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Conserved domains on  [gi|157818781|ref|NP_001100276|]
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glucosidase 2 subunit beta precursor [Rattus norvegicus]

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 ...
 20-162 2.58e-40

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: 143.78  E-value: 2.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781   20 RGVSLSNHHFY--DESKPFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 96
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818781   97 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 162
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 ...
 377-505 3.62e-14

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: 69.86  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  377 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 449
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818781  450 AGpdddkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 505
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
197-256 9.73e-06

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: 45.17  E-value: 9.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818781 197 WEEQQAAAKARREQ---ELAASAFQELDDNMDGLVSLAELQTH---------------PELDTDGDGGLSEEEAQALL 256
Cdd:COG5126   52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
 
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 ...
 20-162 2.58e-40

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: 143.78  E-value: 2.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781   20 RGVSLSNHHFY--DESKPFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 96
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818781   97 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 162
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 ...
 377-505 3.62e-14

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: 69.86  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  377 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 449
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818781  450 AGpdddkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 505
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
197-256 9.73e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 9.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818781 197 WEEQQAAAKARREQ---ELAASAFQELDDNMDGLVSLAELQTH---------------PELDTDGDGGLSEEEAQALL 256
Cdd:COG5126   52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 143-219 1.02e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818781 143 LIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQELAASAFQE 219
Cdd:COG3883  134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
211-281 1.33e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 211 ELAASAFQELDDNMDGLVSLAELQT--------------HPELDTDGDGGLSEEEAQALL-------------------- 256
Cdd:NF041410 103 ELADDLLSALDTDGDGSISSDELSAgltsagssadssqlFSALDSDGDGSVSSDELAAALqpppppplfslssqgsssst 182

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157818781 257 ------SGDTQTDTTSFYDRVWAAIRDKYRS 281
Cdd:NF041410 183 qpsdssTASSSSNTTEALNKLIANLSKQYQS 213
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 116-284 1.58e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  116 REKGRKEKE----SLQQLAEVTR--EGFRLKKILIEEWKTAREEKQSKLLElQAGKKSLED--QVETLRTAKEEAER--- 184
Cdd:TIGR02794 112 KQAEEKQKQaeeaKAKQAAEAKAkaEAEAERKAKEEAAKQAEEEAKAKAAA-EAKKKAEEAkkKAEAEAKAKAEAEAkak 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  185 -PEKEAKDQHRKLWEEQQAAAKARREQELAASAFQElddnmdglvslaelQTHPELDTDGDGGLSEEEAQALLSGDTQTD 263
Cdd:TIGR02794 191 aEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAA 256

                         170       180
                  ....*....|....*....|.
gi 157818781  264 TTSFYDRVWAAIRDKYRSEVP 284
Cdd:TIGR02794 257 AGSEVDKYAAIIQQAIQQNLY 277
PRK12704 PRK12704
phosphodiesterase; Provisional
 122-256 5.40e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 122 EKESLQQLAEVTREGFRLKKILI----EEWKTARE----EKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQH 193
Cdd:PRK12704  37 EEEAKRILEEAKKEAEAIKKEALleakEEIHKLRNefekELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818781 194 RKLWEEQQAAAKARRE-QELAASAFQELDdnmdglvSLAelqthpeldtdgdgGLSEEEAQALL 256
Cdd:PRK12704 117 KELEQKQQELEKKEEElEELIEEQLQELE-------RIS--------------GLTAEEAKEIL 159
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 36-63 7.20e-03

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 34.15  E-value: 7.20e-03
                           10        20
                   ....*....|....*....|....*...
gi 157818781    36 FTCLDGTaTIPFDQVNDDYCDCKDGSDE 63
Cdd:smart00192   7 FQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
 
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 ...
 20-162 2.58e-40

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: 143.78  E-value: 2.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781   20 RGVSLSNHHFY--DESKPFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 96
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818781   97 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 162
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 ...
 377-505 3.62e-14

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: 69.86  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  377 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 449
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818781  450 AGpdddkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 505
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 410-468 1.79e-10

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: 56.78  E-value: 1.79e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818781  410 SQCYELTTNEYVYRLCPFKLVSQKPK---HGGSPTSLGTWG--SWAGPDDDK--------FSAMKYEQGTGC 468
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKgqeKGGSSFSLGRFSesSWAESTYDDewtkgsnrYISMIYGNGTKC 72
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
197-256 9.73e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 9.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818781 197 WEEQQAAAKARREQ---ELAASAFQELDDNMDGLVSLAELQTH---------------PELDTDGDGGLSEEEAQALL 256
Cdd:COG5126   52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 143-219 1.02e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818781 143 LIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQELAASAFQE 219
Cdd:COG3883  134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-257 1.10e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 117 EKGRKEKESLQQLAEvTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKL 196
Cdd:COG1196  285 EAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818781 197 WEEQQAAAKARREQELAASAF-QELDDNMDGLVSLAELQTHPELDTDGDGGLSEEEAQALLS 257
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
211-281 1.33e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 211 ELAASAFQELDDNMDGLVSLAELQT--------------HPELDTDGDGGLSEEEAQALL-------------------- 256
Cdd:NF041410 103 ELADDLLSALDTDGDGSISSDELSAgltsagssadssqlFSALDSDGDGSVSSDELAAALqpppppplfslssqgsssst 182

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157818781 257 ------SGDTQTDTTSFYDRVWAAIRDKYRS 281
Cdd:NF041410 183 qpsdssTASSSSNTTEALNKLIANLSKQYQS 213
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 116-284 1.58e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  116 REKGRKEKE----SLQQLAEVTR--EGFRLKKILIEEWKTAREEKQSKLLElQAGKKSLED--QVETLRTAKEEAER--- 184
Cdd:TIGR02794 112 KQAEEKQKQaeeaKAKQAAEAKAkaEAEAERKAKEEAAKQAEEEAKAKAAA-EAKKKAEEAkkKAEAEAKAKAEAEAkak 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  185 -PEKEAKDQHRKLWEEQQAAAKARREQELAASAFQElddnmdglvslaelQTHPELDTDGDGGLSEEEAQALLSGDTQTD 263
Cdd:TIGR02794 191 aEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAA 256

                         170       180
                  ....*....|....*....|.
gi 157818781  264 TTSFYDRVWAAIRDKYRSEVP 284
Cdd:TIGR02794 257 AGSEVDKYAAIIQQAIQQNLY 277
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 124-216 1.58e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 124 ESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAA 203
Cdd:COG3883  122 SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                         90
                 ....*....|...
gi 157818781 204 AKARREQELAASA 216
Cdd:COG3883  202 EAELAAAEAAAAA 214
PRK12704 PRK12704
phosphodiesterase; Provisional
 122-256 5.40e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 122 EKESLQQLAEVTREGFRLKKILI----EEWKTARE----EKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQH 193
Cdd:PRK12704  37 EEEAKRILEEAKKEAEAIKKEALleakEEIHKLRNefekELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818781 194 RKLWEEQQAAAKARRE-QELAASAFQELDdnmdglvSLAelqthpeldtdgdgGLSEEEAQALL 256
Cdd:PRK12704 117 KELEQKQQELEKKEEElEELIEEQLQELE-------RIS--------------GLTAEEAKEIL 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 126-234 6.62e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 126 LQQLAEVTREgfrlkkiLIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLweEQQAAAK 205
Cdd:COG4942  141 LKYLAPARRE-------QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL--EKELAEL 211

                         90       100
                 ....*....|....*....|....*....
gi 157818781 206 ARREQELAASAfQELDDNMDGLVSLAELQ 234
Cdd:COG4942  212 AAELAELQQEA-EELEALIARLEAEAAAA 239
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-240 7.77e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  120 RKEKESLQQLAEVTREgfrlkkilIEEWKTAREEkqskLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEE 199
Cdd:COG4913   644 QERREALQRLAEYSWD--------EIDVASAERE----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL 711

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 157818781  200 QQAAAKARREQELAASAFQELDDNMDGLVSLAELQTHPELD 240
Cdd:COG4913   712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 138-216 8.88e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  138 RLKKILI--EEWKTAREEKQSKLLELQAGKKSLED--QVETLRTAKEEAERPEKEAKDQHRKlweEQQAAAKARREQELA 213
Cdd:TIGR02794  69 RQKKLEQqaEEAEKQRAAEQARQKELEQRAAAEKAakQAEQAAKQAEEKQKQAEEAKAKQAA---EAKAKAEAEAERKAK 145


                  ...
gi 157818781  214 ASA 216
Cdd:TIGR02794 146 EEA 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-222 1.43e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781   111 CENTCREKGRKEKESLQQLAEVTREgfrlkkilIEEWKTAREEKQ-------SKLLELQAGKKSLEDQVETLRTAKEEAE 183
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQ--------LEELESKLDELAeelaeleEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 157818781   184 RPEKEAKDQHRKLweeQQAAAKARREQELAASAFQELDD 222
Cdd:TIGR02168  372 SRLEELEEQLETL---RSKVAQLELQIASLNNEIERLEA 407
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 113-255 2.12e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 39.14  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 113 NTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLleLQAGKKSLEDQVETLRTAKEEAERPEKEAKDQ 192
Cdd:PRK14473  35 NLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIV--AQAQERARAQEAEIIAQARREAEKIKEEARAQ 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818781 193 hrklweeqqaaAKARREQELAasafqELDDNMDGLVSL-AELQTHPELDTDGDGGLSEEEAQAL 255
Cdd:PRK14473 113 -----------AEQERQRMLS-----ELKSQIADLVTLtASRVLGAELQARGHDALIAESLAAL 160
fliH PRK06800
flagellar assembly protein H; Validated
 129-267 2.36e-03

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 39.86  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 129 LAEVTREGFRLKKILIEEwktaREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERP------EKEAKDQHRKLWEEQQA 202
Cdd:PRK06800  15 FSEETYELQFPKPIEVEV----EEEIQKDHEELLAQQKSLHKELNQLRQEQQKLERErqqllaDREQFQEHVQQQMKEIE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157818781 203 AAKARREQELAASAFQELDDNMDGLVSLAELQTHPELDTdgdgglSEEEAQALLSGDTQTDTTSF 267
Cdd:PRK06800  91 AARQQFQKEQQETAYEWTELLWDQSFQLAEKIVNQAVDT------RLLDVLPILTGIVQTLPTSF 149
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 117-221 5.10e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781   117 EKGRKEKESLQQLAEVTREGFRLKkilIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKL 196
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908

                           90       100
                   ....*....|....*....|....*.
gi 157818781   197 -WEEQQAAAKARREQELAASAFQELD 221
Cdd:TIGR02169  909 eAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-257 5.13e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 116 REKGRKEKESLQQLAEVTREGFRLKKILiEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRK 195
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEEL-EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818781 196 LWEEQQAAA--KARREQELAASAFQELDDnmdgLVSLAELQTHPELDTDGDGGLSEEEAQALLS 257
Cdd:COG1196  405 LEEAEEALLerLERLEEELEELEEALAEL----EEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 138-221 5.63e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 37.29  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  138 RLKKILieewKTAREEKQSKLLELQAGKKS----LEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQeLA 213
Cdd:pfam00430  23 PLGKVL----DKRRELIADEIAEAEERRKDaaaaLAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAER-II 97


                  ....*...
gi 157818781  214 ASAFQELD 221
Cdd:pfam00430  98 EQAAAEIE 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-254 6.95e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  117 EKGRKEKESLQQLAEVTREgFRLKKILIEEWK------------TAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAER 184
Cdd:COG4913   245 EDAREQIELLEPIRELAER-YAAARERLAELEylraalrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781  185 PEKEAKDQHRKL-------WEEQQAAAKARRE---------QELAASAFQELDDNMDGLVSL-AELQTHPELDTDGDGGL 247
Cdd:COG4913   324 ELDELEAQIRGNggdrleqLEREIERLERELEererrrarlEALLAALGLPLPASAEEFAALrAEAAALLEALEEELEAL 403


                  ....*..
gi 157818781  248 SEEEAQA 254
Cdd:COG4913   404 EEALAEA 410
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 36-63 7.20e-03

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 34.15  E-value: 7.20e-03
                           10        20
                   ....*....|....*....|....*...
gi 157818781    36 FTCLDGTaTIPFDQVNDDYCDCKDGSDE 63
Cdd:smart00192   7 FQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-238 8.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818781 116 REKGRKEKESLQQLAEVTREGFRLKKILIE------EWKTAREE-------------KQSKLLELQAGKKSLEDQVETLR 176
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAElaelperleeleeRLEELRELEEELEELEAELAELQ 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818781 177 TAKEEAERPEKEAKDQH-RKLWEE----QQAAAKARREQELAASAFQELDDNMDGLVSLAELQTHPE 238
Cdd:COG4717  177 EELEELLEQLSLATEEElQDLAEEleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
 
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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