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Conserved domains on  [gi|42542390|ref|NP_055072|]
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C-type lectin domain family 4 member M isoform 1 [Homo sapiens]

Protein Classification

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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 42542390 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 42542390  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542390 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

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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 42542390 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 42542390    268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSRSNRFSWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 42542390    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 42542390   286 QRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqryWNSGEPNNSGN 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 42542390   366 EDCAEFSGS--GWNDNRCDVDNYWICKK 391
Cdd:pfam00059  78 EDCVELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 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 42542390  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRfsWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 42542390  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 42542390    267 HCPKDWTFFQGN--CYFMSNSQRNWHDSVTACQE-VRAQLVVIKTAEEQNFLQLQTSRS-NRFSWMGLSDLN--QEGTWQ 340
Cdd:TIGR00864  317 HCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42542390    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 42542390  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542390 201 LQEIYQELTELKAAVGELPEKskLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCR 266
Cdd:COG4717 427 EEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
PRK03918 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 42542390   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVgelp 150
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY---- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  151 eKSKLQEIYQELTRLKAAVGELPE--------KSKLQEIYQELTRLKAAVGELPEKSKLqeiYQELTELKAAVGELPEKS 222
Cdd:PRK03918 306 -LDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRL 381

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42542390  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 42542390    152 KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEK--SKLQEIYQELTELKAAVgeLPEKSKLQEIYQ 229
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKL--RDRKDALEEELRQLKQLEDELEDCdpTELDRAKEKLKKLLQEI--MIKVKKLEELEE 232

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 42542390    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

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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQlQTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 42542390 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 42542390    268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSRSNRFSWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 42542390    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 42542390 278 NCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSR-SNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqrYWN 356
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKsSSSDVWIGLNDLSSEGTWKWSDGSPLVDYT--NWA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42542390 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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSnrFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEKPWKWIDGSPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 42542390 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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQE-----VRAQLVVIKTAEEQNFL--QLQTSRSNRFS---WMGLSDLNQEG 337
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydLFESSRGPDTPyglWIGLHDRTSEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42542390 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 42542390   286 QRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFqryWNSGEPNNSGN 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 42542390   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 42542390 280 YFMSNSQR-NWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSfqrYWNSG 358
Cdd:cd03591   3 IFVTNGEEkNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYT---NWKPG 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 42542390 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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVR--AQLVVIKTAEEQNFL-----QLQTSRSNrfSWMGLSDLNQEGTWQ 340
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIaslisSYQKAYQP--VWIGLHDPQQSRGWE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42542390 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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLqlqTSRSNRFSWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 42542390 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 42542390 280 YFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL-QLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSpsfQRYWNSG 358
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINNEGTWVDTDKKELE---YKNWAPG 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 42542390 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 42542390 288 NWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNrFSWMGLSDLNQEGTWQWVDGsplSPSFQRYWNSGEP--NNSGN 365
Cdd:cd03603  11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDG---EESTYTNWGSGEPhnNGGGN 86

                        90
                ....*....|....*...
gi 42542390 366 EDCA---EFSGS--GWND 378
Cdd:cd03603  87 EDYAainHFPGIsgKWND 104
PHA02642 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 42542390  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRfsWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 42542390  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 42542390 280 YFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDlnQEGTWQWVDGSPLSPsfqRYWNSGE 359
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYR--DVDSWRWSDGSESSF---RNWNTFQ 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 42542390 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 42542390 279 CYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQ---LQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFQRYW 355
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWERE 90

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 42542390 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

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 42542390    267 HCPKDWTFFQGN--CYFMSNSQRNWHDSVTACQE-VRAQLVVIKTAEEQNFLQLQTSRS-NRFSWMGLSDLN--QEGTWQ 340
Cdd:TIGR00864  317 HCPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAH 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42542390    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 42542390  58 FMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIY-------QNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 126 LPEKSKLQEIYQELTRLKAAVG-----ELPEKSKLQEIYQELTRlkaavgelpeksKLQEIYQELTRLKAAVGELPEKSK 200
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQELKE------------ELEELEEQLEELLGELEELLEALD 426

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542390 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 42542390  92 NLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGElpeksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGE 171
Cdd:COG4717  69 NLKELKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 172 LPEksKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKAAVGELpdQSKQQQIY 251
Cdd:COG4717 144 LPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL--EEELEEAQ 219

                       170
                ....*....|...
gi 42542390 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 42542390  79 LSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELPE-KSKLQE 157
Cdd:COG4717  97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEElEAELAE 174

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42542390 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 42542390 280 YFMSNSQR-NWHDSVTACQEVRAQLVVIKTAEEQNFLQ--LQTSR-SNRFSWMGL---SDLNQEGT-----WQWVDGSPl 347
Cdd:cd03595  17 YFQDSRRRlNFEEARQACREDGGELLSIESENEQKLIErfIQTLRaSDGDFWIGLrrsSQYNVTSSacsslYYWLDGSI- 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42542390 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 42542390 107 SKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELT 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42542390 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 42542390 108 KLQEIYQELTQLKAAVGELPEksKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSK---------- 177
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPA--ELAELEDELAALEARLEAA--KTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 178 ----LQEIYQELTRLKAAVGELpEKsKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVgelpdQSKQQQIYQE 253
Cdd:COG1579  87 nnkeYEALQKEIESLKRRISDL-ED-EILELMERIEELEEELAEL--EAELAELEAELEEKKAEL-----DEELAELEAE 157

                       170
                ....*....|....*...
gi 42542390 254 LTDLKTAFERLCRHCPKD 271
Cdd:COG1579 158 LEELEAEREELAAKIPPE 175
COG1340 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 42542390  71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEksKLQEIYQELTQLKAAVGEL----PEKSKLQEIYQEL------- 139
Cdd:COG1340  51 QVKELREEAQELREKRDELNEKVKELKEERDELNE--KLNELREELDELRKELAELnkagGSIDKLRKEIERLewrqqte 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 140 ------------------TRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELpeKSKL 201
Cdd:COG1340 129 vlspeeekelvekikeleKELEKAKKALEKNEKLKELRAELKELRKEAEEI--HKKIKELAEEAQELHEEMIEL--YKEA 204

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42542390 202 QEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELPDQSKQQQIYQE 253
Cdd:COG1340 205 DELRKEADELHKEIVEA--QEKADELHEEIIELQKELRELRKELKKLRKKQR 254
PRK03918 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 42542390   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVgelp 150
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER--IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY---- 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  151 eKSKLQEIYQELTRLKAAVGELPE--------KSKLQEIYQELTRLKAAVGELPEKSKLqeiYQELTELKAAVGELPEKS 222
Cdd:PRK03918 306 -LDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRL 381

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42542390  223 K---LQEIYQELTQLKAAVGELPDQ-----SKQQQIYQELTDLKTAFERL 264
Cdd:PRK03918 382 TgltPEKLEKELEELEKAKEEIEEEiskitARIGELKKEIKELKKAIEEL 431
COG1340 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 42542390  77 SSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLK-------AAVGELPE-----KSKLQEIYQELTRLKA 144
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEEL--KEKRDELNEELKELAekrdelnAQVKELREeaqelREKRDELNEKVKELKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 145 AVGELpeKSKLQEIYQELTRLKAAVGEL----PEKSKLQEIYQEL-------------------------TRLKAAVGEL 195
Cdd:COG1340  79 ERDEL--NEKLNELREELDELRKELAELnkagGSIDKLRKEIERLewrqqtevlspeeekelvekikeleKELEKAKKAL 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42542390 196 PEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGEL 241
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEI--HKKIKELAEEAQELHEEMIEL 200
PRK03918 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 42542390   71 QVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpEKSKLQEIYQELTRLKAAVGELp 150
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKL- 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  151 eKSKLQEIYQELTRLKAAVGELPE-KSKLQEIYQELTRLKAAVGELPEKS---------KLQEIYQELTELKAAVGELPE 220
Cdd:PRK03918 538 -KGEIKSLKKELEKLEELKKKLAElEKKLDELEEELAELLKELEELGFESveeleerlkELEPFYNEYLELKDAEKELER 616

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42542390  221 KSKLQEIYQEltQLKAAVGELPDQSKQ-QQIYQELTDLKTAF 261
Cdd:PRK03918 617 EEKELKKLEE--ELDKAFEELAETEKRlEELRKELEELEKKY 656
PHA03097 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 42542390  268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNF----LQLQTsrsnrfSWMGLSDLNQEGTWQWVD 343
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFvsryKGGQD------LWIGIEKKKGDDDDREVL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 42542390  344 GSPLSPsfqrywnsgepnnSGNEDCAEFSGSGWNDNRCDVDNYWIC 389
Cdd:PHA03097 120 DKVVKP-------------PKSGKCAYLKDKTIISSNCNATKGWIC 152
PRK03918 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 42542390   77 SSLSQEQSEQDAIYQNLTQLKAAVGELSEKskLQEIYQELTQLK-AAVGELPEKSK-LQEIYQELTRLKAAVGELP---- 150
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEE--LAELLKELEELGfESVEELEERLKeLEPFYNEYLELKDAEKELEreek 619

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  151 ----EKSKLQEIYQELTRLKAAVGELPEK-SKLQEIY----------------QELTRLKAAVGELpeKSKLQEIYQELT 209
Cdd:PRK03918 620 elkkLEEELDKAFEELAETEKRLEELRKElEELEKKYseeeyeelreeylelsRELAGLRAELEEL--EKRREEIKKTLE 697

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42542390  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 42542390 268 CPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL--QLQTSRSNRFS---WMGLSDLNQEgTWQWV 342
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVlkELQKHQMTKQKltpWVGLRKINVS-YWCWE 79

                        90       100
                ....*....|....*....|..
gi 42542390 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 42542390  55 LLSFMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELpeKSKLQE 134
Cdd:COG4942   5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRAL--EQELAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 135 IYQELTRLKAAVGEL-PEKSKLQEIYQELTRLKAAVGELPEKSKL------QEIYQELTRLKAAVGELpeKSKLQEIYQE 207
Cdd:COG4942  81 LEAELAELEKEIAELrAELEAQKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPAR--REQAEELRAD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42542390 208 LTELKAAVGELP-EKSKLQEIYQELTQLKAAVGELpdQSKQQQIYQELTDLKTAFER 263
Cdd:COG4942 159 LAELAALRAELEaERAELEALLAELEEERAALEAL--KAERQKLLARLEKELAELAA 213
PHA02867 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 42542390  261 FERLCRHCPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFL 315
Cdd:PHA02867  42 FPYFSKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96
COG4372 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 42542390  70 VQVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELPEKskLQEIYQELTRLKAAVGEL 149
Cdd:COG4372  24 ILIAALSEQLRKALFELDKLQEELEQLREELEQA--REELEQLEEELEQARSELEQLEEE--LEELNEQLQAAQAELAQA 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 150 peKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEKSKLQEiyQELTELKaavgelpekSKLQEIYQ 229
Cdd:COG4372 100 --QEELESLQEEAEELQEELEEL--QKERQDLEQQRKQLEAQIAELQSEIAERE--EELKELE---------EQLESLQE 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42542390 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 42542390 102 ELSEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVG--ELPEKSK-----LQEIYQELTRLKAAVGELpe 174
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPEL--RKELEEAEAALEEFRQKNGlvDLSEEAKlllqqLSELESQLAEARAELAEA-- 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 175 KSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELpeKSKLQEIYQELTQLKAAVGELpDQSKQQQIYQEL 254
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAAL-RAQLQQEAQRIL 315

                       170
                ....*....|
gi 42542390 255 TDLKTAFERL 264
Cdd:COG3206 316 ASLEAELEAL 325
PRK03918 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 42542390  108 KLQEIYQELTQLKAAVGELPEKS-----KLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPE-KSKLQEI 181
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTenieeLIKEKEKELEEVLREINEI--SSELPELREELEKLEKEVKELEElKEEIEEL 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42542390  182 YQELTRLKAAVGELPEK-----SKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLK 235
Cdd:PRK03918 244 EKELESLEGSKRKLEEKireleERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY 302
COG4913 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 42542390   79 LSQEQSEQDAIYQNLTQLKAAVGELsEKSKLQEIYQELTQLKAAVGELpeKSKLQEIYQELTRLKAAVGEL-----PEKS 153
Cdd:COG4913  304 LARLEAELERLEARLDALREELDEL-EAQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAALglplpASAE 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  154 KLQEIYQELTRLKAAVGELpekskLQEIYQELTRLKAAVGELpeKSKLQEIYQELTELKAAVGELPEksKLQEIYQEL-T 232
Cdd:COG4913  381 EFAALRAEAAALLEALEEE-----LEALEEALAEAEAALRDL--RRELRELEAEIASLERRKSNIPA--RLLALRDALaE 451

                        170
                 ....*....|
gi 42542390  233 QLKAAVGELP 242
Cdd:COG4913  452 ALGLDEAELP 461
46 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 42542390  106 KSKLQEIYQELTQLKAAVGELPEKSKLQEIYQE---------LTRLKAAVGELPEKSKlqEIYQELTRLKAAVGELPEK- 175
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEeqrkkngenIARKQNKYDELVEEAK--TIKAEIEELTDELLNLVMDi 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  176 ----SKLQEIYQELTRLKAAVGELpekSKLQEIY----------QELTELKAAVGELpeKSKLQEIYQELTQLKAAVGEL 241
Cdd:PHA02562 251 edpsAALNKLNTAAAKIKSKIEQF---QKVIKMYekggvcptctQQISEGPDRITKI--KDKLKELQHSLEKLDTAIDEL 325

                        170       180
                 ....*....|....*....|...
gi 42542390  242 pdqskqQQIYQELTDLKTAFERL 264
Cdd:PHA02562 326 ------EEIMDEFNEQSKKLLEL 342
PRK11281 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 42542390    50 ALVLQLLSFMLLAGVLVAILVQVSKVPSSL------SQEQSEQDAIYQNLTQlkaavgELSEKSKLQEIYQELTQLKAAV 123
Cdd:PRK11281   16 LFLLLCLSSAFARAASNGDLPTEADVQAQLdalnkqKLLEAEDKLVQQDLEQ------TLALLDKIDRQKEETEQLKQQL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390   124 GELPEksKLQEIYQELTRLKAAVGELPEK-----------SKLQEIYQELTRLKAAVGEL----------PEKS------ 176
Cdd:PRK11281   90 AQAPA--KLRQAQAELEALKDDNDEETREtlstlslrqleSRLAQTLDQLQNAQNDLAEYnsqlvslqtqPERAqaalya 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390   177 ---KLQEIYQELTRLKAAVGEL-PEKSKLQEIYQELTELKAAVG--ELPEKSKLQEIYQELTQLKAAvgelpdqsKQQQI 250
Cdd:PRK11281  168 nsqRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQNDLQrkSLEGNTQLQDLLQKQRDYLTA--------RIQRL 239

                         250
                  ....*....|
gi 42542390   251 YQELTDLKTA 260
Cdd:PRK11281  240 EHQLQLLQEA 249
COG5022 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 42542390   81 QEQSEQDAIYQNLTQLKAAVGELSE-KSKLQEIYQELTQLKAAVGELP-EKSKLQEiyQELTRLKaavgELPEKSKLQEI 158
Cdd:COG5022  872 QSAQRVELAERQLQELKIDVKSISSlKLVNLELESEIIELKKSLSSDLiENLEFKT--ELIARLK----KLLNNIDLEEG 945

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390  159 YQ-ELTRLKAAVGELPEKSKLQEIYQELTRL----KAAVGEL-PEKSKLQEIYQELTELKAAVGELPEKSK-LQEIYQEL 231
Cdd:COG5022  946 PSiEYVKLPELNKLHEVESKLKETSEEYEDLlkksTILVREGnKANSELKNFKKELAELSKQYGALQESTKqLKELPVEV 1025

                        170       180
                 ....*....|....*....|....*..
gi 42542390  232 TQLKAAVGELPDQSKQQQIYQELTDLK 258
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLK 1052
COG4913 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 42542390  129 KSKLQEIYQELTRLKAAVGEL-PEKSKLQEIYQELTRLKAAVgelpekSKLQEIYQELTRLKAAVGELpeksklQEIYQE 207
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAeERLEALEAELDALQERREAL------QRLAEYSWDEIDVASAEREI------AELEAE 676

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42542390  208 LTELKAAVGELpeksklQEIYQELTQLKAAVGELpdQSKQQQIYQELTDLKTAFERL 264
Cdd:COG4913  677 LERLDASSDDL------AALEEQLEELEAELEEL--EEELDELKGEIGRLEKELEQA 725
COG4192 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 42542390  62 AGVLVAILVQVSKVPSSLSQEQSEQdAIYQNLTQLKAAVGELSEKS----KLQEIYQELTQLKAAVGELPEKS-----KL 132
Cdd:COG4192  64 SNELVAALPEFAAATNTTERSQLRN-QLNTQLADIEELLAELEQLTqdagDLRAAVADLRNLLQQLDSLLTQRialrrRL 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542390 133 QEIYQELTRLKAAVGELPEkSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTElk 212
Cdd:COG4192 143 QELLEQINWLHQDFNSELT-PLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIENQI--VSLLREVAAARDQ-- 217

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42542390 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 42542390    152 KSKLQEIYQELTRLKAAVGELpeKSKLQEIYQELTRLKAAVGELPEK--SKLQEIYQELTELKAAVgeLPEKSKLQEIYQ 229
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKL--RDRKDALEEELRQLKQLEDELEDCdpTELDRAKEKLKKLLQEI--MIKVKKLEELEE 232

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 42542390    230 ELTQLKAAVGELpdQSKQQQIYQELTDLKTAFERlCRHC 268
Cdd:smart00787 233 ELQELESKIEDL--TNKKSELNTEIAEAEKKLEQ-CRGF 268
PRK00409 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 42542390   97 KAAVGElsEKSKLQEIYQELTQLKAavgELPEKSK-LQEIYQELTRLKAAVGElpEKSKLQEIYQEL-TRLKAAVGELPE 174
Cdd:PRK00409 508 KKLIGE--DKEKLNELIASLEELER---ELEQKAEeAEALLKEAEKLKEELEE--KKEKLQEEEDKLlEEAEKEAQQAIK 580

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542390  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

References:

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