKLQEIYQELTRLKAAVGEL----------PEKS------ 176
Cdd:PRK11281   90 AQAPA--KLRQAQAELEALKDDNDEETREtlstlslrqleSRLAQTLDQLQNAQNDLAEYnsqlvslqtqPERAqaalya 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   177 ---KLQEIYQELTRLKAAVGEL-PEKSKLQEIYQELTELKAAVG--ELPEKSKLQEIYQELTQLKAAvgelpdqsKQQQI 250
Cdd:PRK11281  168 nsqRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQNDLQrkSLEGNTQLQDLLQKQRDYLTA--------RIQRL 239

                         250
                  ....*....|
gi 46395990   251 YQELTDLKTA 260
Cdd:PRK11281  240 EHQLQLLQEA 249

COG5022

Myosin heavy chain [General function prediction only];

81-258

8.65e-04

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 8.65e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   81 QEQSEQDAIYQNLTQLKAAVGELSE-KSKLQEIYQELTQLKAAVGELP-EKSKLQEiyQELTRLKaavgELPEKSKLQEI 158
Cdd:COG5022  872 QSAQRVELAERQLQELKIDVKSISSlKLVNLELESEIIELKKSLSSDLiENLEFKT--ELIARLK----KLLNNIDLEEG 945

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  159 YQ-ELTRLKAAVGELPEKSKLQEIYQELTRL----KAAVGEL-PEKSKLQEIYQELTELKAAVGELPEKSK-LQEIYQEL 231
Cdd:COG5022  946 PSiEYVKLPELNKLHEVESKLKETSEEYEDLlkksTILVREGnKANSELKNFKKELAELSKQYGALQESTKqLKELPVEV 1025

                        170       180
                 ....*....|....*....|....*..
gi 46395990  232 TQLKAAVGELPDQSKQQQIYQELTDLK 258
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLK 1052

COG4913

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

129-264

2.21e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.21e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  129 KSKLQEIYQELTRLKAAVGEL-PEKSKLQEIYQELTRLKAAVgelpekSKLQEIYQELTRLKAAVGELpeksklQEIYQE 207
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAeERLEALEAELDALQERREAL------QRLAEYSWDEIDVASAEREI------AELEAE 676

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 46395990  208 LTELKAAVGELpeksklQEIYQELTQLKAAVGELpdQSKQQQIYQELTDLKTAFERL 264
Cdd:COG4913  677 LERLDASSDDL------AALEEQLEELEAELEEL--EEELDELKGEIGRLEKELEQA 725

COG4192

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...

62-257

2.30e-03

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];

Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 40.05 E-value: 2.30e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990  62 AGVLVAILVQVSKVPSSLSQEQSEQdAIYQNLTQLKAAVGELSEKS----KLQEIYQELTQLKAAVGELPEKS-----KL 132
Cdd:COG4192  64 SNELVAALPEFAAATNTTERSQLRN-QLNTQLADIEELLAELEQLTqdagDLRAAVADLRNLLQQLDSLLTQRialrrRL 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990 133 QEIYQELTRLKAAVGELPEkSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTElk 212
Cdd:COG4192 143 QELLEQINWLHQDFNSELT-PLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIENQI--VSLLREVAAARDQ-- 217

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 46395990 213 AAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDL 257
Cdd:COG4192 218 ADVDNLFDR--LQYLKDELDRNLQALKNYPSTITLRQLIDELLAI 260

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

152-268

3.32e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 3.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990    152 KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEK--SKLQEIYQELTELKAAVgeLPEKSKLQEIYQ 229
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKL--RDRKDALEEELRQLKQLEDELEDCdpTELDRAKEKLKKLLQEI--MIKVKKLEELEE 232

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 46395990    230 ELTQLKAAVGELpdQSKQQQIYQELTDLKTAFERlCRHC 268
Cdd:smart00787 233 ELQELESKIEDL--TNKKSELNTEIAEAEKKLEQ-CRGF 268

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

97-240

9.24e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.27 E-value: 9.24e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395990   97 KAAVGElsEKSKLQEIYQELTQLKAavgELPEKSK-LQEIYQELTRLKAAVGElpEKSKLQEIYQEL-TRLKAAVGELPE 174
Cdd:PRK00409 508 KKLIGE--DKEKLNELIASLEELER---ELEQKAEeAEALLKEAEKLKEELEE--KKEKLQEEEDKLlEEAEKEAQQAIK 580

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395990  175 KSKlQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELPEksKLQEIYQELTQLKaaVGE 240
Cdd:PRK00409 581 EAK-KEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK--KKKKQKEKQEELK--VGD 641

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