2A6X,2A6V,2A6Y


Conserved Protein Domain Family
lectin_EMP46_EMP47

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cd06903: lectin_EMP46_EMP47 
Click on image for an interactive view with Cn3D
EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain
EMP46 and EMP47, N-terminal carbohydrate recognition domain. EMP46 and EMP47 are fungal type-I transmembrane proteins that cycle between the endoplasmic reticulum and the golgi apparatus and are thought to function as cargo receptors that transport newly synthesized glycoproteins. EMP47 is a receptor for EMP46 responsible for the selective transport of EMP46 by forming hetero-oligomerization between the two proteins. EMP46 and EMP47 have an N-terminal lectin-like carbohydrate recognition domain (represented by this alignment model) as well as a C-terminal transmembrane domain. EMP46 and EMP47 are 45% sequence-identical to one another and have sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. L-type lectins have a dome-shaped beta-barrel carbohydrate recognition domain with a curved seven-stranded beta-sheet referred to as the "front face" and a flat six-stranded beta-sheet referred to as the "back face". This domain homodimerizes so that adjacent back sheets form a contiguous 12-stranded sheet and homotetramers occur by a back-to-back association of these homodimers. Though L-type lectins exhibit both sequence and structural similarity to one another, their carbohydrate binding specificities differ widely.
Statistics
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PSSM-Id: 173891
View PSSM: cd06903
Aligned: 20 rows
Threshold Bit Score: 243.735
Threshold Setting Gi: 46434591
Created: 24-Mar-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
metal bindingcarbohydrate
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:metal binding site [ion binding site]
Evidence:
  • Structure:2A6V; S.cerevisiae Emp46p Crd with bound potassium
    View structure with Cn3D
  • Comment:The carbohydrate recognition domain of Saccharomyces cerevisiae EMP47 cargo receptor binds K2+.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
2A6X_A         7 WNKGYSLPNLlevtd--qqkelSQWTLGDKVKLe----eGRFVLTpg--knTKGSLWLKPEYSIKdAMTIEWTFRSFGfr 78  baker's yeast
2A6V_A         7 WNKGYSLPNLlevtd--qqkelSQWTLGDKVKLe----eGRFVLTpg--knTKGSLWLKPEYSIKdAMTIEWTFRSFGfr 78  baker's yeast
2A6Y_A        14 LSSDYSLPDLintr-----kvpNNWQTGEQASLe----eGRIVLTsn--qnSKGSLWLKQGFDLKdSFTMEWTFRSVGys 82  baker's yeast
XP_449345     33 LDLEYSLPELvkln----dklpAHWRTSDATKLe----aGRFILTpt--knSKGSLWLKKSFNLEtSFTIEWTFRDVGfe 102 Candida glabrat...
XP_453323     37 LDASHSLPDLvhmn-----avpSDWKTSGGLVLe----eGRLRLTps--asSQSSIWHKTDYQIKdSFTIEWTFRSVDfi 105 Kluyveromyces l...
XP_001646692  31 LNKDFSLTNVlnmk-----kipDVWDVQGSSVLe----eGRIILTpk--esTKGSLWHKTSYPLGdSFTIEWTFRSVNhv 99  Vanderwaltozyma...
XP_001941817  24 VIDNLSFGHKetlsp--ngrgiPHWNIQGNEDWlpqlfsDRIILTppypgnKRGSVWTEDPLHHKgDWVAEVHFRASGqe 101 Pyrenophora tri...
XP_001557171  23 LNNDLSFGHDgkisp--ngraiPNFHMIGQPNYpdi-lsNRIVLTppalgnQRGAVWTEKKLQHS-QWAADIEFRATGpe 98  Botryotinia fuc...
XP_001229457  22 LVNELSFGHShrispe-gtqsiPNFSLQGRPNVpel-lsDKVILTpvapgnQRGAVWADKSLQNQ-NWIADVEFRANGpe 98  Chaetomium glob...
XP_382705     21 LISELSFGHAgrispaesrgqiPNFAVQGNPNTpei-lsNRIILTplapgnQRGAIWGQQPLLRT-QWIADVDFRANGpd 98  Gibberella zeae...
Feature 1                                                               #         ##    #        
2A6X_A        79 gstKGGLAFWLKQGNEgdst------elfgGSSKKFNGLMILLRLDDklgESVTAFLNDGTKDLDIEs---SPYFASCLF 149 baker's yeast
2A6V_A        79 gstKGGLAFWLKQGNEgdst------elfgGSSKKFNGLMILLRLDDklgESVTAYLNDGTKDLDIEs---SPYFASCLF 149 baker's yeast
2A6Y_A        83 gqtDGGISFWFVQDSNiprd------kqlyNGPVNYDGLQLLVDNNGplgPTLRGQLNDGQKPVDKTki-yDQSFASCLM 155 baker's yeast
XP_449345    103 gdsKAAMAFWFVTGSSeqeidetlkdksmvNGPSKFDGLMLHLDTNEvhgPSIRAQLNDKITAFTPEiv-hEKSFGSCLL 181 Candida glabrat...
XP_453323    106 gksEGGLSFWLVEGKSaggt-------slfGGPEAFDGLQILVDSNGpvgSSVRGILNDGSKKLTEKnv-yDHSFAYCLL 177 Kluyveromyces l...
XP_001646692 100 gksEGGLSFWFITGAQkddq-------alfNGPSTYDGLQLLVDNNGpvsPSIRAILNDGSKPVPKAdl-yDKTFAYCLM 171 Vanderwaltozyma...
XP_001941817 102 -rgGGNLQIWYTKQSQarep------paslYTTHKFDGLVLLVDQYEnhgGSLRGFLNDGTVDIGAHpdpdTLAFGKCDY 174 Pyrenophora tri...
XP_001557171  99 -raGGNLNIWYAKNEDikv--------ssiYTVGKFDGLALVIDQYAgsgGYIRGFLNDGTTEYSSHhsvdSLAFGHCPY 169 Botryotinia fuc...
XP_001229457  99 -raGGNLNIWLVRDGAhvvg------sdsvYSAGKFEGLGLVIDQHSgsgGMLRGFLNDGTTDYKNNhnvdSLAFAQCSF 171 Chaetomium glob...
XP_382705     99 -rgRGNLNIWLVRNGPatig------agsiYTVGKFDGLALVIDTSGgssGMVRGFLNDGNTDYSRQnnvdELSFGHCPY 171 Gibberella zeae...
Feature 1                                                                                   
2A6X_A       150 QYQDSMVPSTLRLTYNpldnHLLKLQMDNRVCFQTRKVKFMgsSPFRIGTSAINDa---SKESFEILKMKLYDGV 221 baker's yeast
2A6V_A       150 QYQDSMVPSTLRLTYNpldnHLLKLQMDNRVCFQTRKVKFMgsSPFRIGTSAINDa---SKESFEILKMKLYDGV 221 baker's yeast
2A6Y_A       156 GYQDSSVPSTIRVTYDleddNLLKVQVDNKVCFQTRKVRFPs-GSYRIGVTAQNGavnnNAESFEIFKMQFFNGV 229 baker's yeast
XP_449345    182 AYQDSAVPTTARLTYDkdnkSMLKLQIDNRVCFQTFKVKLPq-GLYRFGVTAVNDn---NAESFEILKMHAYNGV 252 Candida glabrata CBS138
XP_453323    178 AYQDTTIPTTIRLSYDrknnNLLKLQVDNRVCFQTRQIQFPqnAKMKMGITAKNDa---NKESFEVLKVHTHNGL 249 Kluyveromyces lactis...
XP_001646692 172 GYQDSSVPSTLRLTYDrndnNLLKLQVDNRVCFQTRKVQIPk-GNYRIGVTADNGn---TPEHFELFKMKTFDGV 242 Vanderwaltozyma poly...
XP_001941817 175 AYRNRGELTPIKLHHAe---GFLEVIIDGETCFKTDKVILP--EGYYFGISASSAe---NPDSFEVHKFTVSTTY 241 Pyrenophora tritici-...
XP_001557171 170 SYRNRGIPSKIHIRQTa---DNFKVEVDGALCFQSDKIKLP--LGYVFGVTAASAe---NPDSFEIFKFVVTTDS 236 Botryotinia fuckelia...
XP_001229457 172 TYRNLGRPTQIKLRHTe---SKFSVEVAGRHCFDTDKVRIP--SGYNFGISAASAd---NPDSFEVFKLAVLTTN 238 Chaetomium globosum ...
XP_382705    172 NYRNLGRPSQVKLRQTa---RAFRVELDGKLCFESDKISIP--TGYQFGVTAATPd---NPDSFEVFKMVVMADN 238 Gibberella zeae PH-1

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