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Conserved domains on  [gi|359279914|ref|NP_001240672|]
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low affinity immunoglobulin epsilon Fc receptor isoform A [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132480)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 159-279 7.34e-42

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: 140.90  E-value: 7.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 237
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 359279914 238 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 279
Cdd:cd03590   81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 36-147 3.23e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    36 IQNVSHVTKDLQKF--QSNQLAQKSQ------VVQMSQNLQELQAEQKQMKAQDSRLSQNltglQEDLRNaQSQNSKLSQ 107
Cdd:pfam15921   80 LEEYSHQVKDLQRRlnESNELHEKQKfylrqsVIDLQTKLQEMQMERDAMADIRRRESQS----QEDLRN-QLQNTVHEL 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 359279914   108 NLNR-LQDDLVNIKSLGLNEKRTASDSLEKLQEEVAKLWIE 147
Cdd:pfam15921  155 EAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD 195
 
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 ...
 159-279 7.34e-42

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: 140.90  E-value: 7.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 237
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 359279914 238 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 279
Cdd:cd03590   81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 159-279 5.00e-39

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 133.49  E-value: 5.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS----WIGLQDLNMEGEFVWSDGS 234
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 359279914   235 P-VGYSNWNPGEPNNGgqGEDCV-MMRGSGQWNDAFCRSYLdAWVCE 279
Cdd:smart00034  81 GpVSYSNWAPGEPNNS--SGDCVvLSTSGGKWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 177-280 2.41e-30

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.26  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  177 SKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINK--KDSWIGLQDLNMEGEFVWSDGSPVGYSNWNPgEPNNGGQGED 254
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 359279914  255 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 280
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKN-PFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 159-234 8.74e-13

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 66.29  E-value: 8.74e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGS 234
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNS 163
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 112-279 2.46e-08

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: 55.47  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   112 LQDDLVNIKSLGLNekrtASDSLEKLQEEVAKlwieiliskgTACNICPKNWLHFQQ--KCYYFGKGSKQWIQARFACSD 189
Cdd:TIGR00864  285 LDLSIQNRGGSDLD----AAWKITAHGEEPAK----------ASHPHCPKDGEIFEEngHCFQIVPEEAAWLDAQEQCLA 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   190 L-QGRLVSIHSQKEQDFLMQHINK---KDSWIGLQDLNM--EGEFVWSDGSPV-GYSNWNPGEPNNgGQGEDCVMMRGSG 262
Cdd:TIGR00864  351 RaGAALAIVDNDALQNFLARKVTHsldRGVWIGFSDVNGaeKGPAHQGEAFEAeECEEGLAGEPHP-ARAEHCVRLDPRG 429

                          170
                   ....*....|....*..
gi 359279914   263 QWNDAFCrSYLDAWVCE 279
Cdd:TIGR00864  430 QCNSDLC-NAPHAYVCE 445
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 36-147 3.23e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    36 IQNVSHVTKDLQKF--QSNQLAQKSQ------VVQMSQNLQELQAEQKQMKAQDSRLSQNltglQEDLRNaQSQNSKLSQ 107
Cdd:pfam15921   80 LEEYSHQVKDLQRRlnESNELHEKQKfylrqsVIDLQTKLQEMQMERDAMADIRRRESQS----QEDLRN-QLQNTVHEL 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 359279914   108 NLNR-LQDDLVNIKSLGLNEKRTASDSLEKLQEEVAKLWIE 147
Cdd:pfam15921  155 EAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD 195
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-148 5.04e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  23 ETEKNLKQLG---DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQ 99
Cdd:COG4372   42 KLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 359279914 100 SQNSKLSQNLNRLQDDLVNIKSlglnEKRTASDSLEKLQEEVAKLWIEI 148
Cdd:COG4372  122 KERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEEL 166
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 22-116 2.07e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.41  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   22 WETEKNLKQLgDTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQ-NLTGLQEDLRNAQS 100
Cdd:TIGR04320 254 NSLAALQAKL-ATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEA 332

                          90
                  ....*....|....*.
gi 359279914  101 QNSKLSQNLNRLQDDL 116
Cdd:TIGR04320 333 RLAKAKEALANLNADL 348
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 35-112 9.67e-04

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 38.10  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    35 AIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAE--------QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLS 106
Cdd:smart00503  16 NIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDikrlakeiRAKLKELEKENLENRASGSASDRTRKAQTEKLR 95


                   ....*.
gi 359279914   107 QNLNRL 112
Cdd:smart00503  96 KKFKEV 101
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
 57-145 2.43e-03

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 39.31  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  57 KSQVVQMSQNLQELQAE----QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSLGLNEKRTA-S 131
Cdd:PRK10920  59 KQQAQNQTATNDALANQltalQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAqA 138

                         90
                 ....*....|....
gi 359279914 132 DSLEKLQEEvaKLW 145
Cdd:PRK10920 139 DFLVKLAGR--KLW 150
 
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 ...
 159-279 7.34e-42

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: 140.90  E-value: 7.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 237
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 359279914 238 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 279
Cdd:cd03590   81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 159-279 5.00e-39

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 133.49  E-value: 5.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS----WIGLQDLNMEGEFVWSDGS 234
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 359279914   235 P-VGYSNWNPGEPNNGgqGEDCV-MMRGSGQWNDAFCRSYLdAWVCE 279
Cdd:smart00034  81 GpVSYSNWAPGEPNNS--SGDCVvLSTSGGKWNDVSCTSKL-PFVCE 124
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 159-278 6.14e-36

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: 125.93  E-value: 6.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSD-----LQGRLVSIHSQKEQDF---LMQHINKKDS----WIGLQDLNMEG 226
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFvydLFESSRGPDTpyglWIGLHDRTSEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 359279914 227 EFVWSDGSPVGYSNWNPGEPNNGGQGEDCVMMR----GSGQWNDAFCrSYLDAWVC 278
Cdd:cd03589   81 PFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWrrgdAGQSWNDMPC-DAVFPYIC 135
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 169-280 1.14e-34

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: 121.96  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 169 KCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS---WIGLQDLNMEGEFVWSDGSP-VGYSNWNPG 244
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 359279914 245 EPNNGGqGEDCVMMRGS--GQWNDAFCRSYLdAWVCEQ 280
Cdd:cd00037   81 EPNPGG-SEDCVVLSSSsdGKWNDVSCSSKL-PFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 177-280 2.41e-30

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 110.26  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  177 SKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINK--KDSWIGLQDLNMEGEFVWSDGSPVGYSNWNPgEPNNGGQGED 254
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 359279914  255 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 280
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKN-PFVCEK 105
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 168-279 2.67e-29

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: 107.77  E-value: 2.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 168 QKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS--WIGLQDLNMEGEFVWSDGSPVGYSNWNPGE 245
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTyaFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 359279914 246 PNNGGQGEDCVMMRGSGQWNDAFCRSYLDAwVCE 279
Cdd:cd03591   81 PNNAGGGEDCVEMYTSGKWNDVACNLTRLF-VCE 113
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 159-273 2.20e-23

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: 92.64  E-value: 2.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKdSWIGLQDLNMEGEFVWSDGSPVGY 238
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDY-QWIGLNDRTIEGDFRWSDGHPLQF 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 359279914 239 SNWNPGEPNN-GGQGEDCVMMRG--SGQWNDAFCRSYL 273
Cdd:cd03588   80 ENWRPNQPDNfFATGEDCVVMIWheEGEWNDVPCNYHL 117
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 171-266 5.44e-22

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: 88.64  E-value: 5.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 171 YYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHI-NKKDSWIGLQDLNMEGEFVWSDGSPVGYSNWNPGEP-NN 248
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFgGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPhNN 82

                         90       100
                 ....*....|....*....|..
gi 359279914 249 GGQGEDCVMMRG----SGQWND 266
Cdd:cd03603   83 GGGNEDYAAINHfpgiSGKWND 104
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 159-280 8.38e-21

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: 85.46  E-value: 8.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGSPvgY 238
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSP--L 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 359279914 239 SNWNpgEPNNGGQGEDCVMMrGSGQWNDAFCrSYLDAWVCEQ 280
Cdd:cd03593   79 NNLF--NIRGSTKSGNCAYL-SSTGIYSEDC-STKKRWICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 159-279 1.16e-17

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: 77.41  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCY-YFGKgSKQWIQARFACSDLQ--GRLVSIHSQKEQDFLMQHINK-----KDSWIGLQDLNMEGEFVW 230
Cdd:cd03594    1 CPKGWLPYKGNCYgYFRQ-PLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSyqkayQPVWIGLHDPQQSRGWEW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 359279914 231 SDGSPVGYSNWNPGEPNNggQGEDCVMMRGSG---QWNDAFCRSyLDAWVCE 279
Cdd:cd03594   80 SDGSKLDYRSWDRNPPYA--RGGYCAELSRSTgflKWNDANCEE-RNPFICK 128
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 171-279 3.64e-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: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 171 YYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS---WIGLQDLNMEGEFVWSDGSPVGYSNWNPGEPN 247
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 359279914 248 NGGqGEDCVMM--RGSGQWNDAFCRSYLDAwVCE 279
Cdd:cd03592   83 NGR-NENCLEIyiKDNGKWNDEPCSKKKSA-ICY 114
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 169-279 3.60e-15

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: 70.88  E-value: 3.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 169 KCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINK-----KDSWIGLQDLNMEGEFVWSDGSPVGYSNWN- 242
Cdd:cd03596   10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKAsvpgnWEVWLGINDMVAEGKWVDVNGSPISYFNWEr 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 359279914 243 --PGEPnNGGQGEDCVMMRGS--GQWNDAFCRSYLdAWVCE 279
Cdd:cd03596   90 eiTAQP-DGGKRENCVALSSSaqGKWFDEDCRREK-PYVCE 128
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 159-234 8.74e-13

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 66.29  E-value: 8.74e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGS 234
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNS 163
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 171-269 2.58e-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: 62.39  E-value: 2.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 171 YYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS--WIGLQDLNmeGEFVWSDGSPVGYSNWNPGEPnn 248
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSaaWIGLYRDV--DSWRWSDGSESSFRNWNTFQP-- 78

                         90       100
                 ....*....|....*....|.
gi 359279914 249 gGQGEDCVMMRGSGQWNDAFC 269
Cdd:cd03602   79 -FGQGDCATMYSSGRWYAALC 98
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 169-278 8.50e-12

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: 60.93  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 169 KCYYFGKGSKQWIQARFACSDL-QGRLVSIHSQkeqDFLMQ------HINKKDSWIGLQDLNMEG--EFVWSDGSPVGYS 239
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRCyRGNLASIHSF---AFNYRvqrlvsTLNQAQVWIGGIITGKGRcrRFSWVDGSVWNYA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 359279914 240 NWNPGEPnnGGQGEDCVMM--RGsGQWNDAFCrSYLDAWVC 278
Cdd:cd03598   79 YWAPGQP--GNRRGHCVELctRG-GHWRRAHC-KLRRPFIC 115
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 172-269 2.74e-09

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: 54.08  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 172 YFGKGSKQWIQARFACSDLQGRLVSI---HSQKEQDFLMQHINKK-DSWIGLQDL-NMEGEFVWSDGSPVG--YSNWNPG 244
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLASLamrDSEMRDAILAFTLVKGhGYWVGADNLqDGEYDFLWNDGVSLPtdSDLWAPN 83

                         90       100
                 ....*....|....*....|....*.
gi 359279914 245 EPNNGGQGEDCVMM-RGSGQWNDAFC 269
Cdd:cd03601   84 EPSNPQSRQLCVQLwSKYNLLDDEYC 109
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 159-250 4.07e-09

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 54.13  E-value: 4.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-------WIGLQDLNMEgEFVWS 231
Cdd:cd03597    1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMtkqkltpWVGLRKINVS-YWCWE 79

                         90       100
                 ....*....|....*....|.
gi 359279914 232 DGSPVGYS--NWNPGEPNNGG 250
Cdd:cd03597   80 DMSPFTNTtlQWLPGEPSDAG 100
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 112-279 2.46e-08

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: 55.47  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   112 LQDDLVNIKSLGLNekrtASDSLEKLQEEVAKlwieiliskgTACNICPKNWLHFQQ--KCYYFGKGSKQWIQARFACSD 189
Cdd:TIGR00864  285 LDLSIQNRGGSDLD----AAWKITAHGEEPAK----------ASHPHCPKDGEIFEEngHCFQIVPEEAAWLDAQEQCLA 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   190 L-QGRLVSIHSQKEQDFLMQHINK---KDSWIGLQDLNM--EGEFVWSDGSPV-GYSNWNPGEPNNgGQGEDCVMMRGSG 262
Cdd:TIGR00864  351 RaGAALAIVDNDALQNFLARKVTHsldRGVWIGFSDVNGaeKGPAHQGEAFEAeECEEGLAGEPHP-ARAEHCVRLDPRG 429

                          170
                   ....*....|....*..
gi 359279914   263 QWNDAFCrSYLDAWVCE 279
Cdd:TIGR00864  430 QCNSDLC-NAPHAYVCE 445
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 166-271 4.37e-08

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 51.43  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 166 FQQKCY---YFGKGSKQ--WIQARFACSDLQGRLVSIHSQKEQDFLMQHI-----NKKDSWIGL--------QDLNMEGE 227
Cdd:cd03595    8 TEKPCYkiaYFQDSRRRlnFEEARQACREDGGELLSIESENEQKLIERFIqtlraSDGDFWIGLrrssqynvTSSACSSL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 359279914 228 FVWSDGSPVGYSNWNPGEPNNGgqGEDCVMM-------RGSG-----QWNDAFCRS 271
Cdd:cd03595   88 YYWLDGSISTFRNWYVDEPSCG--SEVCVVMyhqpsapAGQGgpylfQWNDDNCNM 141
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 170-279 1.22e-07

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: 50.12  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 170 CYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS---------WIGLQ---------DLNMEGeFVW- 230
Cdd:cd03600    6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslrlWIGLQreprqcsdpSLPLRG-FSWv 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 359279914 231 SDGSPVGYSNWnPGEPNNGGQGEDCVMMRGSGQ------WNDAFCRSYLDAWVCE 279
Cdd:cd03600   85 TGDQDTDFSNW-LQEPAGTCTSPRCVALSAAGStpdnlkWKDGPCSARADGYLCK 138
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 36-147 3.23e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    36 IQNVSHVTKDLQKF--QSNQLAQKSQ------VVQMSQNLQELQAEQKQMKAQDSRLSQNltglQEDLRNaQSQNSKLSQ 107
Cdd:pfam15921   80 LEEYSHQVKDLQRRlnESNELHEKQKfylrqsVIDLQTKLQEMQMERDAMADIRRRESQS----QEDLRN-QLQNTVHEL 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 359279914   108 NLNR-LQDDLVNIKSLGLNEKRTASDSLEKLQEEVAKLWIE 147
Cdd:pfam15921  155 EAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD 195
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-148 5.04e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  23 ETEKNLKQLG---DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQ 99
Cdd:COG4372   42 KLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 359279914 100 SQNSKLSQNLNRLQDDLVNIKSlglnEKRTASDSLEKLQEEVAKLWIEI 148
Cdd:COG4372  122 KERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEEL 166
PHA02867 PHA02867
C-type lectin protein; Provisional
 158-217 5.14e-06

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 45.83  E-value: 5.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914 158 ICPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHiNKKDSWI 217
Cdd:PHA02867  48 VCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRY-GKGSYWI 106
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 46-143 1.73e-05

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 43.84  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   46 LQKFQSNQLAQKS---QVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDL------ 116
Cdd:pfam11559  44 LQQRDRDLEFRESlneTIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELqrlkna 123

                          90       100
                  ....*....|....*....|....*...
gi 359279914  117 -VNIKSLGLNEKRTASDSLEKLQEEVAK 143
Cdd:pfam11559 124 lQQIKTQFAHEVKKRDREIEKLKERLAQ 151
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
37-147 3.12e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  37 QNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDdl 116
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE-- 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 359279914 117 vnikslglnEKRTASDSLEKLQEEVAKLWIE 147
Cdd:COG4372  109 ---------EAEELQEELEELQKERQDLEQQ 130
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
33-148 5.63e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  33 DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRL 112
Cdd:COG4372   34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 359279914 113 QDDLVNIKslglNEKRTASDSLEKLQEEVAKLWIEI 148
Cdd:COG4372  114 QEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 54-144 6.67e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  54 LAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNI-KSLGLNEKR--TA 130
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEiaEL 95

                         90
                 ....*....|....
gi 359279914 131 SDSLEKLQEEVAKL 144
Cdd:COG4942   96 RAELEAQKEELAEL 109
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 159-237 1.07e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 41.77  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359279914 159 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGSPVG 237
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKGDDDDREVLDKVVK 124
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 22-116 2.07e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.41  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   22 WETEKNLKQLgDTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQ-NLTGLQEDLRNAQS 100
Cdd:TIGR04320 254 NSLAALQAKL-ATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEA 332

                          90
                  ....*....|....*.
gi 359279914  101 QNSKLSQNLNRLQDDL 116
Cdd:TIGR04320 333 RLAKAKEALANLNADL 348
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
55-148 2.76e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  55 AQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSLGL---NEKRTAS 131
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaqEELESLQ 107

                         90
                 ....*....|....*..
gi 359279914 132 DSLEKLQEEVAKLWIEI 148
Cdd:COG4372  108 EEAEELQEELEELQKER 124
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 31-143 4.64e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 41.25  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   31 LGDTAIQNVshvTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQ-NL 109
Cdd:TIGR04320 244 FDKTPIPNP---PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNL 320

                          90       100       110
                  ....*....|....*....|....*....|....
gi 359279914  110 NRLQDDLVNIKSlglnEKRTASDSLEKLQEEVAK 143
Cdd:TIGR04320 321 ATAQAALANAEA----RLAKAKEALANLNADLAK 350
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 56-145 8.36e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 40.48  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   56 QKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSLGLNEK----RTAS 131
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAqnnlATAQ 324

                          90
                  ....*....|....
gi 359279914  132 DSLEKLQEEVAKLW 145
Cdd:TIGR04320 325 AALANAEARLAKAK 338
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 35-112 9.67e-04

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 38.10  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    35 AIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAE--------QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLS 106
Cdd:smart00503  16 NIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDikrlakeiRAKLKELEKENLENRASGSASDRTRKAQTEKLR 95


                   ....*.
gi 359279914   107 QNLNRL 112
Cdd:smart00503  96 KKFKEV 101
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
 57-145 2.43e-03

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 39.31  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  57 KSQVVQMSQNLQELQAE----QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSLGLNEKRTA-S 131
Cdd:PRK10920  59 KQQAQNQTATNDALANQltalQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAqA 138

                         90
                 ....*....|....
gi 359279914 132 DSLEKLQEEvaKLW 145
Cdd:PRK10920 139 DFLVKLAGR--KLW 150
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 53-141 2.64e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914   53 QLAQKSQVVQMSQNLQELQAEQKQMKAQD-----------SRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDlvnIKS 121
Cdd:COG3096   520 QLAELEQRLRQQQNAERLLEEFCQRIGQQldaaeeleellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR---IKE 596

                          90       100
                  ....*....|....*....|..
gi 359279914  122 LGLNEK--RTASDSLEKLQEEV 141
Cdd:COG3096   597 LAARAPawLAAQDALERLREQS 618
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 43-144 3.45e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  43 TKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSl 122
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337

                         90       100
                 ....*....|....*....|..
gi 359279914 123 glnEKRTASDSLEKLQEEVAKL 144
Cdd:COG1196  338 ---ELEELEEELEEAEEELEEA 356
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-127 9.30e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914  23 ETEKNLKQLG---DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQ 99
Cdd:COG4372   77 QLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

                         90       100
                 ....*....|....*....|....*...
gi 359279914 100 SQNSKLSQNLNRLQDDLVNIKSLGLNEK 127
Cdd:COG4372  157 EQLESLQEELAALEQELQALSEAEAEQA 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-147 9.64e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 9.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359279914    23 ETEKNLKQLGDTAIQNVSHvTKDLQKFQSnQLAQ-KSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQ 101
Cdd:TIGR02168  240 ELEELQEELKEAEEELEEL-TAELQELEE-KLEElRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 359279914   102 NSKLS----QNLNRLQDDLVNIKSLG--LNEKRTASDSLEKLQEEVAKLWIE 147
Cdd:TIGR02168  318 LEELEaqleELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEE 369
 
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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