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Conserved domains on  [gi|6323109|ref|NP_013181|]
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Emp46p [Saccharomyces cerevisiae S288C]

Protein Classification

lectin_EMP46_EMP47 domain-containing protein( domain architecture ID 10160976)

lectin_EMP46_EMP47 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lectin_EMP46_EMP47 cd06903
EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain; EMP46 and EMP47, ...
 56-270 4.22e-104

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.


:

Pssm-ID: 173891  Cd Length: 215  Bit Score: 308.06  E-value: 4.22e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109   56 WNKGYSLPNLLEVTDQQKELSQWTLGDKVKLEEGRFVLTPGKNTKGSLWLKPEYSIKDAMTIEWTFRSFGFRGSTKGGLA 135
Cdd:cd06903   1 LNKDLSLPNLLKISPNGKLIPNWQTSGNPKLESGRIILTPPGNQRGSLWLKKPLSLKDEWTIEWTFRSTGPEGRSGGGLN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109  136 FWLKQGNEGDSTELFGGSSKKFNGLMILLRLDDKLGESVTAYLNDGTKDLDIES--SPYFASCLFQYQDSMVPSTLRLTY 213
Cdd:cd06903  81 FWLVKDGNADVGTSSIYGPSKFDGLQLLIDNNGGSGGSLRGFLNDGSKDYKNEDvdSLAFGSCLFAYQDSGVPSTIRLSY 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323109  214 NPlDNHLLKLQMDNRVCFQTRKVKFMGsSPFRIGTSAINDASKESFEILKMKLYDGV 270
Cdd:cd06903 161 DA-LNSLFKVQVDNRLCFQTDKVQLPQ-GGYRFGITAANADNPESFEILKLKVWNGL 215
 
Name Accession Description Interval E-value
lectin_EMP46_EMP47 cd06903
EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain; EMP46 and EMP47, ...
 56-270 4.22e-104

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.


Pssm-ID: 173891  Cd Length: 215  Bit Score: 308.06  E-value: 4.22e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109   56 WNKGYSLPNLLEVTDQQKELSQWTLGDKVKLEEGRFVLTPGKNTKGSLWLKPEYSIKDAMTIEWTFRSFGFRGSTKGGLA 135
Cdd:cd06903   1 LNKDLSLPNLLKISPNGKLIPNWQTSGNPKLESGRIILTPPGNQRGSLWLKKPLSLKDEWTIEWTFRSTGPEGRSGGGLN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109  136 FWLKQGNEGDSTELFGGSSKKFNGLMILLRLDDKLGESVTAYLNDGTKDLDIES--SPYFASCLFQYQDSMVPSTLRLTY 213
Cdd:cd06903  81 FWLVKDGNADVGTSSIYGPSKFDGLQLLIDNNGGSGGSLRGFLNDGSKDYKNEDvdSLAFGSCLFAYQDSGVPSTIRLSY 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323109  214 NPlDNHLLKLQMDNRVCFQTRKVKFMGsSPFRIGTSAINDASKESFEILKMKLYDGV 270
Cdd:cd06903 161 DA-LNSLFKVQVDNRLCFQTDKVQLPQ-GGYRFGITAANADNPESFEILKLKVWNGL 215
Lectin_leg-like pfam03388
Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific ...
 78-268 1.11e-30

Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. These two proteins were the first recognized members of a family of animal lectins similar (19-24%) to the leguminous plant lectins. The alignment for this family aligns residues lying towards the N-terminus, where the similarity of VIP36 and ERGIC-53 is greatest. However, while Fiedler and Simons identified these proteins as a new family of animal lectins, our alignment also includes yeast sequences. ERGIC-53 is a 53kD protein, localized to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a calcium-dependent, mannose-specific lectin. Its dysfunction has been associated with combined factors V and VIII deficiency OMIM:227300 OMIM:601567, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein- secreting pathway.


Pssm-ID: 397453  Cd Length: 226  Bit Score: 117.92  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109     78 WTLGDKVKLEEGRFVLTPG-KNTKGSLWLKPEYSIKDaMTIEWTFRSFGFRGSTKGGLAFWLKQgNEGDSTELFgGSSKK 156
Cdd:pfam03388  24 WEYGGSTILSSNYIRLTPDlQSQKGSLWTKQPTDLDS-WEVEVTFRVHGSSRLFGDGLAIWYTS-ERGIEGPVF-GSKDK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109    157 FNGLMILLRLDD----KLGESVTAYLNDGTKDLDIESSPY---FASCLFQYQDSMVPSTLRLTY--NPL----DNHLLKL 223
Cdd:pfam03388 101 FNGLAIFLDTYDnhngPLFPYISGMLNDGSKPYDHDKDGThqeLASCTADFRNKDYPTLIRIKYdnNTLtvmiDNGLLEN 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6323109    224 QMDNRVCFQTRKVKFmgSSPFRIGTSAINDASKESFEILKMKLYD 268
Cdd:pfam03388 181 KVDWKLCFQVNNVIL--PTGYYFGVSAQTGDLSDNHDIFSILTFQ 223
 
Name Accession Description Interval E-value
lectin_EMP46_EMP47 cd06903
EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain; EMP46 and EMP47, ...
 56-270 4.22e-104

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.


Pssm-ID: 173891  Cd Length: 215  Bit Score: 308.06  E-value: 4.22e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109   56 WNKGYSLPNLLEVTDQQKELSQWTLGDKVKLEEGRFVLTPGKNTKGSLWLKPEYSIKDAMTIEWTFRSFGFRGSTKGGLA 135
Cdd:cd06903   1 LNKDLSLPNLLKISPNGKLIPNWQTSGNPKLESGRIILTPPGNQRGSLWLKKPLSLKDEWTIEWTFRSTGPEGRSGGGLN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109  136 FWLKQGNEGDSTELFGGSSKKFNGLMILLRLDDKLGESVTAYLNDGTKDLDIES--SPYFASCLFQYQDSMVPSTLRLTY 213
Cdd:cd06903  81 FWLVKDGNADVGTSSIYGPSKFDGLQLLIDNNGGSGGSLRGFLNDGSKDYKNEDvdSLAFGSCLFAYQDSGVPSTIRLSY 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323109  214 NPlDNHLLKLQMDNRVCFQTRKVKFMGsSPFRIGTSAINDASKESFEILKMKLYDGV 270
Cdd:cd06903 161 DA-LNSLFKVQVDNRLCFQTDKVQLPQ-GGYRFGITAANADNPESFEILKLKVWNGL 215
lectin_leg-like cd07308
legume-like lectins: ERGIC-53, ERGL, VIP36, VIPL, EMP46, and EMP47; The legume-like (leg-like) ...
 56-268 1.42e-38

legume-like lectins: ERGIC-53, ERGL, VIP36, VIPL, EMP46, and EMP47; The legume-like (leg-like) lectins are eukaryotic intracellular sugar transport proteins with a carbohydrate recognition domain similar to that of the legume lectins. This domain binds high-mannose-type oligosaccharides for transport from the endoplasmic reticulum to the Golgi complex. These leg-like lectins include ERGIC-53, ERGL, VIP36, VIPL, EMP46, EMP47, and the UIP5 (ULP1-interacting protein 5) precursor protein. Leg-like lectins have different intracellular distributions and dynamics in the endoplasmic reticulum-Golgi system of the secretory pathway and interact with N-glycans of glycoproteins in a calcium-dependent manner, suggesting a role in glycoprotein sorting and trafficking. 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.


Pssm-ID: 173892  Cd Length: 218  Bit Score: 139.02  E-value: 1.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109   56 WNKGYSLPNLLEVTDQqKELSQWTLGDKVKLEEGRFVLTP-GKNTKGSLWLKPEYSIKDaMTIEWTFRSFGFRGSTKGGL 134
Cdd:cd07308   1 FISEHSLSPPFLDDND-GEIGNWTVGGSTVITKNYIRLTPdVPSQSGSLWSRVPIPAKD-FEIEVEFSIHGGSGLGGDGF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109  135 AFWLKQgNEGDSTELFGGsSKKFNGLMILLRLDD---KLGESVTAYLNDGTKDLDIESS---PYFASCLFQYQDSMVPST 208
Cdd:cd07308  79 AFWYTE-EPGSDGPLFGG-PDKFKGLAIFFDTYDndgKGFPSISVFLNDGTKSYDYETDgekLELASCSLKFRNSNAPTT 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323109  209 LRLTYNpldNHLLKLQMD------NRVCFQTRKVKFMgsSPFRIGTSAINDASKESFEILKMKLYD 268
Cdd:cd07308 157 LRISYL---NNTLKVDITysegnnWKECFTVEDVILP--SQGYFGFSAQTGDLSDNHDILSVHTYE 217
Lectin_leg-like pfam03388
Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific ...
 78-268 1.11e-30

Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. These two proteins were the first recognized members of a family of animal lectins similar (19-24%) to the leguminous plant lectins. The alignment for this family aligns residues lying towards the N-terminus, where the similarity of VIP36 and ERGIC-53 is greatest. However, while Fiedler and Simons identified these proteins as a new family of animal lectins, our alignment also includes yeast sequences. ERGIC-53 is a 53kD protein, localized to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a calcium-dependent, mannose-specific lectin. Its dysfunction has been associated with combined factors V and VIII deficiency OMIM:227300 OMIM:601567, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein- secreting pathway.


Pssm-ID: 397453  Cd Length: 226  Bit Score: 117.92  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109     78 WTLGDKVKLEEGRFVLTPG-KNTKGSLWLKPEYSIKDaMTIEWTFRSFGFRGSTKGGLAFWLKQgNEGDSTELFgGSSKK 156
Cdd:pfam03388  24 WEYGGSTILSSNYIRLTPDlQSQKGSLWTKQPTDLDS-WEVEVTFRVHGSSRLFGDGLAIWYTS-ERGIEGPVF-GSKDK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323109    157 FNGLMILLRLDD----KLGESVTAYLNDGTKDLDIESSPY---FASCLFQYQDSMVPSTLRLTY--NPL----DNHLLKL 223
Cdd:pfam03388 101 FNGLAIFLDTYDnhngPLFPYISGMLNDGSKPYDHDKDGThqeLASCTADFRNKDYPTLIRIKYdnNTLtvmiDNGLLEN 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6323109    224 QMDNRVCFQTRKVKFmgSSPFRIGTSAINDASKESFEILKMKLYD 268
Cdd:pfam03388 181 KVDWKLCFQVNNVIL--PTGYYFGVSAQTGDLSDNHDIFSILTFQ 223
 
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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