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Conserved domains on  [gi|568973089|ref|XP_006532977|]
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macrophage galactose N-acetyl-galactosamine specific lectin 2 isoform X3 [Mus musculus]

Protein Classification

Lectin_N and CLECT_DC-SIGN_like domain-containing protein( domain architecture ID 10265841)

Lectin_N and CLECT_DC-SIGN_like domain-containing protein

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 ...
 160-333 6.23e-43

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: 145.14  E-value: 6.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 236
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 237 KGFKYvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqffifrnWRPLQPDNWHghmlGGGEDCAHFSYD- 315
Cdd:cd03590   81 SSKTF------------------------------------------------WHPGEPNNWG----GGGEDCAELVYDs 108

                        170
                 ....*....|....*...
gi 568973089 316 GRWNDDVCQRHYHWICET 333
Cdd:cd03590  109 GGWNDVPCNLEYRWICEK 126
Lectin_N super family cl04343
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 9-150 5.68e-30

Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits.


The actual alignment was detected with superfamily member pfam03954:

Pssm-ID: 461106  Cd Length: 140  Bit Score: 111.65  E-value: 5.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089    9 PSQSFLWRILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLGTLRAILDNTTSKIKAEFQSLDSRadnfekgisslk 88
Cdd:pfam03954  23 PPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTEAEVQALHSQ------------ 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973089   89 vdvedhrqelqaGRDLSQKVTSLESTLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANL 150
Cdd:pfam03954  91 ------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQMAFL 140
 
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 ...
 160-333 6.23e-43

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: 145.14  E-value: 6.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 236
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 237 KGFKYvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqffifrnWRPLQPDNWHghmlGGGEDCAHFSYD- 315
Cdd:cd03590   81 SSKTF------------------------------------------------WHPGEPNNWG----GGGEDCAELVYDs 108

                        170
                 ....*....|....*...
gi 568973089 316 GRWNDDVCQRHYHWICET 333
Cdd:cd03590  109 GGWNDVPCNLEYRWICEK 126
Lectin_N pfam03954
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 9-150 5.68e-30

Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits.


Pssm-ID: 461106  Cd Length: 140  Bit Score: 111.65  E-value: 5.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089    9 PSQSFLWRILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLGTLRAILDNTTSKIKAEFQSLDSRadnfekgisslk 88
Cdd:pfam03954  23 PPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTEAEVQALHSQ------------ 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973089   89 vdvedhrqelqaGRDLSQKVTSLESTLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANL 150
Cdd:pfam03954  91 ------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQMAFL 140
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 160-332 6.24e-25

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: 97.67  E-value: 6.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS----WMGLTD--QNGPWRWVDGT 233
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   234 DfdkgfkyvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqFFIFRNWRPLQPDNwhghmlgGGEDCAHFS 313
Cdd:smart00034  81 G-------------------------------------------------PVSYSNWAPGEPNN-------SSGDCVVLS 104

                          170       180
                   ....*....|....*....|
gi 568973089   314 YD-GRWNDDVCQRHYHWICE 332
Cdd:smart00034 105 TSgGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 179-333 5.25e-19

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 80.98  E-value: 5.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  179 KSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL--ANVLSWMGLTDQ--NGPWRWVDGTDFDkgfkyvcrlqlaplylgl 254
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRknEGTWKWVDGSPVN------------------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  255 sylfsifsdprdlggpsgnmadgqiwsaqffiFRNWRPLQPDNwhghmlGGGEDCAHFSY-DGRWNDDVCQRHYHWICET 333
Cdd:pfam00059  64 --------------------------------YTNWAPEPNNN------GENEDCVELSSsSGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 160-239 2.59e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 59.74  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLTDQ--NGPWRWVDGTDFDK 237
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREssNHPWKWADNSNYNA 167


                 ..
gi 568973089 238 GF 239
Cdd:PHA02642 168 SF 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
41-153 1.70e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  41 IGSQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQA----GRDLSQKVTSLES 113
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESlqeeAEELQEELEELQK 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568973089 114 ---TLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANLKNN 153
Cdd:COG4372  123 erqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 41-153 3.30e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   41 IGSQNSQLRRdlgtlraiLDNTTSKIKAEFQSLDSRADNFEKGISslkvdvedhrqelqagrDLSQKVTSLESTLEKREQ 120
Cdd:TIGR04523 435 IIKNNSEIKD--------LTNQDSVKELIIKNLDNTRESLETQLK-----------------VLSRSINKIKQNLEQKQK 489

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568973089  121 ALKT---DLSDLTDHVQQLETDLKALTCQLANLKNN 153
Cdd:TIGR04523 490 ELKSkekELKKLNEEKKELEEKVKDLTKKISSLKEK 525
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 160-238 4.40e-04

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: 42.38  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   160 CPLHWTEHEGS--CYWFSESEKSWPEADKYCR-LENSHLVVVNSLEEQNFLQNRLANVLS---WMGLTDQN----GPWRW 229
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLARKVTHSLDrgvWIGFSDVNgaekGPAHQ 397


                   ....*....
gi 568973089   230 VDGTDFDKG 238
Cdd:TIGR00864  398 GEAFEAEEC 406
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
43-122 2.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  43 SQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVD---VEDHRQELQAGRD-LSQKVTSLESTL 115
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDlgnAEDFLEELREERDeLREREAELEATL 435


                 ....*..
gi 568973089 116 EKREQAL 122
Cdd:PRK02224 436 RTARERV 442
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 47-143 8.51e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 37.39  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  47 QLRRDLGTLRAILDNTTSKIKAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRDLSQKVTSLESTLEKREQALKTdl 126
Cdd:cd21116   95 QLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEK-- 172

                         90
                 ....*....|....*..
gi 568973089 127 sdLTDHVQQLETDLKAL 143
Cdd:cd21116  173 --LSNDWQTLDSDIKEL 187
 
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 ...
 160-333 6.23e-43

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: 145.14  E-value: 6.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL-ANVLSWMGLTDQN--GPWRWVDGTDFD 236
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 237 KGFKYvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqffifrnWRPLQPDNWHghmlGGGEDCAHFSYD- 315
Cdd:cd03590   81 SSKTF------------------------------------------------WHPGEPNNWG----GGGEDCAELVYDs 108

                        170
                 ....*....|....*...
gi 568973089 316 GRWNDDVCQRHYHWICET 333
Cdd:cd03590  109 GGWNDVPCNLEYRWICEK 126
Lectin_N pfam03954
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 9-150 5.68e-30

Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, also known as Asialoglycoprotein receptors (ASGRs). ASGRs function as scavengers to mediate the endocytosis of plasma glycoproteins with terminal galactose and N-acetylgalactosamine units. ASGR is composed of a major (ASGR1) and a minor (ASGR2) subunits, both of which are type II, single-pass transmembrane proteins. ASGR is highly expressed in liver but has been also identified in human peripheral blood monocytes, representing a mobile pool of the receptor reaching distant sites from the liver to play a scavenger function where there is an infection or a damaged tissue. This domain includes the short, single transmembrane domain and the stalk region which mediates the oligomerization between subunits.


Pssm-ID: 461106  Cd Length: 140  Bit Score: 111.65  E-value: 5.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089    9 PSQSFLWRILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLGTLRAILDNTTSKIKAEFQSLDSRadnfekgisslk 88
Cdd:pfam03954  23 PPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTEAEVQALHSQ------------ 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973089   89 vdvedhrqelqaGRDLSQKVTSLESTLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANL 150
Cdd:pfam03954  91 ------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQMAFL 140
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 160-332 6.24e-25

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: 97.67  E-value: 6.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS----WMGLTD--QNGPWRWVDGT 233
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   234 DfdkgfkyvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqFFIFRNWRPLQPDNwhghmlgGGEDCAHFS 313
Cdd:smart00034  81 G-------------------------------------------------PVSYSNWAPGEPNN-------SSGDCVVLS 104

                          170       180
                   ....*....|....*....|
gi 568973089   314 YD-GRWNDDVCQRHYHWICE 332
Cdd:smart00034 105 TSgGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 170-332 2.42e-23

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: 93.07  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 170 SCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS---WMGLTDQ--NGPWRWVDGTdfdkgfkyvcr 244
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvWIGLNDLssEGTWKWSDGS----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 245 lqlaplylglsylfsifsdprdlggpsgnmadgqiwsaQFFIFRNWRPLQPDNwhghmlGGGEDCAHFSY--DGRWNDDV 322
Cdd:cd00037   70 --------------------------------------PLVDYTNWAPGEPNP------GGSEDCVVLSSssDGKWNDVS 105

                        170
                 ....*....|
gi 568973089 323 CQRHYHWICE 332
Cdd:cd00037  106 CSSKLPFICE 115
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 160-331 1.70e-22

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: 91.65  E-value: 1.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRL-----ENSHLVVVNSLEEQNFLQNRLANVLS-------WMGLTD--QNG 225
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGpdtpyglWIGLHDrtSEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 226 PWRWVDGTDFDkgfkyvcrlqlaplylglsylfsifsdprdlggpsgnmadgqiwsaqffiFRNWRPLQPDNWhghmlGG 305
Cdd:cd03589   81 PFEWTDGSPVD--------------------------------------------------FTKWAGGQPDNY-----GG 105

                        170       180       190
                 ....*....|....*....|....*....|
gi 568973089 306 GEDCAHFSY----DGRWNDDVCQRHYHWIC 331
Cdd:cd03589  106 NEDCVQMWRrgdaGQSWNDMPCDAVFPYIC 135
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 160-239 4.08e-22

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: 89.70  E-value: 4.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLTDQ--NGPWRWVDGTDFDK 237
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREksEKPWKWIDGSPLNN 80


                 ..
gi 568973089 238 GF 239
Cdd:cd03593   81 LF 82
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 179-333 5.25e-19

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 80.98  E-value: 5.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  179 KSWPEADKYCRLENSHLVVVNSLEEQNFLQNRL--ANVLSWMGLTDQ--NGPWRWVDGTDFDkgfkyvcrlqlaplylgl 254
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRknEGTWKWVDGSPVN------------------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  255 sylfsifsdprdlggpsgnmadgqiwsaqffiFRNWRPLQPDNwhghmlGGGEDCAHFSY-DGRWNDDVCQRHYHWICET 333
Cdd:pfam00059  64 --------------------------------YTNWAPEPNNN------GENEDCVELSSsSGKWNDENCNSKNPFVCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 160-332 9.30e-14

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: 67.22  E-value: 9.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLqNRLANVLSWMGLTDQ--NGPWRWVDGTdfdk 237
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV-NNNAQDYQWIGLNDRtiEGDFRWSDGH---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 238 gfkyvcrlqlaPLylglsylfsifsdprdlggpsgnmadgqiwsaqffIFRNWRPLQPDNWhghmLGGGEDCAHFSY--D 315
Cdd:cd03588   76 -----------PL-----------------------------------QFENWRPNQPDNF----FATGEDCVVMIWheE 105

                        170
                 ....*....|....*..
gi 568973089 316 GRWNDDVCQRHYHWICE 332
Cdd:cd03588  106 GEWNDVPCNYHLPFTCK 122
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 172-333 3.40e-11

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: 59.70  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 172 YWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS---WMGLTDQNGPWRWVDgtdfdkgfkyvcrlqla 248
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVD----------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 249 plylglsylfsifsdprdlggpsgnmADGQIWSAQffifrNWRPLQPDNwhghmlGGGEDCAHFSY--DGRWNDDVCQRH 326
Cdd:cd03592   66 --------------------------TDKKELEYK-----NWAPGEPNN------GRNENCLEIYIkdNGKWNDEPCSKK 108


                 ....*..
gi 568973089 327 YHWICET 333
Cdd:cd03592  109 KSAICYT 115
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 160-239 2.59e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 59.74  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLTDQ--NGPWRWVDGTDFDK 237
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREssNHPWKWADNSNYNA 167


                 ..
gi 568973089 238 GF 239
Cdd:PHA02642 168 SF 169
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 172-331 6.06e-10

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: 55.84  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 172 YWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQN--RLANVLSWMGLTDQNGPWRWVDGTDFDkgfkyvcrlqlap 249
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNlsRVSNSAAWIGLYRDVDSWRWSDGSESS------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 250 lylglsylfsifsdprdlggpsgnmadgqiwsaqffiFRNWRPLQPDnwhghmlgGGEDCAHFSYDGRWNDDVCQRHYHW 329
Cdd:cd03602   70 -------------------------------------FRNWNTFQPF--------GQGDCATMYSSGRWYAALCSALKPF 104


                 ..
gi 568973089 330 IC 331
Cdd:cd03602  105 IC 106
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 160-236 1.55e-09

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: 55.46  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRL--ENSHLVVVNSLEEQNFL-------QNRLANVlsWMGLTD--QNGPWR 228
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIaslissyQKAYQPV--WIGLHDpqQSRGWE 78


                 ....*...
gi 568973089 229 WVDGTDFD 236
Cdd:cd03594   79 WSDGSKLD 86
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 172-233 8.44e-09

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: 52.81  E-value: 8.44e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973089 172 YWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLA-NVLSWMGLTDQN--GPWRWVDGT 233
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGgYGASWIGASDAAteGTWKWSDGE 67
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 287-332 2.15e-08

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: 51.53  E-value: 2.15e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568973089 287 FRNWRPLQPDNWhghmlGGGEDCAHFSYDGRWNDDVCQRHYHWICE 332
Cdd:cd03591   73 YTNWKPGEPNNA-----GGGEDCVEMYTSGKWNDVACNLTRLFVCE 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
41-153 1.70e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  41 IGSQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQA----GRDLSQKVTSLES 113
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESlqeeAEELQEELEELQK 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568973089 114 ---TLEKREQALKTDLSDLTDHVQQLETDLKALTCQLANLKNN 153
Cdd:COG4372  123 erqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 71-153 8.60e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  71 QSLDSRADNFEKGISSLKVDVEDHRQELQAgrdLSQKVTSLESTLEKreqaLKTDLSDLTDHVQQLETDLKALTCQLANL 150
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAA---LEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGNV 85


                 ...
gi 568973089 151 KNN 153
Cdd:COG1579   86 RNN 88
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 160-221 3.13e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 3.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLSWMGLT 221
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIE 107
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 41-153 3.30e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   41 IGSQNSQLRRdlgtlraiLDNTTSKIKAEFQSLDSRADNFEKGISslkvdvedhrqelqagrDLSQKVTSLESTLEKREQ 120
Cdd:TIGR04523 435 IIKNNSEIKD--------LTNQDSVKELIIKNLDNTRESLETQLK-----------------VLSRSINKIKQNLEQKQK 489

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568973089  121 ALKT---DLSDLTDHVQQLETDLKALTCQLANLKNN 153
Cdd:TIGR04523 490 ELKSkekELKKLNEEKKELEEKVKDLTKKISSLKEK 525
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
47-152 3.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  47 QLRRDLGTLRAILDNTTSKIKAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRdlsQKVTSLESTLEKREQALKTDL 126
Cdd:COG4372   17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQLQAAQ 93

                         90       100
                 ....*....|....*....|....*....
gi 568973089 127 SDLTDHVQQLET---DLKALTCQLANLKN 152
Cdd:COG4372   94 AELAQAQEELESlqeEAEELQEELEELQK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-155 3.59e-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: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   42 GSQNSQLRRDLGTLRAILDNttskikaefqsLDSRADNFEKGISSLKVDVEDHRQELQAgrdLSQKVTSLESTLEKREQA 121
Cdd:COG4913   337 GDRLEQLEREIERLERELEE-----------RERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEA 402

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568973089  122 LKTDLSDLTDHVQQLETDLKALTCQLANLKNNGS 155
Cdd:COG4913   403 LEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 160-238 4.40e-04

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: 42.38  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   160 CPLHWTEHEGS--CYWFSESEKSWPEADKYCR-LENSHLVVVNSLEEQNFLQNRLANVLS---WMGLTDQN----GPWRW 229
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLARKVTHSLDrgvWIGFSDVNgaekGPAHQ 397


                   ....*....
gi 568973089   230 VDGTDFDKG 238
Cdd:TIGR00864  398 GEAFEAEEC 406
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 59-153 7.56e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   59 LDNTTSKIKAEFQSLDSRADNFEKGISSLKVDVEDHRQELQagrDLSQKVTSLEST---LEKREQALKTDLSDLTDHVQQ 135
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE---RLKETIIKNNSEikdLTNQDSVKELIIKNLDNTRES 465

                          90
                  ....*....|....*...
gi 568973089  136 LETDLKALTCQLANLKNN 153
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQN 483
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 43-152 7.62e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  43 SQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRDLSQKVTSLE--STLEK 117
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQK 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568973089 118 REQALKTDLSDLTDHVQQLETDLKALTCQLANLKN 152
Cdd:COG1579   97 EIESLKRRISDLEDEILELMERIEELEEELAELEA 131
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 167-277 9.04e-04

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 38.95  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089 167 HEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVLS---------WMGL-------TDQNGPWR-- 228
Cdd:cd03600    2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslrlWIGLqreprqcSDPSLPLRgf 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568973089 229 -WVDG---TDFDKGFKYVCRLQLAPLYLGLSYLFSIFSDPRDLGGPSGNMADG 277
Cdd:cd03600   82 sWVTGdqdTDFSNWLQEPAGTCTSPRCVALSAAGSTPDNLKWKDGPCSARADG 134
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
41-151 9.13e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 9.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  41 IGSQNSQLRRDLGTLRAILDNTTSKIKAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGR-DLSQ---KVTSLESTLE 116
Cdd:COG4372    4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEeELEQarsELEQLEEELE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568973089 117 KREQALKTDLSDLTDHVQQLET----------DLKALTCQLANLK 151
Cdd:COG4372   84 ELNEQLQAAQAELAQAQEELESlqeeaeelqeELEELQKERQDLE 128
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
43-149 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  43 SQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAgrdLSQKVTSLESTLEKRE 119
Cdd:COG4372   73 SELEQLEEELEELNEQLQAAQAELaqaQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---LEAQIAELQSEIAERE 149

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568973089 120 ---QALKTDLSDLTDHVQQLETDLKALTCQLAN 149
Cdd:COG4372  150 eelKELEEQLESLQEELAALEQELQALSEAEAE 182
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
43-122 2.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  43 SQNSQLRRDLGTLRAILDNTTSKI---KAEFQSLDSRADNFEKGISSLKVD---VEDHRQELQAGRD-LSQKVTSLESTL 115
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGDAPVDlgnAEDFLEELREERDeLREREAELEATL 435


                 ....*..
gi 568973089 116 EKREQAL 122
Cdd:PRK02224 436 RTARERV 442
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-150 5.17e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  67 KAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRDLSQKVTSLESTLEKREQALKTDLSDLTDHVQQLETDLKALTCQ 146
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105


                 ....
gi 568973089 147 LANL 150
Cdd:COG4942  106 LAEL 109
PHA02867 PHA02867
C-type lectin protein; Provisional
 160-207 5.43e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 37.35  E-value: 5.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568973089 160 CPLHWTEHEGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFL 207
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFV 96
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 285-332 6.88e-03

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: 36.21  E-value: 6.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568973089 285 FIFRNWRPLQPDNWHGHMLG---GG--EDCAHFS--YDGRWNDDVCQRHYHWICE 332
Cdd:cd03596   74 WVDVNGSPISYFNWEREITAqpdGGkrENCVALSssAQGKWFDEDCRREKPYVCE 128
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 47-143 8.51e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 37.39  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089  47 QLRRDLGTLRAILDNTTSKIKAEFQSLDSRADNFEKGISSLKVDVEDHRQELQAGRDLSQKVTSLESTLEKREQALKTdl 126
Cdd:cd21116   95 QLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEK-- 172

                         90
                 ....*....|....*..
gi 568973089 127 sdLTDHVQQLETDLKAL 143
Cdd:cd21116  173 --LSNDWQTLDSDIKEL 187
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 47-148 8.68e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 36.86  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973089   47 QLRRDLGTLRAILDNTTSKIKAEFQS-LDSRADNFEKGISSLKVDVEDHRQELQagRDLSQKVTSLESTLEKREQALKTD 125
Cdd:pfam01442  41 RLQKDLEEVRAKLEPYLEELQAKLGQnVEELRQRLEPYTEELRKRLNADAEELQ--EKLAPYGEELRERLEQNVDALRAR 118

                          90       100
                  ....*....|....*....|....
gi 568973089  126 LSDLTDHVQQ-LETDLKALTCQLA 148
Cdd:pfam01442 119 LAPYAEELRQkLAERLEELKESLA 142
 
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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