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Conserved domains on  [gi|1841798949|ref|XP_034245111|]
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protein bark beetle isoform X2 [Thrips palmi]

Protein Classification

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 ...
 781-887 1.74e-25

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: 102.81  E-value: 1.74e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949   781 VRLLGGRTNREGRLQVRIDGAWGTVCNYGWTRLDAALVCHQLG----LVLNPDDWFlerseipqAGTTENILLSNVRCDD 856
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGfggaVSASGSAYF--------GPGSGPIWLDNVRCSG 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1841798949   857 DDTDITQCRaeRPDEFEFSCSHENDVGIRCY 887
Cdd:smart00202   73 TEASLSDCP--HSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1641-1734 4.28e-13

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: 67.40  E-value: 4.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 1641 NEGFLE-YYNRttlQWVPMCDDRFTERNAQVVCRELGFDSlnvFVNHGQRVE-FHYNSLSRIWSWpePLQCKGDESKLED 1718
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCGG---AVSAPSGCSyFGPGSTGPIWLD--DVRCSGNETSLWQ 76

                           90
                   ....*....|....*.
gi 1841798949 1719 CAIRLNGQlyghrHRC 1734
Cdd:pfam00530   77 CPHRPWGN-----HNC 87
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2311-2406 5.28e-08

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: 53.76  E-value: 5.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  2311 CPPGWALVGDTCYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQlyHFLQRQQQGFQLRHHVWV--------------- 2375
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEN--DFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1841798949  2376 -------------QNIDRINQCTAF--AYQTVEVDHCERLNPFVCE 2406
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLstSGGKWNDVSCTSKLPFVCE 124
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 203-286 1.46e-05

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


The actual alignment was detected with superfamily member cd00041:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 113  Bit Score: 46.25  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  203 PAEKDCSKYFFTRPGHVLTLHFLQVRTDRNESAK---IEVYDGANANDELLATIvirNGTK-PQSITTTRHNVYVRFRAQ 278
Cdd:cd00041     23 PNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRF---CGSTlPPPIISSGNSLTVRFRSD 99


                   ....*...
gi 1841798949  279 PKTQLVGF 286
Cdd:cd00041    100 SSVTGRGF 107
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 294-396 4.01e-05

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: 46.25  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  294 RKSYDLNVTGTTIADNNGRGIAAENLrSQIHVHQSSVSNNNHvAGVHvLGGAADVNITDSRIAFNMGDGVNISYTGGSRN 373
Cdd:pfam13229   52 SGSSNNTISNNTISNNGGGGIALRGS-SNNLIENNTISNNGG-AGIY-LSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128

                           90       100
                   ....*....|....*....|...
gi 1841798949  374 ISYSWLSSNKGYGMAVWLNDSKY 396
Cdd:pfam13229  129 ISNNTVTNNKGAGILIVGGSSNN 151
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 102-164 7.52e-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: 42.39  E-value: 7.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841798949  102 VTHSAYNGVNITMPSApIVMKNCTLRNNRGYGVFMNSSSGLAHIENSLIMENGGDGIRYIHHD 164
Cdd:pfam13229   87 ISNNGGAGIYLSDSSN-NTIENNIIHNNGGSGIVIEDSSNNVTISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 929-1001 4.32e-03

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: 40.47  E-value: 4.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841798949  929 IDFARHALESVRIVDNLQDGLGIiysdlyTSGGVNTVRNCEFSNNRGSGVSLKQL-GLKIYGSTMENNKQAGIR 1001
Cdd:pfam13229   29 RGSSNATIENNTITNNGGDGIEI------SGSSNNTISNNTISNNGGGGIALRGSsNNLIENNTISNNGGAGIY 96
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 781-887 1.74e-25

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: 102.81  E-value: 1.74e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949   781 VRLLGGRTNREGRLQVRIDGAWGTVCNYGWTRLDAALVCHQLG----LVLNPDDWFlerseipqAGTTENILLSNVRCDD 856
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGfggaVSASGSAYF--------GPGSGPIWLDNVRCSG 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1841798949   857 DDTDITQCRaeRPDEFEFSCSHENDVGIRCY 887
Cdd:smart00202   73 TEASLSDCP--HSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 786-886 2.51e-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: 93.59  E-value: 2.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  786 GRTNREGRLQVRIDGAWGTVCNYGWTRLDAALVCHQLGLvlnPDDW-FLERSEIPQAGTTENILLSNVRCDDDDTDITQC 864
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGC---GGAVsAPSGCSYFGPGSTGPIWLDDVRCSGNETSLWQC 77

                           90       100
                   ....*....|....*....|..
gi 1841798949  865 RaeRPDEFEFSCSHENDVGIRC 886
Cdd:pfam00530   78 P--HRPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1641-1734 4.28e-13

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: 67.40  E-value: 4.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 1641 NEGFLE-YYNRttlQWVPMCDDRFTERNAQVVCRELGFDSlnvFVNHGQRVE-FHYNSLSRIWSWpePLQCKGDESKLED 1718
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCGG---AVSAPSGCSyFGPGSTGPIWLD--DVRCSGNETSLWQ 76

                           90
                   ....*....|....*.
gi 1841798949 1719 CAIRLNGQlyghrHRC 1734
Cdd:pfam00530   77 CPHRPWGN-----HNC 87
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1628-1745 1.95e-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: 65.44  E-value: 1.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  1628 IRLCTGRNCtqqtNEGFLE-YYNRttlQWVPMCDDRFTERNAQVVCRELGFDSLNVFVnhgQRVEFHYNSlSRIWsWPEp 1706
Cdd:smart00202    1 VRLVGGGSP----CEGRVEvYHNG---QWGTVCDDGWDLRDANVVCRQLGFGGAVSAS---GSAYFGPGS-GPIW-LDN- 67

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1841798949  1707 LQCKGDESKLEDCAIRLNGqlyghRHRCEwDSPFVFIHC 1745
Cdd:smart00202   68 VRCSGTEASLSDCPHSGWG-----SHNCS-HGEDAGVVC 100
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2311-2406 5.28e-08

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: 53.76  E-value: 5.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  2311 CPPGWALVGDTCYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQlyHFLQRQQQGFQLRHHVWV--------------- 2375
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEN--DFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1841798949  2376 -------------QNIDRINQCTAF--AYQTVEVDHCERLNPFVCE 2406
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLstSGGKWNDVSCTSKLPFVCE 124
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 203-286 1.46e-05

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: 46.25  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  203 PAEKDCSKYFFTRPGHVLTLHFLQVRTDRNESAK---IEVYDGANANDELLATIvirNGTK-PQSITTTRHNVYVRFRAQ 278
Cdd:cd00041     23 PNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRF---CGSTlPPPIISSGNSLTVRFRSD 99


                   ....*...
gi 1841798949  279 PKTQLVGF 286
Cdd:cd00041    100 SSVTGRGF 107
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 294-396 4.01e-05

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: 46.25  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  294 RKSYDLNVTGTTIADNNGRGIAAENLrSQIHVHQSSVSNNNHvAGVHvLGGAADVNITDSRIAFNMGDGVNISYTGGSRN 373
Cdd:pfam13229   52 SGSSNNTISNNTISNNGGGGIALRGS-SNNLIENNTISNNGG-AGIY-LSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128

                           90       100
                   ....*....|....*....|...
gi 1841798949  374 ISYSWLSSNKGYGMAVWLNDSKY 396
Cdd:pfam13229  129 ISNNTVTNNKGAGILIVGGSSNN 151
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2322-2407 2.07e-04

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: 43.38  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 2322 CYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQ--LYHFLQRQQQGF---------QLRHHVWV--------------- 2375
Cdd:cd00037      2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENdfLASLLKKSSSSDvwiglndlsSEGTWKWSdgsplvdytnwapge 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1841798949 2376 QNIDRINQCTAFAYQT---VEVDHCERLNPFVCEM 2407
Cdd:cd00037     82 PNPGGSEDCVVLSSSSdgkWNDVSCSSKLPFICEK 116
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 102-164 7.52e-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: 42.39  E-value: 7.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841798949  102 VTHSAYNGVNITMPSApIVMKNCTLRNNRGYGVFMNSSSGLAHIENSLIMENGGDGIRYIHHD 164
Cdd:pfam13229   87 ISNNGGAGIYLSDSSN-NTIENNIIHNNGGSGIVIEDSSNNVTISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 929-1001 4.32e-03

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: 40.47  E-value: 4.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841798949  929 IDFARHALESVRIVDNLQDGLGIiysdlyTSGGVNTVRNCEFSNNRGSGVSLKQL-GLKIYGSTMENNKQAGIR 1001
Cdd:pfam13229   29 RGSSNATIENNTITNNGGDGIEI------SGSSNNTISNNTISNNGGGGIALRGSsNNLIENNTISNNGGAGIY 96
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 203-286 7.89e-03

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: 38.14  E-value: 7.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949   203 PAEKDCSKYFFTRPGHVLTLHFLQVRTDRNESAK---IEVYDGANANDELLATIVIrNGTKPQSITTTRHNVYVRFRAQP 279
Cdd:smart00042   13 PNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEydyVEIYDGPSASSPLLGRFCG-SEAPPPVISSSSNSLTLTFVSDS 91


                    ....*..
gi 1841798949   280 KTQLVGF 286
Cdd:smart00042   92 SVQKRGF 98
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 781-887 1.74e-25

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: 102.81  E-value: 1.74e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949   781 VRLLGGRTNREGRLQVRIDGAWGTVCNYGWTRLDAALVCHQLG----LVLNPDDWFlerseipqAGTTENILLSNVRCDD 856
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGfggaVSASGSAYF--------GPGSGPIWLDNVRCSG 72

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1841798949   857 DDTDITQCRaeRPDEFEFSCSHENDVGIRCY 887
Cdd:smart00202   73 TEASLSDCP--HSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 786-886 2.51e-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: 93.59  E-value: 2.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  786 GRTNREGRLQVRIDGAWGTVCNYGWTRLDAALVCHQLGLvlnPDDW-FLERSEIPQAGTTENILLSNVRCDDDDTDITQC 864
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGC---GGAVsAPSGCSYFGPGSTGPIWLDDVRCSGNETSLWQC 77

                           90       100
                   ....*....|....*....|..
gi 1841798949  865 RaeRPDEFEFSCSHENDVGIRC 886
Cdd:pfam00530   78 P--HRPWGNHNCSHSEDAGVIC 97
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1641-1734 4.28e-13

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: 67.40  E-value: 4.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 1641 NEGFLE-YYNRttlQWVPMCDDRFTERNAQVVCRELGFDSlnvFVNHGQRVE-FHYNSLSRIWSWpePLQCKGDESKLED 1718
Cdd:pfam00530    5 CEGRVEvYHNG---SWGTVCDDGWDLRDAHVVCRQLGCGG---AVSAPSGCSyFGPGSTGPIWLD--DVRCSGNETSLWQ 76

                           90
                   ....*....|....*.
gi 1841798949 1719 CAIRLNGQlyghrHRC 1734
Cdd:pfam00530   77 CPHRPWGN-----HNC 87
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1628-1745 1.95e-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: 65.44  E-value: 1.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  1628 IRLCTGRNCtqqtNEGFLE-YYNRttlQWVPMCDDRFTERNAQVVCRELGFDSLNVFVnhgQRVEFHYNSlSRIWsWPEp 1706
Cdd:smart00202    1 VRLVGGGSP----CEGRVEvYHNG---QWGTVCDDGWDLRDANVVCRQLGFGGAVSAS---GSAYFGPGS-GPIW-LDN- 67

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1841798949  1707 LQCKGDESKLEDCAIRLNGqlyghRHRCEwDSPFVFIHC 1745
Cdd:smart00202   68 VRCSGTEASLSDCPHSGWG-----SHNCS-HGEDAGVVC 100
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2311-2406 5.28e-08

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: 53.76  E-value: 5.28e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  2311 CPPGWALVGDTCYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQlyHFLQRQQQGFQLRHHVWV--------------- 2375
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEN--DFVASLLKNSGSSDYYWIglsdpdsngswqwsd 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1841798949  2376 -------------QNIDRINQCTAF--AYQTVEVDHCERLNPFVCE 2406
Cdd:smart00034   79 gsgpvsysnwapgEPNNSSGDCVVLstSGGKWNDVSCTSKLPFVCE 124
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 203-286 1.46e-05

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: 46.25  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  203 PAEKDCSKYFFTRPGHVLTLHFLQVRTDRNESAK---IEVYDGANANDELLATIvirNGTK-PQSITTTRHNVYVRFRAQ 278
Cdd:cd00041     23 PNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSydyLEIYDGPSTSSPLLGRF---CGSTlPPPIISSGNSLTVRFRSD 99


                   ....*...
gi 1841798949  279 PKTQLVGF 286
Cdd:cd00041    100 SSVTGRGF 107
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 294-396 4.01e-05

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: 46.25  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  294 RKSYDLNVTGTTIADNNGRGIAAENLrSQIHVHQSSVSNNNHvAGVHvLGGAADVNITDSRIAFNMGDGVNISYTGGSRN 373
Cdd:pfam13229   52 SGSSNNTISNNTISNNGGGGIALRGS-SNNLIENNTISNNGG-AGIY-LSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128

                           90       100
                   ....*....|....*....|...
gi 1841798949  374 ISYSWLSSNKGYGMAVWLNDSKY 396
Cdd:pfam13229  129 ISNNTVTNNKGAGILIVGGSSNN 151
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2322-2407 2.07e-04

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: 43.38  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 2322 CYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQ--LYHFLQRQQQGF---------QLRHHVWV--------------- 2375
Cdd:cd00037      2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENdfLASLLKKSSSSDvwiglndlsSEGTWKWSdgsplvdytnwapge 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1841798949 2376 QNIDRINQCTAFAYQT---VEVDHCERLNPFVCEM 2407
Cdd:cd00037     82 PNPGGSEDCVVLSSSSdgkWNDVSCSSKLPFICEK 116
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 337-478 3.36e-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: 43.55  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  337 AGVHVLGGAaDVNITDSRIAFNMGDGVNIsYTGGSRNISYSWLSSNKGYGMAVWLNDSKYMDHVAFHQ------------ 404
Cdd:pfam13229    1 SGILLNGSS-NATIKNNTISNNGGYGIYL-RGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNnggggialrgss 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841798949  405 ETVIAYSEIYKNLDTGILVGNFcgpSFVNITGNGFNNSLNTALEILSCwkanvsiPTKLQIGHNTFVQNKRLGI 478
Cdd:pfam13229   79 NNLIENNTISNNGGAGIYLSDS---SNNTIENNIIHNNGGSGIVIEDS-------SNNVTISNNTVTNNKGAGI 142
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 102-164 7.52e-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: 42.39  E-value: 7.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841798949  102 VTHSAYNGVNITMPSApIVMKNCTLRNNRGYGVFMNSSSGLAHIENSLIMENGGDGIRYIHHD 164
Cdd:pfam13229   87 ISNNGGAGIYLSDSSN-NTIENNIIHNNGGSGIVIEDSSNNVTISNNTVTNNKGAGILIVGGS 148
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 2311-2406 2.45e-03

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: 40.01  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949 2311 CPPGWALVGDTCYIYIGAPMTFHDARNFCRSDNASMPYVMSNYVQlyHFLQRQQQG--------FQLRHHVW-------- 2374
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEEL--EFLQSQIGSssywiglsREKSEKPWkwidgspl 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1841798949 2375 -----VQNIDRINQCTAFAYQTVEVDHCERLNPFVCE 2406
Cdd:cd03593     79 nnlfnIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICE 115
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 929-1001 4.32e-03

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: 40.47  E-value: 4.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841798949  929 IDFARHALESVRIVDNLQDGLGIiysdlyTSGGVNTVRNCEFSNNRGSGVSLKQL-GLKIYGSTMENNKQAGIR 1001
Cdd:pfam13229   29 RGSSNATIENNTITNNGGDGIEI------SGSSNNTISNNTISNNGGGGIALRGSsNNLIENNTISNNGGAGIY 96
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 296-437 5.37e-03

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: 40.08  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949  296 SYDLNVTGTTIADNNGRGIAAENLRSQIhVHQSSVSNNNHVAGvhVLGGAADVNITDSRIAFNMGDGVNISYTGGSRnIS 375
Cdd:pfam13229   31 SSNATIENNTITNNGGDGIEISGSSNNT-ISNNTISNNGGGGI--ALRGSSNNLIENNTISNNGGAGIYLSDSSNNT-IE 106

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841798949  376 YSWLSSNKGYGmaVWLNDSKYmdhvafhqETVIAYSEIYKNLDTGILVGNfcGPSFVNITGN 437
Cdd:pfam13229  107 NNIIHNNGGSG--IVIEDSSN--------NVTISNNTVTNNKGAGILIVG--GSSNNTVENN 156
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 203-286 7.89e-03

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: 38.14  E-value: 7.89e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841798949   203 PAEKDCSKYFFTRPGHVLTLHFLQVRTDRNESAK---IEVYDGANANDELLATIVIrNGTKPQSITTTRHNVYVRFRAQP 279
Cdd:smart00042   13 PNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEydyVEIYDGPSASSPLLGRFCG-SEAPPPVISSSSNSLTLTFVSDS 91


                    ....*..
gi 1841798949   280 KTQLVGF 286
Cdd:smart00042   92 SVQKRGF 98
 
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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