NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46395879|sp|Q8HY10|]
View 

RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 4.86e-59

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: 187.90  E-value: 4.86e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395879 348 SSSfQRYWNSGEPNN--SGDEDCAEFSGS--GWNDNRCNVDNYWICKK 391
Cdd:cd03590  80 NSS-KTFWHPGEPNNwgGGGEDCAELVYDsgGWNDVPCNLEYRWICEK 126
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-260 6.11e-09

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


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.72  E-value: 6.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 107 SKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELPENSRLQEIYQELTQLKAAVGELpeKSKQQEIYQELT 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395879 187 RLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPdqsKQQQIYQELT-DLKTA 260
Cdd:COG3206 295 ALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELP---ELEAELRRLErEVEVA 363
 
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 4.86e-59

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: 187.90  E-value: 4.86e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395879 348 SSSfQRYWNSGEPNN--SGDEDCAEFSGS--GWNDNRCNVDNYWICKK 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 9.54e-41

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: 140.43  E-value: 9.54e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFTWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395879    346 PLSSSFqrYWNSGEPNNSGdEDCAEFSGSG--WNDNRCNVDNYWICK 390
Cdd:smart00034  81 GPVSYS--NWAPGEPNNSS-GDCVVLSTSGgkWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 286-391 1.27e-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: 115.65  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   286 QRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSSFqryWNSGEPNNSGD 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395879   366 EDCAEFSGS--GWNDNRCNVDNYWICKK 391
Cdd:pfam00059  78 EDCVELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 268-391 9.17e-15

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 72.84  E-value: 9.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 46395879  348 SSSFQRywnsgepnnSGDEDCAEFSGSGWNDNRCNVDNYWICKK 391
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSK 200
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 268-390 2.05e-12

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: 69.34  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    268 CPKDWTFFQGN--CYFISNSQRNWHDSVTACQE-VGAQLVVIKSAEEQNFLQLQSSRS-NRFTWMGLSDLN--QEGTWQW 341
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAHQ 397

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 46395879    342 VDGSPLSSSfqRYWNSGEPNNSGDEDCAEFSGSGW-NDNRCNVDNYWICK 390
Cdd:TIGR00864  398 GEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCE 445
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-260 6.11e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.72  E-value: 6.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 107 SKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELPENSRLQEIYQELTQLKAAVGELpeKSKQQEIYQELT 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395879 187 RLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPdqsKQQQIYQELT-DLKTA 260
Cdd:COG3206 295 ALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELP---ELEAELRRLErEVEVA 363
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
79-264 9.99e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 9.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   79 LSQEQSEQDVIYQNLTQLKAAVGELSEKS-KLQEIYQELTQLKAAVGELPE-KSRLQEIYQELTRLKAAVGELPEN---- 152
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISsELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKirel 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  153 -SRLQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAA-VGELPEKSKQQEIY-QELTRLKAAVGELPEKSKQ-QEIY 228
Cdd:PRK03918 265 eERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELREIEKRLSRLeEEINGIEERIKELEEKEERlEELK 344

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46395879  229 QELTRLKAAVGELpdqSKQQQIYQELTDLKTAFERL 264
Cdd:PRK03918 345 KKLKELEKRLEEL---EERHELYEEAKAKKEELERL 377
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 83-222 1.31e-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: 40.39  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879     83 QSEQDVIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSRlqeiyQELTRLKAAVGEL-----PENSRLQE 157
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDR--KDALEEELRQLKQLEDELEDCDP-----TELDRAKEKLKKLlqeimIKVKKLEE 229

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395879    158 IYQELTQLKAAVGELpeKSKQQEIYQELTRLKAAVgelpEKSKQQEIYqELTRLKAAVGELPEKS 222
Cdd:smart00787 230 LEEELQELESKIEDL--TNKKSELNTEIAEAEKKL----EQCRGFTFK-EIEKLKEQLKLLQSLT 287
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 78-258 3.08e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.41  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    78 SLSQEQSEQDviyQNLTQLKAAVGELSekSKLQEIYQELTQLKAAVGELpEKSRLqeiyqELTR----LKAAVGELPENS 153
Cdd:pfam15905  84 ALVQERGEQD---KRLQALEEELEKVE--AKLNAAVREKTSLSASVASL-EKQLL-----ELTRvnelLKAKFSEDGTQK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   154 RLQEIYQELTQLKaavGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGE-LPEKSKQQEIYQELT 232
Cdd:pfam15905 153 KMSSLSMELMKLR---NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEkIEEKSETEKLLEYIT 229

                         170       180
                  ....*....|....*....|....*.
gi 46395879   233 RLKAAVGELPDQSKQQQIYQELTDLK 258
Cdd:pfam15905 230 ELSCVSEQVEKYKLDIAQLEELLKEK 255
 
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 4.86e-59

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: 187.90  E-value: 4.86e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQlQSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46395879 348 SSSfQRYWNSGEPNN--SGDEDCAEFSGS--GWNDNRCNVDNYWICKK 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 9.54e-41

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: 140.43  E-value: 9.54e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQ--LQSSRSNRFTWMGLSDLNQEGTWQWVDGS 345
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46395879    346 PLSSSFqrYWNSGEPNNSGdEDCAEFSGSG--WNDNRCNVDNYWICK 390
Cdd:smart00034  81 GPVSYS--NWAPGEPNNSS-GDCVVLSTSGgkWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 278-391 8.30e-38

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: 132.74  E-value: 8.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 278 NCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQ-LQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSSFqrYWN 356
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYT--NWA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 46395879 357 SGEPNNSGDEDCAEFSGS---GWNDNRCNVDNYWICKK 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 4.47e-35

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: 125.14  E-value: 4.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46395879 348 SSSFQRywnsgePNNSGDEDCAEFSGSGWNDNRCNVDNYWICKK 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 5.69e-32

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: 117.84  E-value: 5.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVG-----AQLVVIKSAEEQNFL--QLQSSRSNRFT---WMGLSDLNQEG 337
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVydLFESSRGPDTPyglWIGLHDRTSEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46395879 338 TWQWVDGSPLSSSfqrYWNSGEPNNS-GDEDCAEF-----SGSGWNDNRCNVDNYWICK 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 1.27e-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: 115.65  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   286 QRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSSFqryWNSGEPNNSGD 365
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTN---WAPEPNNNGEN 77

                          90       100
                  ....*....|....*....|....*...
gi 46395879   366 EDCAEFSGS--GWNDNRCNVDNYWICKK 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 1.23e-23

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 94.67  E-value: 1.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 280 YFISNSQR-NWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSSfqrYWNSG 358
Cdd:cd03591   3 IFVTNGEEkNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYT---NWKPG 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 46395879 359 EPNNSGD-EDCAE-FSGSGWNDNRCNVDNYWIC 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 1.64e-21

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: 89.35  E-value: 1.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEV--GAQLVVIKSAEEQNFLQ---LQSSRSNRFTWMGLSDLNQEGTWQWV 342
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLHDPQQSRGWEWS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46395879 343 DGSPLsssfqRY--WNSGEPNNSGdEDCAEFSGSG----WNDNRCNVDNYWICK 390
Cdd:cd03594  81 DGSKL-----DYrsWDRNPPYARG-GYCAELSRSTgflkWNDANCEERNPFICK 128
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 280-389 6.98e-20

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: 84.35  E-value: 6.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 280 YFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFL-QLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSsfqRYWNSG 358
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINNEGTWVDTDKKELEY---KNWAPG 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 46395879 359 EPNNSGDEDCAE--FSGSG-WNDNRCNVDNYWIC 389
Cdd:cd03592  80 EPNNGRNENCLEiyIKDNGkWNDEPCSKKKSAIC 113
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 268-391 5.54e-19

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: 82.24  E-value: 5.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLqlqSSRSNRFTWMGLSDLNQEGTWQWVDGSPL 347
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46395879 348 ssSFQRyWNSGEPNN--SGDEDCAEFSG---SGWNDNRCNVDNYWICKK 391
Cdd:cd03588  78 --QFEN-WRPNQPDNffATGEDCVVMIWheeGEWNDVPCNYHLPFTCKK 123
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 280-378 1.16e-17

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: 78.24  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 280 YFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNrFTWMGLSDLNQEGTWQWVDGSPLSSSFqryWNSGE 359
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTN---WGSGE 78

                        90       100
                ....*....|....*....|....*.
gi 46395879 360 P--NNSGDEDCA---EFSGS--GWND 378
Cdd:cd03603  79 PhnNGGGNEDYAainHFPGIsgKWND 104
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 268-391 9.17e-15

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 72.84  E-value: 9.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRftWMGLSDLNQEGTWQWVDGSPL 347
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH--WIGLNRESSNHPWKWADNSNY 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 46395879  348 SSSFQRywnsgepnnSGDEDCAEFSGSGWNDNRCNVDNYWICKK 391
Cdd:PHA02642 166 NASFVI---------TGTGECAYLNDIRISSSRVYANRKWICSK 200
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 279-389 2.78e-13

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 66.26  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 279 CYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQ---LQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLSSSFQRYW 355
Cdd:cd03596  11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWERE 90

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 46395879 356 NSGEPNNSGDEDCAEFSGSG---WNDNRCNVDNYWIC 389
Cdd:cd03596  91 ITAQPDGGKRENCVALSSSAqgkWFDEDCRREKPYVC 127
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 280-389 3.51e-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: 65.47  E-value: 3.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 280 YFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDlnQEGTWQWVDGSPLSssfQRYWNSGE 359
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYR--DVDSWRWSDGSESS---FRNWNTFQ 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 46395879 360 PnnSGDEDCAEFSGSG-WNDNRCNVDNYWIC 389
Cdd:cd03602  78 P--FGQGDCATMYSSGrWYAALCSALKPFIC 106
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 268-390 2.05e-12

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: 69.34  E-value: 2.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    268 CPKDWTFFQGN--CYFISNSQRNWHDSVTACQE-VGAQLVVIKSAEEQNFLQLQSSRS-NRFTWMGLSDLN--QEGTWQW 341
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNgaEKGPAHQ 397

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 46395879    342 VDGSPLSSSfqRYWNSGEPNNSGDEDCAEFSGSGW-NDNRCNVDNYWICK 390
Cdd:TIGR00864  398 GEAFEAEEC--EEGLAGEPHPARAEHCVRLDPRGQcNSDLCNAPHAYVCE 445
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 280-390 4.82e-09

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 54.90  E-value: 4.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 280 YFISNSQR-NWHDSVTACQEVGAQLVVIKSAEEQ----NFLQLQSSRSNRFtWMGL---SDLNQEGT-----WQWVDGSP 346
Cdd:cd03595  17 YFQDSRRRlNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDF-WIGLrrsSQYNVTSSacsslYYWLDGSI 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46395879 347 lsSSFqRYWNSGEPNnSGDEDCAEF-------SGSG------WNDNRCNVDNYWICK 390
Cdd:cd03595  96 --STF-RNWYVDEPS-CGSEVCVVMyhqpsapAGQGgpylfqWNDDNCNMKNNFICK 148
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-260 6.11e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.72  E-value: 6.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 107 SKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELPENSRLQEIYQELTQLKAAVGELpeKSKQQEIYQELT 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVI 294

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395879 187 RLKAAVGELpEKSKQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPdqsKQQQIYQELT-DLKTA 260
Cdd:COG3206 295 ALRAQIAAL-RAQLQQEAQRILASLEAELEAL--QAREASLQAQLAQLEARLAELP---ELEAELRRLErEVEVA 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-264 6.63e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   93 LTQLKAAVGELSEK-SKLQEIYQELTQLKAAVGELPEKS-----------RLQEIYQELTRLKAAvgelpeNSRLQEIYQ 160
Cdd:COG4913  619 LAELEEELAEAEERlEALEAELDALQERREALQRLAEYSwdeidvasaerEIAELEAELERLDAS------SDDLAALEE 692

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  161 ELTQLKAAVgelpekskqQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGE 240
Cdd:COG4913  693 QLEELEAEL---------EELEEELDELKGEIGRL--EKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                        170       180
                 ....*....|....*....|....
gi 46395879  241 LPDQSKQQQIYQELTDLKTAFERL 264
Cdd:COG4913  762 AVERELRENLEERIDALRARLNRA 785
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
79-264 2.77e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  79 LSQEQSEQDVIYQNLTQLKAAVGELSEKSK-LQEIYQELTQLKAAVGELPEKSRLQEIYQELTRLKAAVGELPEnsRLQE 157
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEELEEeLEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEE 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 158 IYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPE--KSKQQEIYQELTRLK 235
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELE 230

                       170       180
                ....*....|....*....|....*....
gi 46395879 236 AAVGELPDQSKQQQIYQELTDLKTAFERL 264
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALL 259
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
59-261 9.90e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 9.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  59 TLLAgFLVAILVQVY-KGPSSLSQEQSEQDVIyqNLTQLKAAVGELSEKSKLQEIYQELTQ------------------L 119
Cdd:COG4717  38 TLLA-FIRAMLLERLeKEADELFKPQGRKPEL--NLKELKELEEELKEAEEKEEEYAELQEeleeleeeleeleaeleeL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 120 KAAVGELPEKSRLQEIYQELTRLKAAVGELPEnsRLQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKS 199
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46395879 200 KQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPDQSKQQQIYQELTDLKTAF 261
Cdd:COG4717 193 ELQDLAEELEELQQRLAEL--EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
58-264 1.03e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  58 FTLLAGFLVAILVQVYKGPSSLSQEQSE-------QDVIYQNLTQLKAAVG-----ELSEKSKLQEIYQELTQLKAAVGE 125
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEElqalpalEELEEEELEELLAALGlppdlSPEELLELLDRIEELQELLREAEE 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 126 LPEKSRLQEIYQELTRL--KAAVGELPENSRLQEIYQELTQLKAavgelpeksKQQEIYQELTRLKAAVGELPEKSKQQE 203
Cdd:COG4717 359 LEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEEYQELKE---------ELEELEEQLEELLGELEELLEALDEEE 429

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46395879 204 IYQELTRLKAAVGELPEKskQQEIYQELTRLKAAVGELPDQSKQQQIYQELTDLKTAFERL 264
Cdd:COG4717 430 LEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELAELLQELEELKAELREL 488
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 268-389 3.75e-07

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 49.48  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNF----LQLQSsrsnrfTWMGLSDLNQEGTWQWVD 343
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFvsryKGGQD------LWIGIEKKKGDDDDREVL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46395879  344 GSPLSSsfqrywnsgepnnSGDEDCAEFSGSGWNDNRCNVDNYWIC 389
Cdd:PHA03097 120 DKVVKP-------------PKSGKCAYLKDKTIISSNCNATKGWIC 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
79-264 9.99e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 9.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   79 LSQEQSEQDVIYQNLTQLKAAVGELSEKS-KLQEIYQELTQLKAAVGELPE-KSRLQEIYQELTRLKAAVGELPEN---- 152
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISsELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKirel 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  153 -SRLQEIYQELTQLKAAVGELPEKSKQQEIYQELTRLKAA-VGELPEKSKQQEIY-QELTRLKAAVGELPEKSKQ-QEIY 228
Cdd:PRK03918 265 eERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELREIEKRLSRLeEEINGIEERIKELEEKEERlEELK 344

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46395879  229 QELTRLKAAVGELpdqSKQQQIYQELTDLKTAFERL 264
Cdd:PRK03918 345 KKLKELEKRLEEL---EERHELYEEAKAKKEELERL 377
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-262 3.00e-06

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: 48.00  E-value: 3.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 108 KLQEIYQELTQLKAAVGELPEksRLQEIYQELTRLKAavgelpensRLQEIYQELTQLKAAVGELPEKSKQQEiyQELTR 187
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPA--ELAELEDELAALEA---------RLEAAKTELEDLEKEIKRLELEIEEVE--ARIKK 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395879 188 LKAAVGELpEKSKQQEIYQ-ELTRLKAAVGELpEKsKQQEIYQELTRLKAAVGELpdQSKQQQIYQELTDLKTAFE 262
Cdd:COG1579  78 YEEQLGNV-RNNKEYEALQkEIESLKRRISDL-ED-EILELMERIEELEEELAEL--EAELAELEAELEEKKAELD 148
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 268-391 6.40e-06

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: 45.27  E-value: 6.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFL--QLQSSRSNRFT---WMGLSDLNQEgTWQWV 342
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVlkELQKHQMTKQKltpWVGLRKINVS-YWCWE 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46395879 343 DGSPLS-SSFQryWNSGEPNNSGdeDCA---EFSGSGWNDNRC-NVDNYWICKK 391
Cdd:cd03597  80 DMSPFTnTTLQ--WLPGEPSDAG--FCGyleEPAVSGLKANPCtNPVNGSVCER 129
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
104-264 4.74e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 4.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 104 SEKSKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELpeNSRLQEIYQELTQLKAAVGELPEKSKQ----- 178
Cdd:COG1340   5 ELSSSLEELEEKIEELREEIEEL--KEKRDELNEELKELAEKRDEL--NAQVKELREEAQELREKRDELNEKVKElkeer 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 179 -------QEIYQELTRLKAAVGEL-----PEKSKQQEIYQELTRLKAAVgeLPeKSKQQEIYQELTRLKAAVGELPDQSK 246
Cdd:COG1340  81 delneklNELREELDELRKELAELnkaggSIDKLRKEIERLEWRQQTEV--LS-PEEEKELVEKIKELEKELEKAKKALE 157

                       170       180
                ....*....|....*....|..
gi 46395879 247 Q----QQIYQELTDLKTAFERL 264
Cdd:COG1340 158 KneklKELRAELKELRKEAEEI 179
PHA02867 PHA02867
C-type lectin protein; Provisional
 268-315 1.36e-04

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 42.36  E-value: 1.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 46395879  268 CPKDWTFFQGNCYFISNSQRNWHDSVTACQEVGAQLVVIKSAEEQNFL 315
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-258 1.52e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  104 SEKSKLQEIYQELTQLKAAVGELPEKsrLQEIYQELTRLK-AAVGELPEN-SRLQEIYQELTQLKAAVGELPEKSKQQEI 181
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEE--LAELLKELEELGfESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKK 623

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  182 YQEltRLKAAVGELPEKSKQ-QEIYQELTRLKAAVGELPEKSKQQ---EIYQELTRLKAAVGELpdQSKQQQIYQELTDL 257
Cdd:PRK03918 624 LEE--ELDKAFEELAETEKRlEELRKELEELEKKYSEEEYEELREeylELSRELAGLRAELEEL--EKRREEIKKTLEKL 699


                 .
gi 46395879  258 K 258
Cdd:PRK03918 700 K 700
PRK11281 PRK11281
mechanosensitive channel MscK;
80-263 1.84e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    80 SQEQSEQDVIYQNLTQlkaavgELSEKSKLQEIYQELTQLKAAVGELPEKsrLQEIYQELTRLKAavgelPENSRLQEIY 159
Cdd:PRK11281   52 KLLEAEDKLVQQDLEQ------TLALLDKIDRQKEETEQLKQQLAQAPAK--LRQAQAELEALKD-----DNDEETRETL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   160 --QELTQLkaavgelpeKSKQQEIYQELTRLKAAVGEL----------PEKSkQQEIYQELTRLkaavgelpekskqQEI 227
Cdd:PRK11281  119 stLSLRQL---------ESRLAQTLDQLQNAQNDLAEYnsqlvslqtqPERA-QAALYANSQRL-------------QQI 175

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 46395879   228 YQELTRLKAAVGEL-PDQSKQQQIYQELTDLKTAFER 263
Cdd:PRK11281  176 RNLLKGGKVGGKALrPSQRVLLQAEQALLNAQNDLQR 212
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
77-260 1.87e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  77 SSLSQEQSEQDVIYQNLTQLKAAVGELseKSKLQEIYQELTQLKAAVGELPEksRLQEIYQELTRLKAAVGELpeNSRLQ 156
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQA--REELEQLEEELEQARSELEQLEE--ELEELNEQLQAAQAELAQA--QEELE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 157 EIYQELTQLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEKSKQQEiyQELTRLkaavgelpeKSKQQEIYQELTRLKA 236
Cdd:COG4372 105 SLQEEAEELQEELEEL--QKERQDLEQQRKQLEAQIAELQSEIAERE--EELKEL---------EEQLESLQEELAALEQ 171

                       170       180
                ....*....|....*....|....
gi 46395879 237 AVGELPDQSKQQQIYQELTDLKTA 260
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRN 195
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
115-243 3.40e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 41.96  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 115 ELTQLKAAVGELPEksRLQEIYQELTRLKAAVGELPENSRLQEiyqELTQLKAAVGELPE---KSKQQEIYQELTRLKAA 191
Cdd:COG4223   1 EIAALEAAVAELPA--QLTALEQRLAALEAAPAAAAATAALEA---RLAALRAALAAAREavaAAAAAALEARLAALEAK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46395879 192 VGELPEKSKQQEIYQEL----TRLKAAVgelpekSKQQEIYQELTRLKAAVGELPD 243
Cdd:COG4223  76 AAAPEAEAAAAARAAALalaaAALRAAV------ERGQPFAAELAALEALAPDAPA 125
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
94-231 3.94e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 3.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  94 TQLKAAVGELSEKSKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELpeNSRLQEIYQELTQLKAAVGELP 173
Cdd:COG1340 147 KELEKAKKALEKNEKLKELRAELKELRKEAEEI--HKKIKELAEEAQELHEEMIEL--YKEADELRKEADELHKEIVEAQ 222

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46395879 174 EKSKqqEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKqqEIYQEL 231
Cdd:COG1340 223 EKAD--ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE--EIFEKL 276
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-236 5.50e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   93 LTQLKAAVGELseKSKLQEIYQELTQLKAAVGELpEKSRLQEIYQELTRLKAAVGELpeNSRLQEIYQELTQLKAAVG-- 170
Cdd:COG4913  297 LEELRAELARL--EAELERLEARLDALREELDEL-EAQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAal 371

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46395879  171 ELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEiyQELTRLKAAVGELpeKSKQQEIYQELTRLKA 236
Cdd:COG4913  372 GLPLPASAEEFAALRAEAAALLEALEEELEALE--EALAEAEAALRDL--RRELRELEAEIASLER 433
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 50-241 6.43e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    50 PLVLQLLSFTLLAGFLVAILVQVYKGPSSLSQEQSEQDVIYQNLTQ-LKAAVGELSEKSKLQEIYQELTQlkaAVGELPE 128
Cdd:PRK10929    3 LIITFLMAWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEaLQSALNWLEERKGSLERAKQYQQ---VIDNFPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   129 KSRlqEIYQELTRLKAAVGELPENSRLQEIYQELTQLKAavgELPEKSKQQEIYQELTR-LKAAVGELPEksKQQEIYQE 207
Cdd:PRK10929   80 LSA--ELRQQLNNERDEPRSVPPNMSTDALEQEILQVSS---QLLEKSRQAQQEQDRAReISDSLSQLPQ--QQTEARRQ 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 46395879   208 LT----RLKAA-VGELPEKSKQQEIYQ-ELTRLKAAVGEL 241
Cdd:PRK10929  153 LNeierRLQTLgTPNTPLAQAQLTALQaESAALKALVDEL 192
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-264 7.97e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 7.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   89 IYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSRLQEIYQELTRLKAAVGELpeNSRLQEIYQELTQLKAA 168
Cdd:COG4913  240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERLEAR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  169 VGELPEK------SKQQEIYQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVG--ELPEKSKQQEIYQELTRLKAAVGE 240
Cdd:COG4913  318 LDALREEldeleaQIRGNGGDRLEQLEREIERL--ERELEERERRRARLEALLAalGLPLPASAEEFAALRAEAAALLEA 395

                        170       180
                 ....*....|....*....|....
gi 46395879  241 LPDQSKQQQiyQELTDLKTAFERL 264
Cdd:COG4913  396 LEEELEALE--EALAEAEAALRDL 417
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 83-222 1.31e-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: 40.39  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879     83 QSEQDVIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELPEKSRlqeiyQELTRLKAAVGEL-----PENSRLQE 157
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDR--KDALEEELRQLKQLEDELEDCDP-----TELDRAKEKLKKLlqeimIKVKKLEE 229

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46395879    158 IYQELTQLKAAVGELpeKSKQQEIYQELTRLKAAVgelpEKSKQQEIYqELTRLKAAVGELPEKS 222
Cdd:smart00787 230 LEEELQELESKIEDL--TNKKSELNTEIAEAEKKL----EQCRGFTFK-EIEKLKEQLKLLQSLT 287
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-242 1.63e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   79 LSQEQSEQDVIYQNLTQLKAAVGELSEK-SKLQEIY-----QELTQLKAAVGELpeKSRLQEIYQELTRLKAAVG--ELP 150
Cdd:COG4913  297 LEELRAELARLEAELERLEARLDALREElDELEAQIrgnggDRLEQLEREIERL--ERELEERERRRARLEALLAalGLP 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  151 ENSRLQEIYQELTQLKAAVGELPEKSKQQEiyQELTRLKAAVGELpeKSKQQEIYQELTRLKAAVGELPEksKQQEIYQE 230
Cdd:COG4913  375 LPASAEEFAALRAEAAALLEALEEELEALE--EALAEAEAALRDL--RRELRELEAEIASLERRKSNIPA--RLLALRDA 448

                        170
                 ....*....|...
gi 46395879  231 L-TRLKAAVGELP 242
Cdd:COG4913  449 LaEALGLDEAELP 461
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
102-264 1.84e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 102 ELSEKSKLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVG--ELPEN-----SRLQEIYQELTQLKAAVGELpe 174
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPEL--RKELEEAEAALEEFRQKNGlvDLSEEaklllQQLSELESQLAEARAELAEA-- 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 175 KSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGEL--------P------------EKSKQQEIYQELTRL 234
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhPdvialraqiaalRAQLQQEAQRILASL 318

                       170       180       190
                ....*....|....*....|....*....|
gi 46395879 235 KAAVGELpdQSKQQQIYQELTDLKTAFERL 264
Cdd:COG3206 319 EAELEAL--QAREASLQAQLAQLEARLAEL 346
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 77-297 3.05e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.04  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    77 SSLSQEQSE----QDVIYQNLTQLKAAVGELSEkSKLQEIYQELTQLKAAVGELpEKSRLQEIY-QELTRLKAAVGElpe 151
Cdd:PRK10929  140 SQLPQQQTEarrqLNEIERRLQTLGTPNTPLAQ-AQLTALQAESAALKALVDEL-ELAQLSANNrQELARLRSELAK--- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   152 nSRLQEIYQELTQLKAAVGELpeksKQQEIYQELTR---LKAAVGELPEK-SKQQEIYQELTR-LKAAVGELPEKSKQQ- 225
Cdd:PRK10929  215 -KRSQQLDAYLQALRNQLNSQ----RQREAERALEStelLAEQSGDLPKSiVAQFKINRELSQaLNQQAQRMDLIASQQr 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   226 -------EIYQELTR-----------------LKAAVGELPDQSKQQQIYQELTDLKTA---FERLCCRCPKDWTFFQGN 278
Cdd:PRK10929  290 qaasqtlQVRQALNTlreqsqwlgvsnalgeaLRAQVARLPEMPKPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQAD 369

                         250
                  ....*....|....*....
gi 46395879   279 CYFISNSQRNWHDSVTACQ 297
Cdd:PRK10929  370 GQPLTAEQNRILDAQLRTQ 388
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 78-258 3.08e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.41  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879    78 SLSQEQSEQDviyQNLTQLKAAVGELSekSKLQEIYQELTQLKAAVGELpEKSRLqeiyqELTR----LKAAVGELPENS 153
Cdd:pfam15905  84 ALVQERGEQD---KRLQALEEELEKVE--AKLNAAVREKTSLSASVASL-EKQLL-----ELTRvnelLKAKFSEDGTQK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   154 RLQEIYQELTQLKaavGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGE-LPEKSKQQEIYQELT 232
Cdd:pfam15905 153 KMSSLSMELMKLR---NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEkIEEKSETEKLLEYIT 229

                         170       180
                  ....*....|....*....|....*.
gi 46395879   233 RLKAAVGELPDQSKQQQIYQELTDLK 258
Cdd:pfam15905 230 ELSCVSEQVEKYKLDIAQLEELLKEK 255
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-235 3.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879   78 SLSQEQSEQDVIYQNLTQLKAAVGELSEK-SKLQEIYQElTQLKAAVGELPEKSRlqeiyqELTRLKAAVGELpeNSRLQ 156
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSE-EEYEELREEYLELSR------ELAGLRAELEEL--EKRRE 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  157 EIYQELTQLKAAVGELPEKSKQQEiyqELTRLKAAVGELPEKSKQqeiYQELTRLKA--AVGELpekskQQEIYQELTRL 234
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELE---KLEKALERVEELREKVKK---YKALLKERAlsKVGEI-----ASEIFEELTEG 759


                 .
gi 46395879  235 K 235
Cdd:PRK03918 760 K 760
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-250 8.31e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879  79 LSQEQSEQDVIYQNLTQLKAAVGELSEKskLQEIYQELTQLKAAVGELpeKSRLQEIYQELTRLKAAVGELpeNSRLQEI 158
Cdd:COG4372  54 LEQAREELEQLEEELEQARSELEQLEEE--LEELNEQLQAAQAELAQA--QEELESLQEEAEELQEELEEL--QKERQDL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46395879 159 YQELTQLKAAVGELPEKSKQQEiyQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAV 238
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAERE--EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205

                       170
                ....*....|..
gi 46395879 239 GELPDQSKQQQI 250
Cdd:COG4372 206 EKLIESLPRELA 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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