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Conserved domains on  [gi|1622895057|ref|XP_028694943|]
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glucosidase 2 subunit beta isoform X2 [Macaca mulatta]

Protein Classification

PRKCSH domain-containing protein; EF-hand domain-containing protein( domain architecture ID 11949190)

PRKCSH (protein kinase C substrate 80K-H) domain-containing protein similar to Ustilago maydis glucosidase 2 subunit beta, is a subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins in the endoplasmic reticulum (ER)| EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKCSH-like super family cl28164
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
 21-163 6.91e-46

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


The actual alignment was detected with superfamily member pfam12999:

Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 158.80  E-value: 6.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057  21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622895057  98 D---CCDGTDEynSGIVCENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLTELQ 163
Cdd:pfam12999 100 DydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDELKKRLKELE 166
PRKCSH super family cl06793
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 379-511 2.40e-18

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


The actual alignment was detected with superfamily member pfam13015:

Pssm-ID: 414904  Cd Length: 154  Bit Score: 82.19  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 379 AERSLKDVEESIRNLEQEIS-------FDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSW 451
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 452 AGpehdrfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAAC 511
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
XopAW super family cl49407
XopAW family type III secretion system calcium-binding effector;
214-312 9.24e-06

XopAW family type III secretion system calcium-binding effector;


The actual alignment was detected with superfamily member NF041410:

Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.98  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 214 AADAFQELDDDMDGTVSVTEL----------QTHPE-----------LDTDGDGALSEAEAQALLSGD-TQTDATSFFDr 271
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELaaaappppppPDQAPsteladdllsaLDTDGDGSISSDELSAGLTSAgSSADSSQLFS- 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622895057 272 vwaairdkyrseALPTDlpAPSAPDLTEPKEEQPPVPSPPT 312
Cdd:NF041410  144 ------------ALDSD--GDGSVSSDELAAALQPPPPPPL 170
 
Name Accession Description Interval E-value
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
 21-163 6.91e-46

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 158.80  E-value: 6.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057  21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622895057  98 D---CCDGTDEynSGIVCENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLTELQ 163
Cdd:pfam12999 100 DydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDELKKRLKELE 166
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 379-511 2.40e-18

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. The beta-subunit confers substrate specificity for di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit.


Pssm-ID: 404038  Cd Length: 154  Bit Score: 82.19  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 379 AERSLKDVEESIRNLEQEIS-------FDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSW 451
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 452 AGpehdrfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAAC 511
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-312 9.24e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.98  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 214 AADAFQELDDDMDGTVSVTEL----------QTHPE-----------LDTDGDGALSEAEAQALLSGD-TQTDATSFFDr 271
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELaaaappppppPDQAPsteladdllsaLDTDGDGSISSDELSAGLTSAgSSADSSQLFS- 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622895057 272 vwaairdkyrseALPTDlpAPSAPDLTEPKEEQPPVPSPPT 312
Cdd:NF041410  144 ------------ALDSD--GDGSVSSDELAAALQPPPPPPL 170
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 7.55e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 7.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895057 198 WEEQLAAAKVQREQELAADA---FQELDDDMDGTVSVTELQTH---------------PELDTDGDGALSEAEAQALL 257
Cdd:COG5126    52 REEFVAGMESLFEATVEPFAraaFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
212-257 2.24e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.75  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 212 ELAADAFQELDDDMDGTVSVTELQT--------------HPELDTDGDGALSEAEAQALL 257
Cdd:NF041410  103 ELADDLLSALDTDGDGSISSDELSAgltsagssadssqlFSALDSDGDGSVSSDELAAAL 162
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
208-256 3.91e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.98  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622895057 208 QREQELAADAFQELDDDMDGTVSVTELQTH-----------------PELDTDGDGALSEAE-AQAL 256
Cdd:NF041410   23 ARSQQFQKQLFAKLDSDGDGSVSQDELSSAlssksddgslidlselfSDLDSDGDGSLSSDElAAAA 89
EF-hand_5 pfam13202
EF hand;
216-236 7.52e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.83  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|.
gi 1622895057 216 DAFQELDDDMDGTVSVTELQT 236
Cdd:pfam13202   3 DTFRQIDLNGDGKISKEELRR 23
 
Name Accession Description Interval E-value
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
 21-163 6.91e-46

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 158.80  E-value: 6.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057  21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622895057  98 D---CCDGTDEynSGIVCENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLTELQ 163
Cdd:pfam12999 100 DydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDELKKRLKELE 166
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 379-511 2.40e-18

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. The beta-subunit confers substrate specificity for di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit.


Pssm-ID: 404038  Cd Length: 154  Bit Score: 82.19  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 379 AERSLKDVEESIRNLEQEIS-------FDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSW 451
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 452 AGpehdrfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAAC 511
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 412-470 5.08e-11

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


Pssm-ID: 400321  Cd Length: 72  Bit Score: 58.32  E-value: 5.08e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622895057 412 SQCYELTTNEYVYRLCPFKLVSQKPKL---GGSPTSLGTWG--SWAGPEHD--------RFSAMKYEQGTGC 470
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGqekGGSSFSLGRFSesSWAESTYDdewtkgsnRYISMIYGNGTKC 72
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-312 9.24e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.98  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 214 AADAFQELDDDMDGTVSVTEL----------QTHPE-----------LDTDGDGALSEAEAQALLSGD-TQTDATSFFDr 271
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELaaaappppppPDQAPsteladdllsaLDTDGDGSISSDELSAGLTSAgSSADSSQLFS- 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622895057 272 vwaairdkyrseALPTDlpAPSAPDLTEPKEEQPPVPSPPT 312
Cdd:NF041410  144 ------------ALDSD--GDGSVSSDELAAALQPPPPPPL 170
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 7.55e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 7.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895057 198 WEEQLAAAKVQREQELAADA---FQELDDDMDGTVSVTELQTH---------------PELDTDGDGALSEAEAQALL 257
Cdd:COG5126    52 REEFVAGMESLFEATVEPFAraaFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
212-257 2.24e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.75  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895057 212 ELAADAFQELDDDMDGTVSVTELQT--------------HPELDTDGDGALSEAEAQALL 257
Cdd:NF041410  103 ELADDLLSALDTDGDGSISSDELSAgltsagssadssqlFSALDSDGDGSVSSDELAAAL 162
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
208-256 3.91e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.98  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622895057 208 QREQELAADAFQELDDDMDGTVSVTELQTH-----------------PELDTDGDGALSEAE-AQAL 256
Cdd:NF041410   23 ARSQQFQKQLFAKLDSDGDGSVSQDELSSAlssksddgslidlselfSDLDSDGDGSLSSDElAAAA 89
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
215-271 5.92e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 5.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622895057 215 ADAFQELDDDMDGTVSVTELQTHPE-----------------LDTDGDGALSEAEAQALLS--GDTQTDATSFFDR 271
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMEslfeatvepfaraafdlLDTDGDGKISADEFRRLLTalGVSEEEADELFAR 111
EF-hand_5 pfam13202
EF hand;
216-236 7.52e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.83  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|.
gi 1622895057 216 DAFQELDDDMDGTVSVTELQT 236
Cdd:pfam13202   3 DTFRQIDLNGDGKISKEELRR 23
 
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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