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Conserved domains on  [gi|386769054|ref|NP_001245864|]
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bark beetle, isoform B [Drosophila melanogaster]

Protein Classification

C-type lectin domain-containing protein; C-type lectin and CUB domain-containing protein( domain architecture ID 12193422)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein| C-type lectin and CUB (for complement C1r/C1s, Uegf, Bmp1) domain-containing protein; C-type lectin domain binds carbohydrate in a calcium-dependent manner, whereas CUB domain is found almost exclusively in extracellular and plasma membrane-associated proteins, many of which are developmentally regulated

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1071-1175 4.21e-31

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 118.98  E-value: 4.21e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   1071 VRLVGGAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYSlnpqdWRLLRSQLPNAGTSED-ILMANVRCTLQDR 1149
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFG-----GAVSASGSAYFGPGSGpIWLDNVRCSGTEA 75

                            90       100
                    ....*....|....*....|....*.
gi 386769054   1150 DVTKCRAEYEFENTCSHENDVGLRCY 1175
Cdd:smart00202   76 SLSDCPHSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 191-295 1.79e-27

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 108.58  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054    191 IRLVDGPTPVEGRLQLFHKGAWRSVCSNsrNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQ 270
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDD--GWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLS 78

                            90       100
                    ....*....|....*....|....*
gi 386769054    271 DCAWtsRQMGAGACDYHNDLGIQCL 295
Cdd:smart00202   79 DCPH--SGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1932-2017 1.29e-12

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


:

Pssm-ID: 459844  Cd Length: 98  Bit Score: 66.25  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  1932 NEGFLE-YFNHttlQWVPICDSRFTERNAQVVCRELGY-DPLNVYYGHDRrieFHTNSLTRIwsWVQPLECRGDEERMED 2009
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCgGAVSAPSGCSY---FGPGSTGPI--WLDDVRCSGNETSLWQ 76


                   ....*...
gi 386769054  2010 CAERLNGQ 2017
Cdd:pfam00530   77 CPHRPWGN 84
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2604-2699 2.59e-11

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: 63.39  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   2604 CPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRHLKYPDKVWI--------------- 2668
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAE--NDFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 386769054   2669 -------------QDYNHIDRCTSFVF--GEIEIEDCNKERGFICE 2699
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLSTsgGKWNDVSCTSKLPFVCE 124
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 459-552 2.73e-08

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 54.34  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  459 SLSFTQKYYagSGKECGKYFFTRPGYLLTLHFENFVLMQNETAT---VEIYDGASTNDRLLFEWKARnfTRPQSVTSTRE 535
Cdd:cd00041    15 SPNYPNNYP--NNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRFCGS--TLPPPIISSGN 90

                          90
                  ....*....|....*..
gi 386769054  536 KMFVRIRADARQELNGF 552
Cdd:cd00041    91 SLTVRFRSDSSVTGRGF 107
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 567-656 3.27e-04

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 43.93  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   567 VSQSTVEDNGGRGVAIDNiRSKLHVHSSSVSGNGHvAGVHVtSGAGDVNITSSNISFNNGAGVNITYYGGNRNISRSALT 646
Cdd:pfam13229   59 ISNNTISNNGGGGIALRG-SSNNLIENNTISNNGG-AGIYL-SDSSNNTIENNIIHNNGGSGIVIEDSSNNVTISNNTVT 135

                           90
                   ....*....|
gi 386769054   647 ANKGYGVATW 656
Cdd:pfam13229  136 NNKGAGILIV 145
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1071-1175 4.21e-31

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 118.98  E-value: 4.21e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   1071 VRLVGGAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYSlnpqdWRLLRSQLPNAGTSED-ILMANVRCTLQDR 1149
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFG-----GAVSASGSAYFGPGSGpIWLDNVRCSGTEA 75

                            90       100
                    ....*....|....*....|....*.
gi 386769054   1150 DVTKCRAEYEFENTCSHENDVGLRCY 1175
Cdd:smart00202   76 SLSDCPHSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 191-295 1.79e-27

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 108.58  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054    191 IRLVDGPTPVEGRLQLFHKGAWRSVCSNsrNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQ 270
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDD--GWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLS 78

                            90       100
                    ....*....|....*....|....*
gi 386769054    271 DCAWtsRQMGAGACDYHNDLGIQCL 295
Cdd:smart00202   79 DCPH--SGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1076-1174 1.35e-22

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 94.75  E-value: 1.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  1076 GAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYslnPQDWRLLRSQ-LPNAGTSEDILMANVRCTLQDRDVTKC 1154
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGC---GGAVSAPSGCsYFGPGSTGPIWLDDVRCSGNETSLWQC 77

                           90       100
                   ....*....|....*....|
gi 386769054  1155 RAEYEFENTCSHENDVGLRC 1174
Cdd:pfam00530   78 PHRPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 196-294 6.93e-18

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 81.27  E-value: 6.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   196 GPTPVEGRLQLFHKGAWRSVCSNsrNWTLADYGVACKQLGYRGGrfWNWVERTPGYYP----RLLYEQPKCKGGEGSLQD 271
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDD--GWDLRDAHVVCRQLGCGGA--VSAPSGCSYFGPgstgPIWLDDVRCSGNETSLWQ 76

                           90       100
                   ....*....|....*....|...
gi 386769054   272 CAWtsRQMGAGACDYHNDLGIQC 294
Cdd:pfam00530   77 CPH--RPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1932-2017 1.29e-12

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 66.25  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  1932 NEGFLE-YFNHttlQWVPICDSRFTERNAQVVCRELGY-DPLNVYYGHDRrieFHTNSLTRIwsWVQPLECRGDEERMED 2009
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCgGAVSAPSGCSY---FGPGSTGPI--WLDDVRCSGNETSLWQ 76


                   ....*...
gi 386769054  2010 CAERLNGQ 2017
Cdd:pfam00530   77 CPHRPWGN 84
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1932-2037 9.23e-12

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 63.90  E-value: 9.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   1932 NEGFLEYFNHTtlQWVPICDSRFTERNAQVVCRELGYDPLNVYYGhdrRIEFHTNSlTRIWsWVQpLECRGDEERMEDCA 2011
Cdd:smart00202   10 CEGRVEVYHNG--QWGTVCDDGWDLRDANVVCRQLGFGGAVSASG---SAYFGPGS-GPIW-LDN-VRCSGTEASLSDCP 81

                            90       100
                    ....*....|....*....|....*.
gi 386769054   2012 ERLNGqlyghRHECRWDDVfVFVSCN 2037
Cdd:smart00202   82 HSGWG-----SHNCSHGED-AGVVCS 101
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2604-2699 2.59e-11

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: 63.39  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   2604 CPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRHLKYPDKVWI--------------- 2668
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAE--NDFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 386769054   2669 -------------QDYNHIDRCTSFVF--GEIEIEDCNKERGFICE 2699
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLSTsgGKWNDVSCTSKLPFVCE 124
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 459-552 2.73e-08

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 54.34  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  459 SLSFTQKYYagSGKECGKYFFTRPGYLLTLHFENFVLMQNETAT---VEIYDGASTNDRLLFEWKARnfTRPQSVTSTRE 535
Cdd:cd00041    15 SPNYPNNYP--NNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRFCGS--TLPPPIISSGN 90

                          90
                  ....*....|....*..
gi 386769054  536 KMFVRIRADARQELNGF 552
Cdd:cd00041    91 SLTVRFRSDSSVTGRGF 107
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2615-2699 1.22e-06

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: 49.54  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054 2615 CFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRHlKYPDKVWI-------------------------- 2668
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEE--NDFLASLLKK-SSSSDVWIglndlssegtwkwsdgsplvdytnwa 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386769054 2669 ---QDYNHIDRC---TSFVFGEIEIEDCNKERGFICE 2699
Cdd:cd00037    79 pgePNPGGSEDCvvlSSSSDGKWNDVSCSSKLPFICE 115
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 567-656 3.27e-04

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 43.93  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   567 VSQSTVEDNGGRGVAIDNiRSKLHVHSSSVSGNGHvAGVHVtSGAGDVNITSSNISFNNGAGVNITYYGGNRNISRSALT 646
Cdd:pfam13229   59 ISNNTISNNGGGGIALRG-SSNNLIENNTISNNGG-AGIYL-SDSSNNTIENNIIHNNGGSGIVIEDSSNNVTISNNTVT 135

                           90
                   ....*....|
gi 386769054   647 ANKGYGVATW 656
Cdd:pfam13229  136 NNKGAGILIV 145
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2622-2699 3.56e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 42.46  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  2622 PMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRhlKYPDKVWIqDYNHIDRCTSFV-------------------- 2681
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEE--LDFLSSTLK--KSNKYFWI-GLTDRKNEGTWKwvdgspvnytnwapepnnng 75

                           90       100
                   ....*....|....*....|....*....
gi 386769054  2682 -----------FGEIEIEDCNKERGFICE 2699
Cdd:pfam00059   76 enedcvelsssSGKWNDENCNSKNPFVCE 104
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 459-552 5.85e-04

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 41.61  E-value: 5.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054    459 SLSFTQKYYagSGKECGKYFFTRPGYLLTLHFENFVLMQNETAT---VEIYDGASTNDRLL--FEWKARNftrPQSVTST 533
Cdd:smart00042    5 SPNYPQSYP--NNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEydyVEIYDGPSASSPLLgrFCGSEAP---PPVISSS 79

                            90
                    ....*....|....*....
gi 386769054    534 REKMFVRIRADARQELNGF 552
Cdd:smart00042   80 SNSLTLTFVSDSSVQKRGF 98
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1071-1175 4.21e-31

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 118.98  E-value: 4.21e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   1071 VRLVGGAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYSlnpqdWRLLRSQLPNAGTSED-ILMANVRCTLQDR 1149
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFG-----GAVSASGSAYFGPGSGpIWLDNVRCSGTEA 75

                            90       100
                    ....*....|....*....|....*.
gi 386769054   1150 DVTKCRAEYEFENTCSHENDVGLRCY 1175
Cdd:smart00202   76 SLSDCPHSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 191-295 1.79e-27

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 108.58  E-value: 1.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054    191 IRLVDGPTPVEGRLQLFHKGAWRSVCSNsrNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQ 270
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDD--GWDLRDANVVCRQLGFGGAVSASGSAYFGPGSGPIWLDNVRCSGTEASLS 78

                            90       100
                    ....*....|....*....|....*
gi 386769054    271 DCAWtsRQMGAGACDYHNDLGIQCL 295
Cdd:smart00202   79 DCPH--SGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1076-1174 1.35e-22

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 94.75  E-value: 1.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  1076 GAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYslnPQDWRLLRSQ-LPNAGTSEDILMANVRCTLQDRDVTKC 1154
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGC---GGAVSAPSGCsYFGPGSTGPIWLDDVRCSGNETSLWQC 77

                           90       100
                   ....*....|....*....|
gi 386769054  1155 RAEYEFENTCSHENDVGLRC 1174
Cdd:pfam00530   78 PHRPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 196-294 6.93e-18

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 81.27  E-value: 6.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   196 GPTPVEGRLQLFHKGAWRSVCSNsrNWTLADYGVACKQLGYRGGrfWNWVERTPGYYP----RLLYEQPKCKGGEGSLQD 271
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDD--GWDLRDAHVVCRQLGCGGA--VSAPSGCSYFGPgstgPIWLDDVRCSGNETSLWQ 76

                           90       100
                   ....*....|....*....|...
gi 386769054   272 CAWtsRQMGAGACDYHNDLGIQC 294
Cdd:pfam00530   77 CPH--RPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1932-2017 1.29e-12

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 66.25  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  1932 NEGFLE-YFNHttlQWVPICDSRFTERNAQVVCRELGY-DPLNVYYGHDRrieFHTNSLTRIwsWVQPLECRGDEERMED 2009
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCgGAVSAPSGCSY---FGPGSTGPI--WLDDVRCSGNETSLWQ 76


                   ....*...
gi 386769054  2010 CAERLNGQ 2017
Cdd:pfam00530   77 CPHRPWGN 84
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1932-2037 9.23e-12

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 63.90  E-value: 9.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   1932 NEGFLEYFNHTtlQWVPICDSRFTERNAQVVCRELGYDPLNVYYGhdrRIEFHTNSlTRIWsWVQpLECRGDEERMEDCA 2011
Cdd:smart00202   10 CEGRVEVYHNG--QWGTVCDDGWDLRDANVVCRQLGFGGAVSASG---SAYFGPGS-GPIW-LDN-VRCSGTEASLSDCP 81

                            90       100
                    ....*....|....*....|....*.
gi 386769054   2012 ERLNGqlyghRHECRWDDVfVFVSCN 2037
Cdd:smart00202   82 HSGWG-----SHNCSHGED-AGVVCS 101
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2604-2699 2.59e-11

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: 63.39  E-value: 2.59e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   2604 CPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRHLKYPDKVWI--------------- 2668
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAE--NDFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 386769054   2669 -------------QDYNHIDRCTSFVF--GEIEIEDCNKERGFICE 2699
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLSTsgGKWNDVSCTSKLPFVCE 124
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 459-552 2.73e-08

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 54.34  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  459 SLSFTQKYYagSGKECGKYFFTRPGYLLTLHFENFVLMQNETAT---VEIYDGASTNDRLLFEWKARnfTRPQSVTSTRE 535
Cdd:cd00041    15 SPNYPNNYP--NNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRFCGS--TLPPPIISSGN 90

                          90
                  ....*....|....*..
gi 386769054  536 KMFVRIRADARQELNGF 552
Cdd:cd00041    91 SLTVRFRSDSSVTGRGF 107
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2615-2699 1.22e-06

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: 49.54  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054 2615 CFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRHlKYPDKVWI-------------------------- 2668
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEE--NDFLASLLKK-SSSSDVWIglndlssegtwkwsdgsplvdytnwa 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386769054 2669 ---QDYNHIDRC---TSFVFGEIEIEDCNKERGFICE 2699
Cdd:cd00037    79 pgePNPGGSEDCvvlSSSSDGKWNDVSCSSKLPFICE 115
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 2604-2699 1.24e-04

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: 43.86  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054 2604 CPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRtDKTTLwKYLQSQMRH------LKYPDK----VWIQD--Y 2671
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID-DEEEL-EFLQSQIGSssywigLSREKSekpwKWIDGspL 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386769054 2672 NHI---------DRCTSFVFGEIEIEDCNKERGFICE 2699
Cdd:cd03593    79 NNLfnirgstksGNCAYLSSTGIYSEDCSTKKRWICE 115
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 567-656 3.27e-04

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 43.93  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   567 VSQSTVEDNGGRGVAIDNiRSKLHVHSSSVSGNGHvAGVHVtSGAGDVNITSSNISFNNGAGVNITYYGGNRNISRSALT 646
Cdd:pfam13229   59 ISNNTISNNGGGGIALRG-SSNNLIENNTISNNGG-AGIYL-SDSSNNTIENNIIHNNGGSGIVIEDSSNNVTISNNTVT 135

                           90
                   ....*....|
gi 386769054   647 ANKGYGVATW 656
Cdd:pfam13229  136 NNKGAGILIV 145
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2622-2699 3.56e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 42.46  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054  2622 PMTFHEARDFCRSENSTMPFIRTDKTtlWKYLQSQMRhlKYPDKVWIqDYNHIDRCTSFV-------------------- 2681
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEE--LDFLSSTLK--KSNKYFWI-GLTDRKNEGTWKwvdgspvnytnwapepnnng 75

                           90       100
                   ....*....|....*....|....*....
gi 386769054  2682 -----------FGEIEIEDCNKERGFICE 2699
Cdd:pfam00059   76 enedcvelsssSGKWNDENCNSKNPFVCE 104
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 459-552 5.85e-04

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 41.61  E-value: 5.85e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054    459 SLSFTQKYYagSGKECGKYFFTRPGYLLTLHFENFVLMQNETAT---VEIYDGASTNDRLL--FEWKARNftrPQSVTST 533
Cdd:smart00042    5 SPNYPQSYP--NNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEydyVEIYDGPSASSPLLgrFCGSEAP---PPVISSS 79

                            90
                    ....*....|....*....
gi 386769054    534 REKMFVRIRADARQELNGF 552
Cdd:smart00042   80 SNSLTLTFVSDSSVQKRGF 98
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 579-752 6.97e-04

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 42.78  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   579 GVAIDNiRSKLHVHSSSVSGNGHvAGVHVtSGAGDVNITSSNISFNNGAGVNITYYGGNRnISRSALTANKGYGVATWln 658
Cdd:pfam13229    2 GILLNG-SSNATIKNNTISNNGG-YGIYL-RGSSNATIENNTITNNGGDGIEISGSSNNT-ISNNTISNNGGGGIALR-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   659 qtsdvnrmeyipFNQTSVVEYSQIGGNLETGVFHGNFCRPIwvnITGNSFNGSQQNDIFIESCyqatangrpNMQLQLGH 738
Cdd:pfam13229   76 ------------GSSNNLIENNTISNNGGAGIYLSDSSNNT---IENNIIHNNGGSGIVIEDS---------SNNVTISN 131

                          170
                   ....*....|....
gi 386769054   739 NQFKYSQANSIYLS 752
Cdd:pfam13229  132 NTVTNNKGAGILIV 145
Fil_haemagg_2 pfam13332
Hemagglutinin repeat;
570-652 5.80e-03

Hemagglutinin repeat;


Pssm-ID: 433123 [Multi-domain]  Cd Length: 169  Bit Score: 40.31  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769054   570 STVedNGGRGVAIDNIRSKLHVHSSSVSGNGHVAgvhvTSGAGDVNI---------TSSNISFNNGAGVNITYYGGNRNI 640
Cdd:pfam13332   20 SNI--NAGGNVTITATSGDITIQGSQVSAGNGVA----LSAANDINLlaaenttqtTSTNSSSSASAGVSAGYGGGGGAF 93

                           90
                   ....*....|..
gi 386769054   641 SRSAlTANKGYG 652
Cdd:pfam13332   94 GVGA-SASGGKG 104
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 204-236 7.81e-03

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 38.47  E-value: 7.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 386769054   204 LQLF--HKGAWRSVCSNsrNWTlADYGV-ACKQLGY 236
Cdd:pfam15494    6 LQVYssARPSWLPVCSD--DWN-PAYGRaACQQLGY 38
 
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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