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Conserved domains on  [gi|41054978|ref|NP_957347|]
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glucosidase 2 subunit beta precursor [Danio rerio]

Protein Classification

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 ...
7-169 8.84e-43

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: 150.32  E-value: 8.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978     7 LLTLVFAVSLGTPVEVHRPRGVPLSKKPFYE--ENKPFTCLDGSKTIL-FDQVNDDYCDCKGGSDEPGTAACPNGKFHCT 83
Cdd:pfam12999   1 LLQPLLAISLLVAIALGKLRGVSPDNLHLYQpdENGNWKCLNHSEIKLsFDQVNDDYCDCPDGSDEPGTNACSNGKFYCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978    84 NAGYKPTFIPSSRINDGICD---CCDTTDEynSGAKCENTCKELGRKEREVLQKMAEITKEGFLLKQQLIEEAKKGRGEK 160
Cdd:pfam12999  81 NEGFIPGYIPSFKVDDGVCDydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDEL 158

                  ....*....
gi 41054978   161 QSKVTEMQD 169
Cdd:pfam12999 159 KKRLKELED 167
PRKCSH super family cl06793
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
381-513 3.59e-17

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: 78.72  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   381 AEKALREMDDQIRNIEKELS-------FDFGPNAEFTYLYSQCYELSTSEYIYRLCPFNRVSQKpkfggsETNLGTWGSW 453
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQD------DISIGNFKKQ 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   454 sgpENNKylsMKYEHGTGCWQGPNRSTTVKLTCGKETMLTSTSEPSRCEYLMEFITPAVC 513
Cdd:pfam13015  75 ---EGNK---LYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
PRK00409 super family cl29770
recombination and DNA strand exchange inhibitor protein; Reviewed
145-219 6.18e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


The actual alignment was detected with superfamily member PRK00409:

Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 6.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054978  145 LKQQLIEEAKKGRGEKQSKVTEM----QDNKKQLEEKVEAlrtvketAEQPEREAkERHLKAWEEQKAAIRLVKDKAKM 219
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNELiaslEELERELEQKAEE-------AEALLKEA-EKLKEELEEKKEKLQEEEDKLLE 569
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
217-262 4.96e-03

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054978 217 AKMAEAFLELDDNADGLVSVSELQSH---------------AELDSDTDGTLSEAEAKGLM 262
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
GrpE super family cl03075
nucleotide exchange factor GrpE; GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70) ...
348-400 8.91e-03

nucleotide exchange factor GrpE; GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.


The actual alignment was detected with superfamily member PRK14144:

Pssm-ID: 446000 [Multi-domain]  Cd Length: 199  Bit Score: 37.78  E-value: 8.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41054978  348 EKSQEDEEAM--PPYEADTQVLIEAAQKARDDFEEAEKALREMDDQIRNIEKELS 400
Cdd:PRK14144  33 EESQHQEPALghPSYTALEEQLTLAEQKAHENWEKSVRALAELENVRRRMEREVA 87
 
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 ...
7-169 8.84e-43

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: 150.32  E-value: 8.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978     7 LLTLVFAVSLGTPVEVHRPRGVPLSKKPFYE--ENKPFTCLDGSKTIL-FDQVNDDYCDCKGGSDEPGTAACPNGKFHCT 83
Cdd:pfam12999   1 LLQPLLAISLLVAIALGKLRGVSPDNLHLYQpdENGNWKCLNHSEIKLsFDQVNDDYCDCPDGSDEPGTNACSNGKFYCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978    84 NAGYKPTFIPSSRINDGICD---CCDTTDEynSGAKCENTCKELGRKEREVLQKMAEITKEGFLLKQQLIEEAKKGRGEK 160
Cdd:pfam12999  81 NEGFIPGYIPSFKVDDGVCDydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDEL 158

                  ....*....
gi 41054978   161 QSKVTEMQD 169
Cdd:pfam12999 159 KKRLKELED 167
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
381-513 3.59e-17

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: 78.72  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   381 AEKALREMDDQIRNIEKELS-------FDFGPNAEFTYLYSQCYELSTSEYIYRLCPFNRVSQKpkfggsETNLGTWGSW 453
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQD------DISIGNFKKQ 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   454 sgpENNKylsMKYEHGTGCWQGPNRSTTVKLTCGKETMLTSTSEPSRCEYLMEFITPAVC 513
Cdd:pfam13015  75 ---EGNK---LYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
145-219 6.18e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 6.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054978  145 LKQQLIEEAKKGRGEKQSKVTEM----QDNKKQLEEKVEAlrtvketAEQPEREAkERHLKAWEEQKAAIRLVKDKAKM 219
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNELiaslEELERELEQKAEE-------AEALLKEA-EKLKEELEEKKEKLQEEEDKLLE 569
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
126-218 3.03e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   126 RKEREVLQKMAEITKEgfllKQQliEEAKKGRGEKQ-SKVTEMQ--DNKKQL-----EEKVEALRTVKETAEQPEREAKE 197
Cdd:pfam15709 423 QQQEEFRRKLQELQRK----KQQ--EEAERAEAEKQrQKELEMQlaEEQKRLmemaeEERLEYQRQKQEAEEKARLEAEE 496
                          90       100
                  ....*....|....*....|.
gi 41054978   198 RHLKAweeqKAAIRLVKDKAK 218
Cdd:pfam15709 497 RRQKE----EEAARLALEEAM 513
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
217-262 4.96e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054978 217 AKMAEAFLELDDNADGLVSVSELQSH---------------AELDSDTDGTLSEAEAKGLM 262
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
PTZ00121 PTZ00121
MAEBL; Provisional
109-399 5.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   109 DEYNSGAKCENTCKELGRKEREV-----LQKMAEITKEGFLLKQQlIEEAKKGR--GEKQSKVTEMQDNKKQLEEKVEAl 181
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKkkadeAKKKAEEAKKADEAKKK-AEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKA- 1485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   182 RTVKETAEQPEREAKERHLKAWEEQKAAIRLVKDKAKMAEAFLELDD--NADGLVSVSELQSHAELDSDTDGTLSEAEAK 259
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   260 glmggVEQVDTATfesvweniKDKYHSESQPEEPAPVETPVDEVKEPVVDNESEPYPEDISEEEDEDDDDDDEYHEEDEK 339
Cdd:PTZ00121 1566 -----AEEAKKAE--------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054978   340 APPTMKTPEKSQEDEEAMPPYEADTQVLIEAAQKARDDFEEAEKA--LREMDDQIRNIEKEL 399
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
126-259 6.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 126 RKEREVLQK-MAEITKEGFLLKQQL------IEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRTVKETAEQPE-REAKE 197
Cdd:COG4372 107 QEEAEELQEeLEELQKERQDLEQQRkqleaqIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054978 198 RHLKAWEEQKAAIRLVKDKAKMAEAFLELDDNADGLVSVSELQSHAELDSDTDGTLSEAEAK 259
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-403 7.27e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 118 ENTCKELGRKEREVLQKMAEITKegflLKQQL------IEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRT-------- 183
Cdd:COG4372  55 EQAREELEQLEEELEQARSELEQ----LEEELeelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqdleqq 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 184 ---VKETAEQPERE--AKERHLKAWEEQKAAIRlvkDKAKMAEAFLELDDNADGLVSVSELQSHAELDSDTDGTLSEAEA 258
Cdd:COG4372 131 rkqLEAQIAELQSEiaEREEELKELEEQLESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 259 KGLMGGVEQVDTATFESVWENIKDKY--HSESQPEEPAPVETPVDEVKEPVVDNESEPYPEDISEEEDEDDDDDDEYHEE 336
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLalSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054978 337 DEKAPPTMKTPEKSQEDEEAMPPYEADTQVLIEAAQKARDDFEEAEKALREMDDQIRNIEKELSFDF 403
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
PRK14144 PRK14144
heat shock protein GrpE; Provisional
348-400 8.91e-03

heat shock protein GrpE; Provisional


Pssm-ID: 184535 [Multi-domain]  Cd Length: 199  Bit Score: 37.78  E-value: 8.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41054978  348 EKSQEDEEAM--PPYEADTQVLIEAAQKARDDFEEAEKALREMDDQIRNIEKELS 400
Cdd:PRK14144  33 EESQHQEPALghPSYTALEEQLTLAEQKAHENWEKSVRALAELENVRRRMEREVA 87
 
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 ...
7-169 8.84e-43

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: 150.32  E-value: 8.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978     7 LLTLVFAVSLGTPVEVHRPRGVPLSKKPFYE--ENKPFTCLDGSKTIL-FDQVNDDYCDCKGGSDEPGTAACPNGKFHCT 83
Cdd:pfam12999   1 LLQPLLAISLLVAIALGKLRGVSPDNLHLYQpdENGNWKCLNHSEIKLsFDQVNDDYCDCPDGSDEPGTNACSNGKFYCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978    84 NAGYKPTFIPSSRINDGICD---CCDTTDEynSGAKCENTCKELGRKEREVLQKMAEITKEGFLLKQQLIEEAKKGRGEK 160
Cdd:pfam12999  81 NEGFIPGYIPSFKVDDGVCDydiCCDGSDE--ALGKCPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLLLAAQKKRDEL 158

                  ....*....
gi 41054978   161 QSKVTEMQD 169
Cdd:pfam12999 159 KKRLKELED 167
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
381-513 3.59e-17

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: 78.72  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   381 AEKALREMDDQIRNIEKELS-------FDFGPNAEFTYLYSQCYELSTSEYIYRLCPFNRVSQKpkfggsETNLGTWGSW 453
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQD------DISIGNFKKQ 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   454 sgpENNKylsMKYEHGTGCWQGPNRSTTVKLTCGKETMLTSTSEPSRCEYLMEFITPAVC 513
Cdd:pfam13015  75 ---EGNK---LYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAAC 128
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
414-472 1.33e-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: 60.25  E-value: 1.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054978   414 SQCYELSTSEYIYRLCPFNRVSQKPKF---GGSETNLGTWG--SWSG--------PENNKYLSMKYEHGTGC 472
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGqekGGSSFSLGRFSesSWAEstyddewtKGSNRYISMIYGNGTKC 72
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
145-219 6.18e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 6.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054978  145 LKQQLIEEAKKGRGEKQSKVTEM----QDNKKQLEEKVEAlrtvketAEQPEREAkERHLKAWEEQKAAIRLVKDKAKM 219
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNELiaslEELERELEQKAEE-------AEALLKEA-EKLKEELEEKKEKLQEEEDKLLE 569
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
126-218 3.03e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   126 RKEREVLQKMAEITKEgfllKQQliEEAKKGRGEKQ-SKVTEMQ--DNKKQL-----EEKVEALRTVKETAEQPEREAKE 197
Cdd:pfam15709 423 QQQEEFRRKLQELQRK----KQQ--EEAERAEAEKQrQKELEMQlaEEQKRLmemaeEERLEYQRQKQEAEEKARLEAEE 496
                          90       100
                  ....*....|....*....|.
gi 41054978   198 RHLKAweeqKAAIRLVKDKAK 218
Cdd:pfam15709 497 RRQKE----EEAARLALEEAM 513
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
125-222 4.79e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978  125 GRKEREVLQKMAEITKEGFLLKQQLIEEAKKGRGEKQsKVTEMQDNKKQLEEKVEALRTVKETAEQPEREAKERHLKAWE 204
Cdd:PRK09510  73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151
                         90
                 ....*....|....*...
gi 41054978  205 EQKAAirlvKDKAKMAEA 222
Cdd:PRK09510 152 EAKRA----AAAAKKAAA 165
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
217-262 4.96e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 4.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054978 217 AKMAEAFLELDDNADGLVSVSELQSH---------------AELDSDTDGTLSEAEAKGLM 262
Cdd:COG5126  69 PFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
PTZ00121 PTZ00121
MAEBL; Provisional
109-399 5.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   109 DEYNSGAKCENTCKELGRKEREV-----LQKMAEITKEGFLLKQQlIEEAKKGR--GEKQSKVTEMQDNKKQLEEKVEAl 181
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKkkadeAKKKAEEAKKADEAKKK-AEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKA- 1485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   182 RTVKETAEQPEREAKERHLKAWEEQKAAIRLVKDKAKMAEAFLELDD--NADGLVSVSELQSHAELDSDTDGTLSEAEAK 259
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   260 glmggVEQVDTATfesvweniKDKYHSESQPEEPAPVETPVDEVKEPVVDNESEPYPEDISEEEDEDDDDDDEYHEEDEK 339
Cdd:PTZ00121 1566 -----AEEAKKAE--------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054978   340 APPTMKTPEKSQEDEEAMPPYEADTQVLIEAAQKARDDFEEAEKA--LREMDDQIRNIEKEL 399
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
PTZ00121 PTZ00121
MAEBL; Provisional
123-259 6.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978   123 ELGRKEREVLQKMAEITKEGFLLKQQlIEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRTVKETAEQPEREAK------ 196
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaeek 1390
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054978   197 ---ERHLKAWEEQKAAIRLVKDKAKMAEAFLELDDNADGLVSVSELQSHAELDSDTDGTLSEAEAK 259
Cdd:PTZ00121 1391 kkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
126-259 6.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 126 RKEREVLQK-MAEITKEGFLLKQQL------IEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRTVKETAEQPE-REAKE 197
Cdd:COG4372 107 QEEAEELQEeLEELQKERQDLEQQRkqleaqIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054978 198 RHLKAWEEQKAAIRLVKDKAKMAEAFLELDDNADGLVSVSELQSHAELDSDTDGTLSEAEAK 259
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-403 7.27e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 7.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 118 ENTCKELGRKEREVLQKMAEITKegflLKQQL------IEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRT-------- 183
Cdd:COG4372  55 EQAREELEQLEEELEQARSELEQ----LEEELeelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqdleqq 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 184 ---VKETAEQPERE--AKERHLKAWEEQKAAIRlvkDKAKMAEAFLELDDNADGLVSVSELQSHAELDSDTDGTLSEAEA 258
Cdd:COG4372 131 rkqLEAQIAELQSEiaEREEELKELEEQLESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 259 KGLMGGVEQVDTATFESVWENIKDKY--HSESQPEEPAPVETPVDEVKEPVVDNESEPYPEDISEEEDEDDDDDDEYHEE 336
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLalSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054978 337 DEKAPPTMKTPEKSQEDEEAMPPYEADTQVLIEAAQKARDDFEEAEKALREMDDQIRNIEKELSFDF 403
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
126-221 8.29e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054978 126 RKEREVLQKMAEITKEGFLLKQQLIEEAKKGRGEKQSKVTEMQDNKKQLEEKVEALRTVKETAEQpEREAKERHLKAWEe 205
Cdd:COG4717  52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE-ELEKLEKLLQLLP- 129
                        90
                ....*....|....*.
gi 41054978 206 qkAAIRLVKDKAKMAE 221
Cdd:COG4717 130 --LYQELEALEAELAE 143
PRK14144 PRK14144
heat shock protein GrpE; Provisional
348-400 8.91e-03

heat shock protein GrpE; Provisional


Pssm-ID: 184535 [Multi-domain]  Cd Length: 199  Bit Score: 37.78  E-value: 8.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41054978  348 EKSQEDEEAM--PPYEADTQVLIEAAQKARDDFEEAEKALREMDDQIRNIEKELS 400
Cdd:PRK14144  33 EESQHQEPALghPSYTALEEQLTLAEQKAHENWEKSVRALAELENVRRRMEREVA 87
 
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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