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Conserved domains on  [gi|1907195639|ref|XP_036010596|]
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glucosidase 2 subunit beta isoform X2 [Mus musculus]

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 ...
 21-163 5.80e-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: 142.62  E-value: 5.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  21 RGVSLSNHHFYEESK--PFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYQPDEngNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195639  98 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 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 ...
 373-501 4.23e-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: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 373 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 445
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639 446 AGpdhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 501
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 4.34e-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: 46.32  E-value: 4.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195639 198 WEEQQAAAKARREQ---ERAASAFQELDDNMDGMVSLAELQTH---------------PELDTDGDGALSEEEAQALL 257
Cdd:COG5126    52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
PLN02316 super family cl33462
synthase/transferase
 169-214 7.34e-03

synthase/transferase


The actual alignment was detected with superfamily member PLN02316:

Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.08  E-value: 7.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907195639  169 LEDQVETLRAAKEEAERpEKEAKDQHRKlwEEQQAAAKARREQERA 214
Cdd:PLN02316   252 EEKRRELEKLAKEEAER-ERQAEEQRRR--EEEKAAMEADRAQAKA 294
 
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 5.80e-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: 142.62  E-value: 5.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  21 RGVSLSNHHFYEESK--PFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYQPDEngNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195639  98 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 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 ...
 373-501 4.23e-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: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 373 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 445
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639 446 AGpdhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 501
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 4.34e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 4.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195639 198 WEEQQAAAKARREQ---ERAASAFQELDDNMDGMVSLAELQTH---------------PELDTDGDGALSEEEAQALL 257
Cdd:COG5126    52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-220 2.83e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 118 EKGRKEKESLQQLAEvTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKL 197
Cdd:COG1196   285 EAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100
                  ....*....|....*....|...
gi 1907195639 198 WEEQQAAAKARREQERAASAFQE 220
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAE 386
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 114-256 2.77e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 41.83  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 114 NTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLelQAGKKSLEDQVETLRAAKEEAERPEKEAKdq 193
Cdd:PRK14473   35 NLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVA--QAQERARAQEAEIIAQARREAEKIKEEAR-- 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195639 194 hrklweeqqaaakARREQERaASAFQELDDNMDGMVSL-AELQTHPELDTDGDGALSEEEAQAL 256
Cdd:PRK14473  111 -------------AQAEQER-QRMLSELKSQIADLVTLtASRVLGAELQARGHDALIAESLAAL 160
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 117-285 3.17e-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: 42.91  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKE----SLQQLAEVTR--EGFRLKKILIEEWKTAREEKQSKLLElQAGKKSLEDQVETLRAAKEEAERPEK-- 188
Cdd:TIGR02794 112 KQAEEKQKQaeeaKAKQAAEAKAkaEAEAERKAKEEAAKQAEEEAKAKAAA-EAKKKAEEAKKKAEAEAKAKAEAEAKak 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 189 ----EAKDQHRKLWEEQQAAAKARREQERAASAFQElddnmdgmvslaelQTHPELDTDGDGALSEEEAQALLSGDTQTD 264
Cdd:TIGR02794 191 aeeaKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAA 256

                         170       180
                  ....*....|....*....|.
gi 1907195639 265 TTSFYDRVWAAIRDKYRSEVP 285
Cdd:TIGR02794 257 AGSEVDKYAAIIQQAIQQNLY 277
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-270 1.32e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.43  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195639 214 AASAFQELDDNMDGMVSLAEL----------QTHPE-----------LDTDGDGALSEEEAQALLSGD-TQTDTTSFYD 270
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELaaaappppppPDQAPsteladdllsaLDTDGDGSISSDELSAGLTSAgSSADSSQLFS 143
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-282 2.58e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 214 AASAFQELDDNMDGMVSLAELQTHP--------------ELDTDGDGALSEEEAQALL---------------------- 257
Cdd:NF041410  105 ADDLLSALDTDGDGSISSDELSAGLtsagssadssqlfsALDSDGDGSVSSDELAAALqpppppplfslssqgsssstqp 184

                          90       100
                  ....*....|....*....|....*....
gi 1907195639 258 ----SGDTQTDTTSFYDRVWAAIRDKYRS 282
Cdd:NF041410  185 sdssTASSSSNTTEALNKLIANLSKQYQS 213
PLN02316 PLN02316
synthase/transferase
 169-214 7.34e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.08  E-value: 7.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907195639  169 LEDQVETLRAAKEEAERpEKEAKDQHRKlwEEQQAAAKARREQERA 214
Cdd:PLN02316   252 EEKRRELEKLAKEEAER-ERQAEEQRRR--EEEKAAMEADRAQAKA 294
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 ...
 139-222 9.10e-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: 36.52  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 139 RLKKILieewKTAREEKQSKLLELQAGKKS----LEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQeRA 214
Cdd:pfam00430  23 PLGKVL----DKRRELIADEIAEAEERRKDaaaaLAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAER-II 97


                  ....*...
gi 1907195639 215 ASAFQELD 222
Cdd:pfam00430  98 EQAAAEIE 105
 
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 5.80e-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: 142.62  E-value: 5.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  21 RGVSLSNHHFYEESK--PFTCL-DGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYQPDEngNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195639  98 D---CCDGTDEynSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQ 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 ...
 373-501 4.23e-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: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 373 VERSLKEMEESIRSLEQEIS-------FDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPkhggspTSLGTWGSW 445
Cdd:pfam13015   1 LQMSIDEHEKDIKKIESDITileenlnSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639 446 AGpdhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMT 501
Cdd:pfam13015  75 EG------NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKS 124
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 406-464 3.83e-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: 56.01  E-value: 3.83e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907195639 406 SQCYELTTNEYVYRLCPFKLVSQKPK---HGGSPTSLGTWG--SWAGPDHDK--------FSAMKYEQGTGC 464
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKgqeKGGSSFSLGRFSesSWAESTYDDewtkgsnrYISMIYGNGTKC 72
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 4.34e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 4.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195639 198 WEEQQAAAKARREQ---ERAASAFQELDDNMDGMVSLAELQTH---------------PELDTDGDGALSEEEAQALL 257
Cdd:COG5126    52 REEFVAGMESLFEAtvePFARAAFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-220 2.83e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 118 EKGRKEKESLQQLAEvTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKL 197
Cdd:COG1196   285 EAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100
                  ....*....|....*....|...
gi 1907195639 198 WEEQQAAAKARREQERAASAFQE 220
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAE 386
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 125-217 4.17e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 125 ESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAA 204
Cdd:COG3883   122 SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                          90
                  ....*....|...
gi 1907195639 205 AKARREQERAASA 217
Cdd:COG3883   202 EAELAAAEAAAAA 214
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-256 7.15e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 7.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  121 RKEKESLQQLAEVTREgfrlkkilIEEWKTAREEkqskLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEE 200
Cdd:COG4913    644 QERREALQRLAEYSWD--------EIDVASAERE----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL 711

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639  201 QQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQAL 256
Cdd:COG4913    712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 144-220 9.43e-05

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: 9.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907195639 144 LIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQE 220
Cdd:COG3883   134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 114-256 2.77e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 41.83  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 114 NTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLelQAGKKSLEDQVETLRAAKEEAERPEKEAKdq 193
Cdd:PRK14473   35 NLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVA--QAQERARAQEAEIIAQARREAEKIKEEAR-- 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907195639 194 hrklweeqqaaakARREQERaASAFQELDDNMDGMVSL-AELQTHPELDTDGDGALSEEEAQAL 256
Cdd:PRK14473  111 -------------AQAEQER-QRMLSELKSQIADLVTLtASRVLGAELQARGHDALIAESLAAL 160
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 117-285 3.17e-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: 42.91  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKE----SLQQLAEVTR--EGFRLKKILIEEWKTAREEKQSKLLElQAGKKSLEDQVETLRAAKEEAERPEK-- 188
Cdd:TIGR02794 112 KQAEEKQKQaeeaKAKQAAEAKAkaEAEAERKAKEEAAKQAEEEAKAKAAA-EAKKKAEEAKKKAEAEAKAKAEAEAKak 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 189 ----EAKDQHRKLWEEQQAAAKARREQERAASAFQElddnmdgmvslaelQTHPELDTDGDGALSEEEAQALLSGDTQTD 264
Cdd:TIGR02794 191 aeeaKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAA 256

                         170       180
                  ....*....|....*....|.
gi 1907195639 265 TTSFYDRVWAAIRDKYRSEVP 285
Cdd:TIGR02794 257 AGSEVDKYAAIIQQAIQQNLY 277
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-281 4.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  118 EKGRKEKESLQQLAEVTREgFRLKKILIEEWK------------TAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAER 185
Cdd:COG4913    245 EDAREQIELLEPIRELAER-YAAARERLAELEylraalrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  186 PEKEAKDQHRKL-------WEEQQAAAKARREQ-ERAASAFQELddnmdgmvsLAELQTHPELDTDGDGALSEEEAQALL 257
Cdd:COG4913    324 ELDELEAQIRGNggdrleqLEREIERLERELEErERRRARLEAL---------LAALGLPLPASAEEFAALRAEAAALLE 394

                          170       180
                   ....*....|....*....|....
gi 1907195639  258 SGDTQTDTTSfyDRVWAAIRDKYR 281
Cdd:COG4913    395 ALEEELEALE--EALAEAEAALRD 416
fliH PRK06800
flagellar assembly protein H; Validated
 130-268 5.51e-04

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 41.40  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 130 LAEVTREGFRLKKILIEEwktaREEKQSKLLELQAGKKSLEDQVETLRAAKEEAER------PEKEAKDQHRKLWEEQQA 203
Cdd:PRK06800   15 FSEETYELQFPKPIEVEV----EEEIQKDHEELLAQQKSLHKELNQLRQEQQKLERerqqllADREQFQEHVQQQMKEIE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907195639 204 AAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTdgdgalSEEEAQALLSGDTQTDTTSF 268
Cdd:PRK06800   91 AARQQFQKEQQETAYEWTELLWDQSFQLAEKIVNQAVDT------RLLDVLPILTGIVQTLPTSF 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-226 6.20e-04

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: 42.74  E-value: 6.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  112 CENTCREKGRKEKESLQQLAEVTREgfrlkkilIEEWKTAREEKQ-------SKLLELQAGKKSLEDQVETLRAAKEEAE 184
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQ--------LEELESKLDELAeelaeleEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907195639  185 RPEKEAKDQH----RKLWEEQQAAAKARREQERAASAFQELDDNMD 226
Cdd:TIGR02168  372 SRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 118-222 6.52e-04

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: 42.75  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639  118 EKGRKEKESLQQLAEVTREGFRLKkilIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKL 197
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908

                           90       100
                   ....*....|....*....|....*.
gi 1907195639  198 -WEEQQAAAKARREQERAASAFQELD 222
Cdd:TIGR02169  909 eAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-223 1.28e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKE-EAERPEKEAKDQHR 195
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEE 320

                          90       100
                  ....*....|....*....|....*...
gi 1907195639 196 KLWEEQQAAAKARREQERAASAFQELDD 223
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEE 348
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-270 1.32e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.43  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907195639 214 AASAFQELDDNMDGMVSLAEL----------QTHPE-----------LDTDGDGALSEEEAQALLSGD-TQTDTTSFYD 270
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELaaaappppppPDQAPsteladdllsaLDTDGDGSISSDELSAGLTSAgSSADSSQLFS 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 123-213 1.76e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 123 EKESLQQLAEVTREGFRLKKILI----EEWKTARE----EKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQH 194
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAIKKEALleakEEIHKLRNefekELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116

                          90
                  ....*....|....*....
gi 1907195639 195 RKLWEEQQAAAKARREQER 213
Cdd:PRK12704  117 KELEQKQQELEKKEEELEE 135
PRK11637 PRK11637
AmiB activator; Provisional
 118-214 1.80e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 118 EKGRKEKESL--QQLAEVTREGFRL--KKILiEEWKTAREEKQSKLLELQAGKKSLEDQVEtlRAAKEEAERPEKEAKDQ 193
Cdd:PRK11637  191 EKQSQQKTLLyeQQAQQQKLEQARNerKKTL-TGLESSLQKDQQQLSELRANESRLRDSIA--RAEREAKARAEREAREA 267

                          90       100
                  ....*....|....*....|....*
gi 1907195639 194 HRKLWEEQQAAAKARR----EQERA 214
Cdd:PRK11637  268 ARVRDKQKQAKRKGSTykptESERS 292
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 145-221 2.07e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.00  E-value: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195639 145 IEEWKTAREEKQSKLLELQAGKKSLEDQVETLRA-AKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAAsAFQEL 221
Cdd:COG0711    40 LAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAeARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAK-ALAEL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-257 2.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKILiEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRK 196
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEEL-EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907195639 197 LWEEQQAAA--KARREQERAASAFQELDDNmdgmvsLAELQTHPELDTDGDGALSEEEAQALL 257
Cdd:COG1196   405 LEEAEEALLerLERLEEELEELEEALAELE------EEEEEEEEALEEAAEEEAELEEEEEAL 461
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-233 2.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKI------LIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEA 190
Cdd:PRK02224  491 VEEVEERLERAEDLVEAEDRIERLEERredleeLIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907195639 191 KDQHRKLwEEQQAAAKARREQ-ERAASAFQELDDNMDGMVSLAE 233
Cdd:PRK02224  571 REEVAEL-NSKLAELKERIESlERIRTLLAAIADAEDEIERLRE 613
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
214-282 2.58e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 214 AASAFQELDDNMDGMVSLAELQTHP--------------ELDTDGDGALSEEEAQALL---------------------- 257
Cdd:NF041410  105 ADDLLSALDTDGDGSISSDELSAGLtsagssadssqlfsALDSDGDGSVSSDELAAALqpppppplfslssqgsssstqp 184

                          90       100
                  ....*....|....*....|....*....
gi 1907195639 258 ----SGDTQTDTTSFYDRVWAAIRDKYRS 282
Cdd:NF041410  185 sdssTASSSSNTTEALNKLIANLSKQYQS 213
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 117-243 2.59e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 40.22  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQqlaevTREGFRLKKILI-----EEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEak 191
Cdd:PRK00247  295 REKQKEKKAFLW-----TLRRNRLRMIITpwrapELHAENAEIKKTRTAEKNEAKARKKEIAQKRRAAEREINREARQ-- 367

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639 192 dqhrklwEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTH----PELDTD 243
Cdd:PRK00247  368 -------ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESkgspPQVEAT 416
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
122-223 3.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 122 KEKESLQQLAEVTREG-FRLKKI------LIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQH 194
Cdd:COG4372    21 KTGILIAALSEQLRKAlFELDKLqeeleqLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                          90       100
                  ....*....|....*....|....*....
gi 1907195639 195 RKLWEEQQAAAKARREQERAASAFQELDD 223
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQ 129
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 127-235 3.57e-03

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: 39.75  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 127 LQQLAEVTREgfrlkkiLIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAK 206
Cdd:COG4942   141 LKYLAPARRE-------QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                          90       100
                  ....*....|....*....|....*....
gi 1907195639 207 ARREQERAAsafQELDDNMDGMVSLAELQ 235
Cdd:COG4942   214 ELAELQQEA---EELEALIARLEAEAAAA 239
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-236 4.64e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKILIE------EWKTAREE-------------KQSKLLELQAGKKSLEDQVETLR 177
Cdd:COG4717    97 LEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAElaelperleeleeRLEELRELEEELEELEAELAELQ 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907195639 178 AAKEEAERPE--------KEAKDQHRKLWEEQQAAAKARRE-QERAASAFQELDDNMDGMVSLAELQT 236
Cdd:COG4717   177 EELEELLEQLslateeelQDLAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAALEER 244
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 139-220 6.90e-03

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: 38.67  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 139 RLKKILIEewktAREEKQSKLLElQAGKKSLEDQVetlrAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAF 218
Cdd:TIGR02794  69 RQKKLEQQ----AEEAEKQRAAE-QARQKELEQRA----AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE 139


                  ..
gi 1907195639 219 QE 220
Cdd:TIGR02794 140 AE 141
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-216 7.30e-03

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: 38.59  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKILiEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRK 196
Cdd:COG4942   149 REQAEELRADLAELAALRAELEAERAEL-EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                          90       100
                  ....*....|....*....|
gi 1907195639 197 LWEEQQAAAKARREQERAAS 216
Cdd:COG4942   228 LIARLEAEAAAAAERTPAAG 247
PLN02316 PLN02316
synthase/transferase
 169-214 7.34e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.08  E-value: 7.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907195639  169 LEDQVETLRAAKEEAERpEKEAKDQHRKlwEEQQAAAKARREQERA 214
Cdd:PLN02316   252 EEKRRELEKLAKEEAER-ERQAEEQRRR--EEEKAAMEADRAQAKA 294
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 117-261 7.86e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAE--VTREGFRLKKILIEEWKTAreEKQSKLLELQAGKksLEDQVETLRAAKEEAERPEKEAKDQH 194
Cdd:pfam04012  59 LEQQTEQAKKLEEKAQaaLTKGNEELAREALAEKKSL--EKQAEALETQLAQ--QRSAVEQLRKQLAALETKIQQLKAKK 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907195639 195 RKLwEEQQAAAKARREQER---------AASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDT 261
Cdd:pfam04012 135 NLL-KARLKAAKAQEAVQTslgslstssATDSFERIEEKIEEREARADAAAELASAVDLDAKLEQAGIQMEVSEDV 209
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
117-214 8.61e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLL-ELQAGKKSLEDQVET-LRAAKEEAERPEKEAKDQH 194
Cdd:COG3064     5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEaKRQAEEEAREAKAEAeQRAAELAAEAAKKLAEAEK 84

                          90       100
                  ....*....|....*....|
gi 1907195639 195 RKLWEEQQAAAKARREQERA 214
Cdd:COG3064    85 AAAEAEKKAAAEKAKAAKEA 104
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 ...
 139-222 9.10e-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: 36.52  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 139 RLKKILieewKTAREEKQSKLLELQAGKKS----LEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQeRA 214
Cdd:pfam00430  23 PLGKVL----DKRRELIADEIAEAEERRKDaaaaLAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAER-II 97


                  ....*...
gi 1907195639 215 ASAFQELD 222
Cdd:pfam00430  98 EQAAAEIE 105
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 117-215 9.34e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907195639 117 REKGRKEKESLQQLAEVTREgfrlkkiliEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAE---RPEKEAKDQ 193
Cdd:pfam13868  35 KAEEKEEERRLDEMMEEERE---------RALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYeekLQEREQMDE 105

                          90       100
                  ....*....|....*....|...
gi 1907195639 194 H-RKLWEEQQAAAKARREQERAA 215
Cdd:pfam13868 106 IvERIQEEDQAEAEEKLEKQRQL 128
 
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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