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Conserved domains on  [gi|672068057|ref|XP_008766090|]
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C-type lectin domain family 10 member A isoform X1 [Rattus norvegicus]

Protein Classification

Lectin_N and CLECT_DC-SIGN_like domain-containing protein( domain architecture ID 10512307)

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 ...
 176-301 5.07e-49

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: 159.39  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM-GSVVTWIGLTDQN--GPWRWVDGTDYE 252
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 672068057 253 KGFTHWAPKQPDNWYghglGGGEDCAHFTSD-GRWNDDVCQRPYRWVCEM 301
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126
Lectin_N pfam03954
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 5-166 1.85e-41

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: 140.54  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057    5 YENFQNLGSEEKNQEAGK-AAPPQSFLCNILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLETLRTTLDNTTSNTK 83
Cdd:pfam03954   2 YQDLQQLDSEENDHQLGKgPPPPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   84 AELQALASRgdslqtginslkvevddhgqelqaGRGLSQKVASLESTVEKKEQTLRTDLSEITDRVQQLGKDLKTLTCQL 163
Cdd:pfam03954  82 AEVQALHSQ------------------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQM 137


                  ...
gi 672068057  164 ASL 166
Cdd:pfam03954 138 AFL 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 ...
 176-301 5.07e-49

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: 159.39  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM-GSVVTWIGLTDQN--GPWRWVDGTDYE 252
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 672068057 253 KGFTHWAPKQPDNWYghglGGGEDCAHFTSD-GRWNDDVCQRPYRWVCEM 301
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126
Lectin_N pfam03954
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 5-166 1.85e-41

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: 140.54  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057    5 YENFQNLGSEEKNQEAGK-AAPPQSFLCNILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLETLRTTLDNTTSNTK 83
Cdd:pfam03954   2 YQDLQQLDSEENDHQLGKgPPPPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   84 AELQALASRgdslqtginslkvevddhgqelqaGRGLSQKVASLESTVEKKEQTLRTDLSEITDRVQQLGKDLKTLTCQL 163
Cdd:pfam03954  82 AEVQALHSQ------------------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQM 137


                  ...
gi 672068057  164 ASL 166
Cdd:pfam03954 138 AFL 140
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 176-300 4.71e-32

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: 115.39  E-value: 4.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVT----WIGLTD--QNGPWRWVDGT 249
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 672068057   250 DYEKgFTHWAPKQPDNwyghglgGGEDCAHF-TSDGRWNDDVCQRPYRWVCE 300
Cdd:smart00034  81 GPVS-YSNWAPGEPNN-------SSGDCVVLsTSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 195-301 5.57e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 96.39  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  195 KPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMG--SVVTWIGLTDQ--NGPWRWVDGTDYEkgFTHWAPKQPDNwyghg 270
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKksNKYFWIGLTDRknEGTWKWVDGSPVN--YTNWAPEPNNN----- 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 672068057  271 lGGGEDCAHFT-SDGRWNDDVCQRPYRWVCEM 301
Cdd:pfam00059  75 -GENEDCVELSsSSGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 176-299 2.93e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 62.06  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVTWIGLTDQ--NGPWRWVDGTDYEK 253
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREssNHPWKWADNSNYNA 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672068057 254 GFThwapkqpdnwyghgLGGGEDCAHFtSDGRWNDDVCQRPYRWVC 299
Cdd:PHA02642 168 SFV--------------ITGTGECAYL-NDIRISSSRVYANRKWIC 198
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 176-302 3.26e-09

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: 58.17  E-value: 3.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   176 CPLHWMEHEGS--CYWFSQSGKPWPEADKYCQ-LENSNLVAVNSLAEQNFLQ---THMGSVVTWIGLTDQN----GPWRW 245
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLArkvTHSLDRGVWIGFSDVNgaekGPAHQ 397

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 672068057   246 VDGTDYEKGfTHWAPKQPDnwyghgLGGGEDCAHFTSDGRWNDDVCQRPYRWVCEMK 302
Cdd:TIGR00864  398 GEAFEAEEC-EEGLAGEPH------PARAEHCVRLDPRGQCNSDLCNAPHAYVCELN 447
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-171 7.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   58 GSQNSQLRRDLETLRttldnttsntkAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLESTVEKKEQT 137
Cdd:COG4913   337 GDRLEQLEREIERLE-----------RELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEA 402

                          90       100       110
                  ....*....|....*....|....*....|....
gi 672068057  138 LRTDLSEITDRVQQLGKDLKTLTCQLASLKNNGS 171
Cdd:COG4913   403 LEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
PRK01156 PRK01156
chromosome segregation protein; Provisional
 64-167 1.20e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  64 LRRDLETLRTTLDNttsntkaeLQALASRGDSLQTGINSLKVEVDDHGQELQAGRGLSQKVASLESTVEKKEQTLRTDLS 143
Cdd:PRK01156 641 NKILIEKLRGKIDN--------YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712

                         90       100
                 ....*....|....*....|....*..
gi 672068057 144 EITDRVQQLGKDL---KTLTCQLASLK 167
Cdd:PRK01156 713 ELSDRINDINETLesmKKIKKAIGDLK 739
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 59-169 2.60e-03

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: 39.23  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   59 SQNSQLRRDLETLRttldNTTSNTKAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLESTVEKKEQTL 138
Cdd:TIGR04523 419 QEKELLEKEIERLK----ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV---LSRSINKIKQNLEQKQKEL 491

                          90       100       110
                  ....*....|....*....|....*....|....
gi 672068057  139 RT---DLSEITDRVQQLGKDLKTLTCQLASLKNN 169
Cdd:TIGR04523 492 KSkekELKKLNEEKKELEEKVKDLTKKISSLKEK 525
 
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 ...
 176-301 5.07e-49

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: 159.39  E-value: 5.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM-GSVVTWIGLTDQN--GPWRWVDGTDYE 252
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILsGNRSYWIGLSDEEteGEWKWVDGTPLN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 672068057 253 KGFTHWAPKQPDNWYghglGGGEDCAHFTSD-GRWNDDVCQRPYRWVCEM 301
Cdd:cd03590   81 SSKTFWHPGEPNNWG----GGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126
Lectin_N pfam03954
Hepatic lectin, N-terminal domain; This is the N-terminal domain found in hepatic lectins, ...
 5-166 1.85e-41

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: 140.54  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057    5 YENFQNLGSEEKNQEAGK-AAPPQSFLCNILSWTHLLLFSLGLSLLLLVVISVIGSQNSQLRRDLETLRTTLDNTTSNTK 83
Cdd:pfam03954   2 YQDLQQLDSEENDHQLGKgPPPPQPFLQRLCSGLRLLLLSLGLSLLLLVVVCVIGSQNSQLQRELLTLKETFSNFSSSTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   84 AELQALASRgdslqtginslkvevddhgqelqaGRGLSQKVASLESTVEKKEQTLRTDLSEITDRVQQLGKDLKTLTCQL 163
Cdd:pfam03954  82 AEVQALHSQ------------------------GGSLGDKVTSLESKLEKKQQDLKADHSTLLLHVKQFPKDLRTLSCQM 137


                  ...
gi 672068057  164 ASL 166
Cdd:pfam03954 138 AFL 140
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 176-300 4.71e-32

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: 115.39  E-value: 4.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVT----WIGLTD--QNGPWRWVDGT 249
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDpdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 672068057   250 DYEKgFTHWAPKQPDNwyghglgGGEDCAHF-TSDGRWNDDVCQRPYRWVCE 300
Cdd:smart00034  81 GPVS-YSNWAPGEPNN-------SSGDCVVLsTSGGKWNDVSCTSKLPFVCE 124
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 176-301 2.18e-30

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: 111.68  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSN-----LVAVNSLAEQNFLQTHMGSVVT-------WIGLTD--QNG 241
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFESSRGpdtpyglWIGLHDrtSEG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672068057 242 PWRWVDGTDYEkgFTHWAPKQPDNWYghglgGGEDCAHF----TSDGRWNDDVCQRPYRWVCEM 301
Cdd:cd03589   81 PFEWTDGSPVD--FTKWAGGQPDNYG-----GNEDCVQMwrrgDAGQSWNDMPCDAVFPYICKM 137
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 186-301 1.03e-28

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: 106.55  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 186 SCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM---GSVVTWIGLTDQ--NGPWRWVDGTDYeKGFTHWAP 260
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLssEGTWKWSDGSPL-VDYTNWAP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 672068057 261 KQPDNwyghglGGGEDCAHF--TSDGRWNDDVCQRPYRWVCEM 301
Cdd:cd00037   80 GEPNP------GGSEDCVVLssSSDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 195-301 5.57e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 96.39  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  195 KPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMG--SVVTWIGLTDQ--NGPWRWVDGTDYEkgFTHWAPKQPDNwyghg 270
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKksNKYFWIGLTDRknEGTWKWVDGSPVN--YTNWAPEPNNN----- 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 672068057  271 lGGGEDCAHFT-SDGRWNDDVCQRPYRWVCEM 301
Cdd:pfam00059  75 -GENEDCVELSsSSGKWNDENCNSKNPFVCEK 105
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 176-300 8.66e-23

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: 90.85  E-value: 8.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVTWIGLTDQ--NGPWRWVDGTDYEK 253
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREksEKPWKWIDGSPLNN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 672068057 254 GFTHwapkqpdnwygHGLGGGEDCAhFTSDGRWNDDVCQRPYRWVCE 300
Cdd:cd03593   81 LFNI-----------RGSTKSGNCA-YLSSTGIYSEDCSTKKRWICE 115
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 188-300 2.89e-16

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: 73.18  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 188 YWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVT---WIGLTDQNGPWRWVDGTDYEKGFTHWAPKQPD 264
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 672068057 265 NwyghglGGGEDC--AHFTSDGRWNDDVCQRPYRWVCE 300
Cdd:cd03592   83 N------GRNENCleIYIKDNGKWNDEPCSKKKSAICY 114
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 176-301 2.07e-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: 68.76  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHmGSVVTWIGLTDQ--NGPWRWVDGTDYEk 253
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN-AQDYQWIGLNDRtiEGDFRWSDGHPLQ- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 672068057 254 gFTHWAPKQPDNWYghglGGGEDCAHFT--SDGRWNDDVCQRPYRWVCEM 301
Cdd:cd03588   79 -FENWRPNQPDNFF----ATGEDCVVMIwhEEGEWNDVPCNYHLPFTCKK 123
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 188-288 9.46e-14

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: 66.68  E-value: 9.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 188 YWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMG-SVVTWIGLTDQN--GPWRWVDGTdyEKGFTHWAPKQPD 264
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGgYGASWIGASDAAteGTWKWSDGE--ESTYTNWGSGEPH 80

                         90       100
                 ....*....|....*....|....*...
gi 672068057 265 NwyghGLGGGEDCAH----FTSDGRWND 288
Cdd:cd03603   81 N----NGGGNEDYAAinhfPGISGKWND 104
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 176-300 9.95e-13

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: 63.93  E-value: 9.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQL--ENSNLVAVNSLAEQNFLQTHMGSVVT-----WIGLTD--QNGPWRWV 246
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKayqpvWIGLHDpqQSRGWEWS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672068057 247 DGTDYEkgFTHWAPKQPdnwyghgLGGGEDCAHFTSDG---RWNDDVCQRPYRWVCE 300
Cdd:cd03594   81 DGSKLD--YRSWDRNPP-------YARGGYCAELSRSTgflKWNDANCEERNPFICK 128
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 188-299 1.13e-12

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: 63.16  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 188 YWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQ--THMGSVVTWIGLTDQNGPWRWVDGTDYEkgFTHWAPKQPDn 265
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSnlSRVSNSAAWIGLYRDVDSWRWSDGSESS--FRNWNTFQPF- 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 672068057 266 wyghglgGGEDCAHFTSDGRWNDDVCQRPYRWVC 299
Cdd:cd03602   80 -------GQGDCATMYSSGRWYAALCSALKPFIC 106
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 195-300 1.86e-12

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: 62.70  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 195 KPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM--GSVVTWIGLTDQNGPWRWVDGTDYEKGFTHWAPKQPDNWYGHglg 272
Cdd:cd03591   11 KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVkkGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAGGG--- 87

                         90       100
                 ....*....|....*....|....*...
gi 672068057 273 ggEDCAHFTSDGRWNDDVCQRPYRWVCE 300
Cdd:cd03591   88 --EDCVEMYTSGKWNDVACNLTRLFVCE 113
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 176-299 2.93e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 62.06  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVTWIGLTDQ--NGPWRWVDGTDYEK 253
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNREssNHPWKWADNSNYNA 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672068057 254 GFThwapkqpdnwyghgLGGGEDCAHFtSDGRWNDDVCQRPYRWVC 299
Cdd:PHA02642 168 SFV--------------ITGTGECAYL-NDIRISSSRVYANRKWIC 198
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 176-302 3.26e-09

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: 58.17  E-value: 3.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   176 CPLHWMEHEGS--CYWFSQSGKPWPEADKYCQ-LENSNLVAVNSLAEQNFLQ---THMGSVVTWIGLTDQN----GPWRW 245
Cdd:TIGR00864  318 CPKDGEIFEENghCFQIVPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLArkvTHSLDRGVWIGFSDVNgaekGPAHQ 397

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 672068057   246 VDGTDYEKGfTHWAPKQPDnwyghgLGGGEDCAHFTSDGRWNDDVCQRPYRWVCEMK 302
Cdd:TIGR00864  398 GEAFEAEEC-EEGLAGEPH------PARAEHCVRLDPRGQCNSDLCNAPHAYVCELN 447
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 187-300 1.29e-07

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: 49.69  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 187 CYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHM-----GSVVTWIGLTDQNGPWRWVDGTDYEKGFTHW--- 258
Cdd:cd03596   11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVkasvpGNWEVWLGINDMVAEGKWVDVNGSPISYFNWere 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 672068057 259 APKQPDNwyghglGGGEDCAHF--TSDGRWNDDVCQRPYRWVCE 300
Cdd:cd03596   91 ITAQPDG------GKRENCVALssSAQGKWFDEDCRREKPYVCE 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 185-299 6.95e-07

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 47.45  E-value: 6.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 185 GSCYWFSQSGKPWPEADKYCQ-LENSNLVAVNSLAEQNFLQTHMGS---VVTWIG--LTDQNGPWR--WVDGTDYEkgFT 256
Cdd:cd03598    1 GRCYRFVKSPRTFRDAQVICRrCYRGNLASIHSFAFNYRVQRLVSTlnqAQVWIGgiITGKGRCRRfsWVDGSVWN--YA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 672068057 257 HWAPKQPDNWYGHglgggedC-AHFTSDGRWNDDVCQRPYRWVC 299
Cdd:cd03598   79 YWAPGQPGNRRGH-------CvELCTRGGHWRRAHCKLRRPFIC 115
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 176-299 7.67e-07

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 47.94  E-value: 7.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHMGSVVTWIGLTDQNGpwrwvdgtDYEKGF 255
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKG--------DDDDRE 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 672068057 256 THWAPKQPDnwyghglgGGEDCAhFTSDGRWNDDVCQRPYRWVC 299
Cdd:PHA03097 118 VLDKVVKPP--------KSGKCA-YLKDKTIISSNCNATKGWIC 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-171 7.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   58 GSQNSQLRRDLETLRttldnttsntkAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLESTVEKKEQT 137
Cdd:COG4913   337 GDRLEQLEREIERLE-----------RELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEA 402

                          90       100       110
                  ....*....|....*....|....*....|....
gi 672068057  138 LRTDLSEITDRVQQLGKDLKTLTCQLASLKNNGS 171
Cdd:COG4913   403 LEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 233-300 3.62e-05

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


Pssm-ID: 153071  Cd Length: 119  Bit Score: 42.52  E-value: 3.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672068057 233 WIGLTD-QNGPWR--WVDGTDYEKGFTHWAPKQPDN---WyghglgggEDCAHFTSD-GRWNDDVCQRPYRWVCE 300
Cdd:cd03601   52 WVGADNlQDGEYDflWNDGVSLPTDSDLWAPNEPSNpqsR--------QLCVQLWSKyNLLDDEYCGRAKRVICE 118
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 63-164 2.98e-04

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: 40.71  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   63 QLRRDLETLRTTLDNTTSNTKAELQA----LASRgdsLQTGINSLKVEVDDHGQELQagRGLSQKVASLESTVEKKEQTL 138
Cdd:pfam01442  41 RLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQR---LEPYTEELRKRLNADAEELQ--EKLAPYGEELRERLEQNVDAL 115

                          90       100
                  ....*....|....*....|....*..
gi 672068057  139 RTDLSEITDRVQQ-LGKDLKTLTCQLA 164
Cdd:pfam01442 116 RARLAPYAEELRQkLAERLEELKESLA 142
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
57-168 5.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  57 IGSQNSQLRRDLETLRTTLDNTTSNTKAELQALASRGDSLQTGINSLKVEVDDHGQELQAGRG-LSQKVASLESTVEKKE 135
Cdd:COG4372    4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEeLEQARSELEQLEEELE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 672068057 136 QT---LRTDLSEITDRVQQLG---KDLKTLTCQLASLKN 168
Cdd:COG4372   84 ELneqLQAAQAELAQAQEELEslqEEAEELQEELEELQK 122
PRK01156 PRK01156
chromosome segregation protein; Provisional
 64-167 1.20e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  64 LRRDLETLRTTLDNttsntkaeLQALASRGDSLQTGINSLKVEVDDHGQELQAGRGLSQKVASLESTVEKKEQTLRTDLS 143
Cdd:PRK01156 641 NKILIEKLRGKIDN--------YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712

                         90       100
                 ....*....|....*....|....*..
gi 672068057 144 EITDRVQQLGKDL---KTLTCQLASLK 167
Cdd:PRK01156 713 ELSDRINDINETLesmKKIKKAIGDLK 739
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 77-168 1.23e-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: 40.13  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  77 NTTSNTKAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLestvEKKEQTLRTDLSEITDRVQQLGKDL 156
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAAL----ARRIRALEQELAALEAELAELEKEI 92

                         90
                 ....*....|..
gi 672068057 157 KTLTCQLASLKN 168
Cdd:COG4942   93 AELRAELEAQKE 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
57-169 1.56e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  57 IGSQNSQLRRDLETLRTTLDNTTSN---TKAELQALASRGDSLQTGINSLKVEVDDHGQELQAGRG----LSQKVASLES 129
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEEleqARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEeaeeLQEELEELQK 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 672068057 130 ---TVEKKEQTLRTDLSEITDRVQQLGKDLKTLTCQLASLKNN 169
Cdd:COG4372  123 erqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 76-173 2.43e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  76 DNTTSNTKAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLESTVEKKEQTLRTDLSEITDRVQQLGKd 155
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREELGE- 90

                         90
                 ....*....|....*...
gi 672068057 156 lktltcQLASLKNNGSAV 173
Cdd:COG3883   91 ------RARALYRSGGSV 102
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 59-169 2.60e-03

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: 39.23  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057   59 SQNSQLRRDLETLRttldNTTSNTKAELQALASRGDSLQTGINSLKVEVDDHGQELQAgrgLSQKVASLESTVEKKEQTL 138
Cdd:TIGR04523 419 QEKELLEKEIERLK----ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV---LSRSINKIKQNLEQKQKEL 491

                          90       100       110
                  ....*....|....*....|....*....|....
gi 672068057  139 RT---DLSEITDRVQQLGKDLKTLTCQLASLKNN 169
Cdd:TIGR04523 492 KSkekELKKLNEEKKELEEKVKDLTKKISSLKEK 525
PRK09039 PRK09039
peptidoglycan -binding protein;
59-158 2.66e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  59 SQNSQLRRDLETLRTTLDNTTSNtKAELQAL----ASRGDSLQTGINSLKVEVDDHGQELQAGRG----LSQKVASLEST 130
Cdd:PRK09039  74 QGNQDLQDSVANLRASLSAAEAE-RSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAqvelLNQQIAALRRQ 152

                         90       100       110
                 ....*....|....*....|....*....|...
gi 672068057 131 VEKKEQTLrtDLSEITDRVQQ-----LGKDLKT 158
Cdd:PRK09039 153 LAALEAAL--DASEKRDRESQakiadLGRRLNV 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 85-169 7.92e-03

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: 37.21  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068057  85 ELQALASRGDSLQTGINSLKVEVDDHGQELQagrGLSQKVASLESTVEKkeqtLRTDLSEITDRVQQLGKDLKTLTCQLA 164
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELA---ALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLG 83


                 ....*
gi 672068057 165 SLKNN 169
Cdd:COG1579   84 NVRNN 88
PHA02867 PHA02867
C-type lectin protein; Provisional
 176-234 8.65e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 36.58  E-value: 8.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672068057 176 CPLHWMEHEGSCYWFSQSGKPWPEADKYCQLENSNLVAVNSLAEQNFLQTHmGSVVTWI 234
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRY-GKGSYWI 106
 
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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