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Conserved domains on  [gi|76781460|ref|NP_001029096|]
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low affinity immunoglobulin epsilon Fc receptor isoform a [Rattus norvegicus]

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 ...
186-306 5.41e-41

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: 139.36  E-value: 5.41e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES-WIGLQDLNMEGEFVWPDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76781460 265 --YSNWSPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-175 2.21e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  60 DAAIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTL 139
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 76781460 140 QEDLVNVKsqglNEKRAASDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 114 QEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145
 
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 ...
186-306 5.41e-41

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: 139.36  E-value: 5.41e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES-WIGLQDLNMEGEFVWPDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76781460 265 --YSNWSPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
186-306 2.19e-37

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: 130.03  E-value: 2.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES----WIGLQDLNMEGEFVWPDGS 261
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 76781460    262 P-VGYSNWSPGEPNNGgqGEDCVMMRGS-GQWNDAFCRSYLdAWVCE 306
Cdd:smart00034  81 GpVSYSNWAPGEPNNS--SGDCVVLSTSgGKWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
204-307 5.55e-29

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 107.56  E-value: 5.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460   204 SKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINK--KESWIGLQDLNMEGEFVWPDGSPVGYSNWSPgEPNNGGQGED 281
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79
                          90       100
                  ....*....|....*....|....*..
gi 76781460   282 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 307
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKN-PFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
186-261 7.94e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.98  E-value: 7.94e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76781460  186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKESWIGLQDLNMEGEFVWPDGS 261
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNS 163
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-175 2.21e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  60 DAAIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTL 139
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 76781460 140 QEDLVNVKsqglNEKRAASDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 114 QEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
60-170 1.81e-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: 44.23  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    60 DAAIQNVSHVTkdLQNYQSNQLAQKS---QALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNL 136
Cdd:pfam11559  33 IARIINVIYEL--LQQRDRDLEFRESlneTIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKL 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 76781460   137 NTLQEDL-------VNVKSQGLNEKRAASDSLEKLQEEVAK 170
Cdd:pfam11559 111 KNEKEELqrlknalQQIKTQFAHEVKKRDREIEKLKERLAQ 151
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
91-172 5.19e-05

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: 44.33  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    91 SQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGLNEK----RAASDSLEKLQE 166
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAqnnlATAQAALANAEA 332

                  ....*.
gi 76781460   167 EVAKLW 172
Cdd:TIGR04320 333 RLAKAK 338
PRK11281 PRK11281
mechanosensitive channel MscK;
55-171 6.69e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 6.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    55 LKQLGDAAIQNVSHVTKDLQNYQSNQLAQKSQALQmSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQ----NS 130
Cdd:PRK11281   85 LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQA 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 76781460   131 ELSQNLNTLQEdLVNVKSQGLNEKRAASDSL-EKLQEEVAKL 171
Cdd:PRK11281  164 ALYANSQRLQQ-IRNLLKGGKVGGKALRPSQrVLLQAEQALL 204
 
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 ...
186-306 5.41e-41

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: 139.36  E-value: 5.41e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES-WIGLQDLNMEGEFVWPDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 76781460 265 --YSNWSPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
186-306 2.19e-37

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: 130.03  E-value: 2.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES----WIGLQDLNMEGEFVWPDGS 261
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyyWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 76781460    262 P-VGYSNWSPGEPNNGgqGEDCVMMRGS-GQWNDAFCRSYLdAWVCE 306
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 ...
186-305 2.12e-34

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: 122.85  E-value: 2.12e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCY-YFGEgSKQWIQAK-----FTCSDLEGRLVSIHSQKEQDFLMQHINKKES-------WIGLQDLNME 252
Cdd:cd03589   1 CPTFWTAFGGYCYrFFGD-RLTWEEAElrcrsFSIPGLIAHLVSIHSQEENDFVYDLFESSRGpdtpyglWIGLHDRTSE 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 76781460 253 GEFVWPDGSPVGYSNWSPGEPNNGGQGEDCVMMR----GSGQWNDAFCrSYLDAWVC 305
Cdd:cd03589  80 GPFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWrrgdAGQSWNDMPC-DAVFPYIC 135
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
196-307 7.67e-33

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: 118.11  E-value: 7.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 196 KCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES---WIGLQDLNMEGEFVWPDGSP-VGYSNWSPG 271
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSsdvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 76781460 272 EPNNGGqGEDCVMMRGS--GQWNDAFCRSYLdAWVCEQ 307
Cdd:cd00037  81 EPNPGG-SEDCVVLSSSsdGKWNDVSCSSKL-PFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
204-307 5.55e-29

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 107.56  E-value: 5.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460   204 SKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINK--KESWIGLQDLNMEGEFVWPDGSPVGYSNWSPgEPNNGGQGED 281
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79
                          90       100
                  ....*....|....*....|....*..
gi 76781460   282 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 307
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 ...
195-306 4.20e-26

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: 100.06  E-value: 4.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 195 QKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES--WIGLQDLNMEGEFVWPDGSPVGYSNWSPGE 272
Cdd:cd03591   1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTyaFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 76781460 273 PNNGGQGEDCVMMRGSGQWNDAFCRSYLDAwVCE 306
Cdd:cd03591  81 PNNAGGGEDCVEMYTSGKWNDVACNLTRLF-VCE 113
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
186-300 4.46e-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: 92.26  E-value: 4.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKEsWIGLQDLNMEGEFVWPDGSPVGY 265
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-WIGLNDRTIEGDFRWSDGHPLQF 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 76781460 266 SNWSPGEPNN-GGQGEDCVMMRG--SGQWNDAFCRSYL 300
Cdd:cd03588  80 ENWRPNQPDNfFATGEDCVVMIWheEGEWNDVPCNYHL 117
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
186-307 2.44e-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: 87.39  E-value: 2.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKESWIGLQDLNMEGEFVWPDGSPvgY 265
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSP--L 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 76781460 266 SNWspGEPNNGGQGEDCVMMrGSGQWNDAFCrSYLDAWVCEQ 307
Cdd:cd03593  79 NNL--FNIRGSTKSGNCAYL-SSTGIYSEDC-STKKRWICEK 116
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
198-293 3.08e-19

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: 81.70  E-value: 3.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 198 YYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINK-KESWIGLQDLNMEGEFVWPDGSPVGYSNWSPGEP-NN 275
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGyGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPhNN 82
                        90       100
                ....*....|....*....|..
gi 76781460 276 GGQGEDCVMMRG----SGQWND 293
Cdd:cd03603  83 GGGNEDYAAINHfpgiSGKWND 104
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
186-306 2.00e-16

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: 74.72  E-value: 2.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCY-YFGEgSKQWIQAKFTCSDLE--GRLVSIHSQKEQDFLMQHINK-----KESWIGLQDLNMEGEFVW 257
Cdd:cd03594   1 CPKGWLPYKGNCYgYFRQ-PLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSyqkayQPVWIGLHDPQQSRGWEW 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 76781460 258 PDGSPVGYSNWSPGEPNNggQGEDCVMMRGSG---QWNDAFCRSyLDAWVCE 306
Cdd:cd03594  80 SDGSKLDYRSWDRNPPYA--RGGYCAELSRSTgflKWNDANCEE-RNPFICK 128
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
196-306 3.70e-16

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: 73.96  E-value: 3.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 196 KCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINK-----KESWIGLQDLNMEGEFVWPDGSPVGYSNW-- 268
Cdd:cd03596  10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKAsvpgnWEVWLGINDMVAEGKWVDVNGSPISYFNWer 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 76781460 269 -SPGEPnNGGQGEDCVMMRGS--GQWNDAFCRSYLdAWVCE 306
Cdd:cd03596  90 eITAQP-DGGKRENCVALSSSaqGKWFDEDCRREK-PYVCE 128
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
198-306 5.32e-14

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: 67.40  E-value: 5.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 198 YYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES---WIGLQDLNMEGEFVWPDGSPVGYSNWSPGEPN 274
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 76781460 275 NGGqGEDCVMM--RGSGQWNDAFCRSYLDAwVCE 306
Cdd:cd03592  83 NGR-NENCLEIyiKDNGKWNDEPCSKKKSA-ICY 114
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
196-305 5.78e-13

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: 64.78  E-value: 5.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 196 KCYYFGEGSKQWIQAKFTCSDL-EGRLVSIHSQkeqDFLMQ------HINKKESWIGLQDLNMEG--EFVWPDGSPVGYS 266
Cdd:cd03598   2 RCYRFVKSPRTFRDAQVICRRCyRGNLASIHSF---AFNYRvqrlvsTLNQAQVWIGGIITGKGRcrRFSWVDGSVWNYA 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 76781460 267 NWSPGEPnnGGQGEDCVMM--RGsGQWNDAFCrSYLDAWVC 305
Cdd:cd03598  79 YWAPGQP--GNRRGHCVELctRG-GHWRRAHC-KLRRPFIC 115
PHA02642 PHA02642
C-type lectin-like protein; Provisional
186-261 7.94e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.98  E-value: 7.94e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76781460  186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKESWIGLQDLNMEGEFVWPDGS 261
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 ...
198-296 1.72e-10

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 57.38  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 198 YYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKK--ESWIGLQDLNmeGEFVWPDGSPVGYSNWSPGEPnn 275
Cdd:cd03602   3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSnsAAWIGLYRDV--DSWRWSDGSESSFRNWNTFQP-- 78
                        90       100
                ....*....|....*....|.
gi 76781460 276 gGQGEDCVMMRGSGQWNDAFC 296
Cdd:cd03602  79 -FGQGDCATMYSSGRWYAALC 98
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
199-296 1.54e-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: 54.85  E-value: 1.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 199 YFGEGSKQWIQAKFTCSDLEGRLVSI---HSQKEQDFLMQHINKKES-WIGLQDL-NMEGEFVWPDGSPVG--YSNWSPG 271
Cdd:cd03601   4 LCSDETMNYAKAGAFCRSRGMRLASLamrDSEMRDAILAFTLVKGHGyWVGADNLqDGEYDFLWNDGVSLPtdSDLWAPN 83
                        90       100
                ....*....|....*....|....*.
gi 76781460 272 EPNNGGQGEDCVMM-RGSGQWNDAFC 296
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 ...
186-277 4.78e-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: 53.74  E-value: 4.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES-------WIGLQDLNMEgEFVWP 258
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMtkqkltpWVGLRKINVS-YWCWE 79
                        90       100
                ....*....|....*....|.
gi 76781460 259 DGSPVGYS--NWSPGEPNNGG 277
Cdd:cd03597  80 DMSPFTNTtlQWLPGEPSDAG 100
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
197-306 4.22e-08

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: 51.66  E-value: 4.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 197 CYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKES---------WIGLQ---------DLNMEGeFVW- 257
Cdd:cd03600   6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslrlWIGLQreprqcsdpSLPLRG-FSWv 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 76781460 258 PDGSPVGYSNWsPGEPNNGGQGEDCVMMRGSGQ------WNDAFCRSYLDAWVCE 306
Cdd:cd03600  85 TGDQDTDFSNW-LQEPAGTCTSPRCVALSAAGStpdnlkWKDGPCSARADGYLCK 138
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
193-298 7.61e-07

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: 47.96  E-value: 7.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460 193 FQQKCY---YFGEGSKQ--WIQAKFTCSDLEGRLVSIHSQKEQDFLMQHI-NKKES----WIGL--------QDLNMEGE 254
Cdd:cd03595   8 TEKPCYkiaYFQDSRRRlnFEEARQACREDGGELLSIESENEQKLIERFIqTLRASdgdfWIGLrrssqynvTSSACSSL 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 76781460 255 FVWPDGSPVGYSNWSPGEPNNGgqGEDCVMM-------RGSG-----QWNDAFCRS 298
Cdd:cd03595  88 YYWLDGSISTFRNWYVDEPSCG--SEVCVVMyhqpsapAGQGgpylfQWNDDNCNM 141
PHA02867 PHA02867
C-type lectin protein; Provisional
185-244 1.06e-06

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 48.14  E-value: 1.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  185 VCPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHiNKKESWI 244
Cdd:PHA02867  48 VCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRY-GKGSYWI 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-175 2.21e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  60 DAAIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTL 139
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 76781460 140 QEDLVNVKsqglNEKRAASDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 114 QEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
53-171 3.13e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  53 KSLKQLGDAAIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSEL 132
Cdd:COG4372  48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 76781460 133 SQNLNTLQEDLVNVKSQGLN---EKRAASDSLEKLQEEVAKL 171
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEreeELKELEEQLESLQEELAAL 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
50-167 1.42e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  50 ETEKSLKQLgDAAIQNVSHVTKDLQNYQSNQLAQKSQ-------ALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDL 122
Cdd:COG4372  67 ELEQARSEL-EQLEEELEELNEQLQAAQAELAQAQEEleslqeeAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 76781460 123 INVKSQNSELSQNLNTLQEDLVNVKSQGLNEKRAASDS-LEKLQEE 167
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaLDELLKE 191
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
60-170 1.81e-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: 44.23  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    60 DAAIQNVSHVTkdLQNYQSNQLAQKS---QALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNL 136
Cdd:pfam11559  33 IARIINVIYEL--LQQRDRDLEFRESlneTIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKL 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 76781460   137 NTLQEDL-------VNVKSQGLNEKRAASDSLEKLQEEVAK 170
Cdd:pfam11559 111 KNEKEELqrlknalQQIKTQFAHEVKKRDREIEKLKERLAQ 151
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
82-175 2.44e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  82 AQKSQALQMSQ-NLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGL---NEKRAA 157
Cdd:COG4372  27 AALSEQLRKALfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaqEELESL 106
                        90
                ....*....|....*...
gi 76781460 158 SDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 107 QEEAEELQEELEELQKER 124
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
64-170 4.41e-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: 44.75  E-value: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  64 QNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDL 143
Cdd:COG4942 129 EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
                        90       100
                ....*....|....*....|....*..
gi 76781460 144 VNVKSQgLNEKRAASDSLEKLQEEVAK 170
Cdd:COG4942 209 AELAAE-LAELQQEAEELEALIARLEA 234
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
91-172 5.19e-05

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: 44.33  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    91 SQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGLNEK----RAASDSLEKLQE 166
Cdd:TIGR04320 253 PNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAqnnlATAQAALANAEA 332

                  ....*.
gi 76781460   167 EVAKLW 172
Cdd:TIGR04320 333 RLAKAK 338
PHA03097 PHA03097
C-type lectin-like protein; Provisional
186-246 5.33e-05

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 42.93  E-value: 5.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76781460  186 CPKDWLHFQQKCYYFGEGSKQWIQAKFTCSDLEGRLVSIHSQKEQDFLMQHINKKESWIGL 246
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGI 106
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
81-171 5.60e-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: 44.37  E-value: 5.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  81 LAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLvNVKSQGLN----EKRA 156
Cdd:COG4942  16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAelekEIAE 94
                        90
                ....*....|....*
gi 76781460 157 ASDSLEKLQEEVAKL 171
Cdd:COG4942  95 LRAELEAQKEELAEL 109
PRK11281 PRK11281
mechanosensitive channel MscK;
55-171 6.69e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 6.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    55 LKQLGDAAIQNVSHVTKDLQNYQSNQLAQKSQALQmSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQ----NS 130
Cdd:PRK11281   85 LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQA 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 76781460   131 ELSQNLNTLQEdLVNVKSQGLNEKRAASDSL-EKLQEEVAKL 171
Cdd:PRK11281  164 ALYANSQRLQQ-IRNLLKGGKVGGKALRPSQrVLLQAEQALL 204
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
53-143 1.37e-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: 43.18  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    53 KSLKQLGDAAIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQ-NLNELQEDLINVKSQNSE 131
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEARLAK 336
                          90
                  ....*....|..
gi 76781460   132 LSQNLNTLQEDL 143
Cdd:TIGR04320 337 AKEALANLNADL 348
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
68-168 1.64e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    68 HVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVK 147
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
                          90       100
                  ....*....|....*....|.
gi 76781460   148 sqglNEKRAASDSLEKLQEEV 168
Cdd:pfam05483 548 ----DELESVREEFIQKGDEV 564
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
77-171 1.80e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  77 QSNQLAQKSQALQMS-QNLEELQAEQKQMKSQDSQLSqnlnELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQgLNEKR 155
Cdd:COG1579  70 EVEARIKKYEEQLGNvRNNKEYEALQKEIESLKRRIS----DLEDEILELMERIEELEEELAELEAELAELEAE-LEEKK 144
                        90
                ....*....|....*..
gi 76781460 156 AASDS-LEKLQEEVAKL 171
Cdd:COG1579 145 AELDEeLAELEAELEEL 161
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
77-172 1.95e-04

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 42.78  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460   77 QSNQLAQKSQALQmsqnlEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGLNEKR- 155
Cdd:PRK10920  61 QAQNQTATNDALA-----NQLTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLl 135
                         90
                 ....*....|....*..
gi 76781460  156 AASDSLEKLQEEvaKLW 172
Cdd:PRK10920 136 AQADFLVKLAGR--KLW 150
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
62-171 2.45e-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: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    62 AIQNVSHVTKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQ-NLNTLQ 140
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQ 324
                          90       100       110
                  ....*....|....*....|....*....|.
gi 76781460   141 EDLVNVKSQGLNEKRAASDSLEKLQEEVAKL 171
Cdd:TIGR04320 325 AALANAEARLAKAKEALANLNADLAKKQAAL 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
70-176 2.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  70 TKDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQ 149
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                        90       100
                ....*....|....*....|....*..
gi 76781460 150 gLNEKRAASDSLEKLQEEVAKLWIEIL 176
Cdd:COG1196 339 -LEELEEELEEAEEELEEAEAELAEAE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
50-175 3.51e-04

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: 42.35  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460     50 ETEKSLKQLGdAAIQNVSHVTKDLQNYQSNQLAQKSQALQM-----------SQNLEELQAEQKQMKSQDSQLSQNLNEL 118
Cdd:TIGR02168  730 ALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERleeaeeelaeaEAEIEELEAQIEQLKEELKALREALDEL 808
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    119 QEDLINVKSQNSELSQNLNTLQEDLVNVKSQG---LNEKRAASDSLEKLQEEVAKLWIEI 175
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLedlEEQIEELSEDIESLAAEIEELEELI 868
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-171 3.83e-04

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: 42.35  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460     70 TKDLQNYQSNQLAQKSQALQMSQNLEELQAEQK-------QMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQED 142
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQeleekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
                           90       100       110
                   ....*....|....*....|....*....|..
gi 76781460    143 LVNVKSQ--GLNEKRAASDS-LEKLQEEVAKL 171
Cdd:TIGR02168  311 LANLERQleELEAQLEELESkLDELAEELAEL 342
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
80-168 5.90e-04

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: 41.86  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460   80 QLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLinvKSQNSELSQNLNTLQEDLVNVKSQG--LNEK--- 154
Cdd:COG3096  520 QLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL---EAQLEELEEQAAEAVEQRSELRQQLeqLRARike 596
                         90       100
                 ....*....|....*....|..
gi 76781460  155 --------RAASDSLEKLQEEV 168
Cdd:COG3096  597 laarapawLAAQDALERLREQS 618
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
79-171 9.26e-04

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: 41.20  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460     79 NQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLS---QNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQgLNEKR 155
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleEELEELQEELERLEEALEELREELEEAEQALDAAERE-LAQLQ 488
                           90
                   ....*....|....*.
gi 76781460    156 AASDSLEKLQEEVAKL 171
Cdd:TIGR02168  489 ARLDSLERLQENLEGF 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
79-163 1.04e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  79 NQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQE---------DLINVKSQNSELSQNLNTLQEDLVNVKSQ 149
Cdd:COG3206 155 NALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknGLVDLSEEAKLLLQQLSELESQLAEARAE 234
                        90
                ....*....|....
gi 76781460 150 gLNEKRAASDSLEK 163
Cdd:COG3206 235 -LAEAEARLAALRA 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-171 1.31e-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: 40.43  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460     52 EKSLKQLGDAAIQNVSHvtKDLQNYQSNQLAQKSQALQ-----MSQNLEELQAEQKQMKSQdsqlsqnLNELQEDLINVK 126
Cdd:TIGR02168  315 ERQLEELEAQLEELESK--LDELAEELAELEEKLEELKeelesLEAELEELEAELEELESR-------LEELEEQLETLR 385
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 76781460    127 SQNSELSQNLNTLQEDLVNVKSQglneKRAASDSLEKLQEEVAKL 171
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEAR----LERLEDRRERLQQEIEEL 426
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
79-146 1.60e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 36.87  E-value: 1.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76781460  79 NQLAQKSQALQMSqnLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNV 146
Cdd:COG3074   7 EELEAKVQQAVDT--IELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSL 72
RmuC pfam02646
RmuC family; This family contains several bacterial RmuC DNA recombination proteins. The ...
95-150 1.65e-03

RmuC family; This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures


Pssm-ID: 460637  Cd Length: 286  Bit Score: 39.40  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 76781460    95 EELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQG 150
Cdd:pfam02646  12 EKLEKFLEKVEETEKERSERLASLKEQLGELQELNQQVGDEANNLTRALKNPKTRG 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
74-174 1.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  74 QNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEdlinVKSQNSELSQNLNTLQEDLVNVKSQgLN- 152
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEE-LEs 105
                        90       100
                ....*....|....*....|....*
gi 76781460 153 ---EKRAASDSLEKLQEEVAKLWIE 174
Cdd:COG4372 106 lqeEAEELQEELEELQKERQDLEQQ 130
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
94-171 4.85e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460     94 LEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGLNEK---RAASDSLEKLQEEVAK 170
Cdd:TIGR02169  415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeyDRVEKELSKLQRELAE 494

                   .
gi 76781460    171 L 171
Cdd:TIGR02169  495 A 495
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
50-141 4.97e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.17  E-value: 4.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  50 ETEKSLKQLGDAAIQNVSHVT---KDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVK 126
Cdd:COG4026 111 EIKNAIIRAGLKSLQNIPEYNelrEELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIK 190
                        90
                ....*....|....*
gi 76781460 127 SQNSELSQNLNTLQE 141
Cdd:COG4026 191 SEYSDLKSRFEELLK 205
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
85-171 5.09e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 5.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  85 SQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQglnekraasdsLEKL 164
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE-----------IEER 84

                ....*..
gi 76781460 165 QEEVAKL 171
Cdd:COG3883  85 REELGER 91
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
89-171 7.57e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 37.40  E-value: 7.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  89 QMSQNLEELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQEDLVNVKSQGLNEKRAASDSLEKLQEEV 168
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211

                ...
gi 76781460 169 AKL 171
Cdd:COG4026 212 FSL 214
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
71-175 8.96e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 8.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460  71 KDLQNYQSNQLAQKSQALQMSQNLEELQAEQKQMKSQDSQLSQNLNELQEdlinVKSQNSELSQNLNTLQEDLVNVKSQG 150
Cdd:COG3883 112 ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA----LKAELEAAKAELEAQQAEQEALLAQL 187
                        90       100
                ....*....|....*....|....*
gi 76781460 151 LNEKRAASDSLEKLQEEVAKLWIEI 175
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAA 212
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
71-154 8.98e-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: 37.69  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76781460    71 KDLQNYQSNQLAQKSQALQMSQNL----------EELQAEQKQMKSQDSQLSQNLNELQEDLINVKSQNSELSQNLNTLQ 140
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
                          90
                  ....*....|....
gi 76781460   141 EDLVNVKSQgLNEK 154
Cdd:TIGR04523 260 DEQNKIKKQ-LSEK 272
 
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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