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Conserved domains on  [gi|75677363|ref|NP_068591|]
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protein ERGIC-53-like precursor [Homo sapiens]

Protein Classification

L-type lectin family protein( domain architecture ID 46946)

L-type (leguminous) lectin family protein binds carbohydrates using a a dome-shaped beta-barrel carbohydrate recognition domain

CATH:  2.60.120.200
Gene Ontology:  GO:0030246|GO:0046872
PubMed:  14572026|14533788
SCOP:  4000327

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lectin_L-type super family cl14058
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
 31-253 1.57e-131

legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate binding proteins that generally display no enzymatic activity toward the sugars they bind. This family includes arcelin, concanavalinA, the lectin-like receptor kinases, the ERGIC-53/VIP36/EMP46 type1 transmembrane proteins, and an alpha-amylase inhibitor. 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.


The actual alignment was detected with superfamily member cd06902:

Pssm-ID: 472686  Cd Length: 225  Bit Score: 381.29  E-value: 1.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  31 RRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGM 110
Cdd:cd06902   1 RRFEYKYSFKGPHLAQKDGTVPFWSHGGDAIASLEQVRLTPSLRSKKGSVWTKNPFSFENWEVEVTFRVTGRGRIGADGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 111 AVWYTRGRGHVGSVLGGLASWDGIGIFFDSPAED-TQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRA 189
Cdd:cd06902  81 AIWYTKERGEEGPVFGSSDKWNGVGIFFDSFDNDgKKNNPAILVVGNDGTKSYDHQNDGLTQALGSCLRDFRNKPYPVRA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677363 190 RITYWGQRLRMSLNSGLTPS-DPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSLS 253
Cdd:cd06902 161 KITYYQNVLTVSINNGFTPNkDDYELCTRVENMVLPPNGYFGVSAATGGLADDHDVLSFLTFSLT 225
 
Name Accession Description Interval E-value
lectin_ERGIC-53_ERGL cd06902
ERGIC-53 and ERGL type 1 transmembrane proteins, N-terminal lectin domain; ERGIC-53 and ERGL, ...
 31-253 1.57e-131

ERGIC-53 and ERGL type 1 transmembrane proteins, N-terminal lectin domain; ERGIC-53 and ERGL, N-terminal carbohydrate recognition domain. ERGIC-53 and ERGL are eukaryotic mannose-binding type 1 transmembrane proteins of the early secretory pathway that transport newly synthesized glycoproteins from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). ERGIC-53 and ERGL have an N-terminal lectin-like carbohydrate recognition domain (represented by this alignment model) as well as a C-terminal transmembrane domain. ERGIC-53 functions as a 'cargo receptor' to facilitate the export of glycoproteins with different characteristics from the ER, while the ERGIC-53-like protein (ERGL) which may act as a regulator of ERGIC-53. In mammals, ERGIC-53 forms a complex with MCFD2 (multi-coagulation factor deficiency 2) which then recruits blood coagulation factors V and VIII. Mutations in either MCFD2 or ERGIC-53 cause a mild form of inherited hemophilia known as combined deficiency of factors V and VIII (F5F8D). In addition to the lectin and transmembrane domains, ERGIC-53 and ERGL have a short N-terminal cytoplasmic region of about 12 amino acids. ERGIC-53 forms disulphide-linked homodimers and homohexamers. ERGIC-53 and ERGL are sequence-similar to the lectins of leguminous plants. 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: 173890  Cd Length: 225  Bit Score: 381.29  E-value: 1.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  31 RRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGM 110
Cdd:cd06902   1 RRFEYKYSFKGPHLAQKDGTVPFWSHGGDAIASLEQVRLTPSLRSKKGSVWTKNPFSFENWEVEVTFRVTGRGRIGADGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 111 AVWYTRGRGHVGSVLGGLASWDGIGIFFDSPAED-TQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRA 189
Cdd:cd06902  81 AIWYTKERGEEGPVFGSSDKWNGVGIFFDSFDNDgKKNNPAILVVGNDGTKSYDHQNDGLTQALGSCLRDFRNKPYPVRA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677363 190 RITYWGQRLRMSLNSGLTPS-DPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSLS 253
Cdd:cd06902 161 KITYYQNVLTVSINNGFTPNkDDYELCTRVENMVLPPNGYFGVSAATGGLADDHDVLSFLTFSLT 225
Lectin_leg-like pfam03388
Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific ...
 31-252 2.92e-69

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: 221.54  E-value: 2.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363    31 RRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGM 110
Cdd:pfam03388   1 DRFKREHSLKKPYLGQGSGTIPNWEYGGSTILSSNYIRLTPDLQSQKGSLWTKQPTDLDSWEVEVTFRVHGSSRLFGDGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363   111 AVWYTRGRGHVGSVLGGLASWDGIGIFFDS-PAEDTQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRA 189
Cdd:pfam03388  81 AIWYTSERGIEGPVFGSKDKFNGLAIFLDTyDNHNGPLFPYISGMLNDGSKPYDHDKDGTHQELASCTADFRNKDYPTLI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75677363   190 RITYWGQRLRMSLNSGLTP-SDPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSL 252
Cdd:pfam03388 161 RIKYDNNTLTVMIDNGLLEnKVDWKLCFQVNNVILPTGYYFGVSAQTGDLSDNHDIFSILTFQL 224
 
Name Accession Description Interval E-value
lectin_ERGIC-53_ERGL cd06902
ERGIC-53 and ERGL type 1 transmembrane proteins, N-terminal lectin domain; ERGIC-53 and ERGL, ...
 31-253 1.57e-131

ERGIC-53 and ERGL type 1 transmembrane proteins, N-terminal lectin domain; ERGIC-53 and ERGL, N-terminal carbohydrate recognition domain. ERGIC-53 and ERGL are eukaryotic mannose-binding type 1 transmembrane proteins of the early secretory pathway that transport newly synthesized glycoproteins from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). ERGIC-53 and ERGL have an N-terminal lectin-like carbohydrate recognition domain (represented by this alignment model) as well as a C-terminal transmembrane domain. ERGIC-53 functions as a 'cargo receptor' to facilitate the export of glycoproteins with different characteristics from the ER, while the ERGIC-53-like protein (ERGL) which may act as a regulator of ERGIC-53. In mammals, ERGIC-53 forms a complex with MCFD2 (multi-coagulation factor deficiency 2) which then recruits blood coagulation factors V and VIII. Mutations in either MCFD2 or ERGIC-53 cause a mild form of inherited hemophilia known as combined deficiency of factors V and VIII (F5F8D). In addition to the lectin and transmembrane domains, ERGIC-53 and ERGL have a short N-terminal cytoplasmic region of about 12 amino acids. ERGIC-53 forms disulphide-linked homodimers and homohexamers. ERGIC-53 and ERGL are sequence-similar to the lectins of leguminous plants. 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: 173890  Cd Length: 225  Bit Score: 381.29  E-value: 1.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  31 RRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGM 110
Cdd:cd06902   1 RRFEYKYSFKGPHLAQKDGTVPFWSHGGDAIASLEQVRLTPSLRSKKGSVWTKNPFSFENWEVEVTFRVTGRGRIGADGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 111 AVWYTRGRGHVGSVLGGLASWDGIGIFFDSPAED-TQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRA 189
Cdd:cd06902  81 AIWYTKERGEEGPVFGSSDKWNGVGIFFDSFDNDgKKNNPAILVVGNDGTKSYDHQNDGLTQALGSCLRDFRNKPYPVRA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677363 190 RITYWGQRLRMSLNSGLTPS-DPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSLS 253
Cdd:cd06902 161 KITYYQNVLTVSINNGFTPNkDDYELCTRVENMVLPPNGYFGVSAATGGLADDHDVLSFLTFSLT 225
Lectin_leg-like pfam03388
Legume-like lectin family; Lectins are structurally diverse proteins that bind to specific ...
 31-252 2.92e-69

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: 221.54  E-value: 2.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363    31 RRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGM 110
Cdd:pfam03388   1 DRFKREHSLKKPYLGQGSGTIPNWEYGGSTILSSNYIRLTPDLQSQKGSLWTKQPTDLDSWEVEVTFRVHGSSRLFGDGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363   111 AVWYTRGRGHVGSVLGGLASWDGIGIFFDS-PAEDTQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRA 189
Cdd:pfam03388  81 AIWYTSERGIEGPVFGSKDKFNGLAIFLDTyDNHNGPLFPYISGMLNDGSKPYDHDKDGTHQELASCTADFRNKDYPTLI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75677363   190 RITYWGQRLRMSLNSGLTP-SDPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSL 252
Cdd:pfam03388 161 RIKYDNNTLTVMIDNGLLEnKVDWKLCFQVNNVILPTGYYFGVSAQTGDLSDNHDIFSILTFQL 224
lectin_leg-like cd07308
legume-like lectins: ERGIC-53, ERGL, VIP36, VIPL, EMP46, and EMP47; The legume-like (leg-like) ...
 33-252 1.15e-48

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: 167.53  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  33 FEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGMAV 112
Cdd:cd07308   1 FISEHSLSPPFLDDNDGEIGNWTVGGSTVITKNYIRLTPDVPSQSGSLWSRVPIPAKDFEIEVEFSIHGGSGLGGDGFAF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 113 WYTRGRGHVGSVLGGLASWDGIGIFFDSPAEDTQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRARIT 192
Cdd:cd07308  81 WYTEEPGSDGPLFGGPDKFKGLAIFFDTYDNDGKGFPSISVFLNDGTKSYDYETDGEKLELASCSLKFRNSNAPTTLRIS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 193 YWGQRLRMSLNSglTPSDPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSL 252
Cdd:cd07308 161 YLNNTLKVDITY--SEGNNWKECFTVEDVILPSQGYFGFSAQTGDLSDNHDILSVHTYEL 218
lectin_VIP36_VIPL cd06901
VIP36 and VIPL type 1 transmembrane proteins, lectin domain; The vesicular integral protein of ...
 48-255 5.45e-42

VIP36 and VIPL type 1 transmembrane proteins, lectin domain; The vesicular integral protein of 36 kDa (VIP36) is a type 1 transmembrane protein of the mammalian early secretory pathway that acts as a cargo receptor transporting high mannose type glycoproteins between the Golgi and the endoplasmic reticulum (ER). Lectins of the early secretory pathway are involved in the selective transport of newly synthesized glycoproteins from the ER to the ER-Golgi intermediate compartment (ERGIC). The most prominent cycling lectin is the mannose-binding type1 membrane protein ERGIC-53, which functions as a cargo receptor to facilitate export of glycoproteins from the ER. 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: 173889  Cd Length: 248  Bit Score: 150.62  E-value: 5.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  48 GAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRR-GAQGMAVWYTRGRGHVGSVLG 126
Cdd:cd06901  16 GSSMPLWDFLGSTMVTSQYIRLTPDHQSKQGSIWNRVPCYLRDWEMHVHFKVHGSGKNlFGDGFAIWYTKERMQPGPVFG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 127 GLASWDGIGIFFDS----PAEDTQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRARITYWGQRLRMSL 202
Cdd:cd06901  96 SKDNFHGLAIFFDTysnqNGEHEHVHPYISAMVNNGSLSYDHDRDGTHTELAGCSAPFRNKDHDTFVAIRYSKGRLTVMT 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75677363 203 NSgltpSDPGEF--CVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSLSEP 255
Cdd:cd06901 176 DI----DGKNEWkeCFDVTGVRLPTGYYFGASAATGDLSDNHDIISMKLYELDVE 226
lectin_L-type cd01951
legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate ...
 50-251 2.87e-18

legume lectins; The L-type (legume-type) lectins are a highly diverse family of carbohydrate binding proteins that generally display no enzymatic activity toward the sugars they bind. This family includes arcelin, concanavalinA, the lectin-like receptor kinases, the ERGIC-53/VIP36/EMP46 type1 transmembrane proteins, and an alpha-amylase inhibitor. 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: 173886 [Multi-domain]  Cd Length: 223  Bit Score: 83.63  E-value: 2.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  50 GIPFWSHHGDAILGLEEV--RLTPSMRNRSGAVWSRASVPFSA-WEVEVQMRVTGLGRRGAQGMAVWYT------RGRGH 120
Cdd:cd01951  12 NQSNWQLNGSATLTTDSGvlRLTPDTGNQAGSAWYKTPIDLSKdFTTTFKFYLGTKGTNGADGIAFVLQndpagaLGGGG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 121 VGSVLGGLASWDGIGIFFDS-PAEDTQD--SPAIRVlasdgHIPSEQPGDGASQGLGSCHWDFRNRPHPFR-ARITY--W 194
Cdd:cd01951  92 GGGGLGYGGIGNSVAVEFDTyKNDDNNDpnGNHISI-----DVNGNGNNTALATSLGSASLPNGTGLGNEHtVRITYdpT 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677363 195 GQRLRMSLNSGltpSDPGEFCVDVgPLLLVPGG----FFGVSAATGTLADDHDVLSFLTFS 251
Cdd:cd01951 167 TNTLTVYLDNG---STLTSLDITI-PVDLIQLGptkaYFGFTASTGGLTNLHDILNWSFTS 223
lectin_EMP46_EMP47 cd06903
EMP46 and EMP47 type 1 transmembrane proteins, N-terminal lectin domain; EMP46 and EMP47, ...
 48-251 5.62e-16

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: 76.94  E-value: 5.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363  48 GAGIPFWSHHGDAILGLEEVRLTPSMRNRsGAVWSRASVPFS-AWEVEVQMRVTGLGRRGAQGMAVWYTRGRGHVGSV-- 124
Cdd:cd06903  17 GKLIPNWQTSGNPKLESGRIILTPPGNQR-GSLWLKKPLSLKdEWTIEWTFRSTGPEGRSGGGLNFWLVKDGNADVGTss 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363 125 LGGLASWDGIGIFFDSpaeDTQDSPAIRVLASDGHIPSeQPGDGASQGLGSCHWDFRNRPHPFRARITYwgqrlrMSLNS 204
Cdd:cd06903  96 IYGPSKFDGLQLLIDN---NGGSGGSLRGFLNDGSKDY-KNEDVDSLAFGSCLFAYQDSGVPSTIRLSY------DALNS 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75677363 205 GLTPSDPGEFCVDVGPLLLVPGGF-FGVSAATGTLADDHDVLSFLTFS 251
Cdd:cd06903 166 LFKVQVDNRLCFQTDKVQLPQGGYrFGITAANADNPESFEILKLKVWN 213
Lectin_legB pfam00139
Legume lectin domain;
186-263 5.87e-03

Legume lectin domain;


Pssm-ID: 459688  Cd Length: 245  Bit Score: 38.39  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677363   186 PFRARITYWGQRLRMS-----LNSGLTPSDP-GEFCVDVGPLLlvPGGFFGVSAATGTLADDHDVLSFlTFSLSEPSPEV 259
Cdd:pfam00139 162 PMQVWIDYDGSTKNLSvtlapYGLNNKPKRPlLSYPVDLSKVL--PEVYVGFSASTGNVSELHYILSW-SFSSSGPAPAI 238


                  ....
gi 75677363   260 PPQP 263
Cdd:pfam00139 239 DISK 242
 
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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