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Conserved domains on  [gi|48255889|ref|NP_002734|]
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glucosidase 2 subunit beta isoform 1 precursor [Homo sapiens]

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 4.92e-45

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: 156.49  E-value: 4.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889    21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48255889    98 D---CCDGTDEynSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQ 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 ...
 376-507 1.08e-13

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: 68.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   376 KFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSWIGp 455
Cdd:pfam13015   4 SIDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQEG- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 48255889   456 dhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELM 507
Cdd:pfam13015  77 -----NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVK 123
XopAW super family cl49407
XopAW family type III secretion system calcium-binding effector;
199-293 5.79e-06

XopAW family type III secretion system calcium-binding effector;


The actual alignment was detected with superfamily member NF041410:

Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 47.75  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  199 EEQLAAAKAQ--------QEQELAADAFKELDDDMDGTVSVTELQTHP--------------ELDTDGDGALSEAEAQAL 256
Cdd:NF041410  82 SDELAAAAPPpppppdqaPSTELADDLLSALDTDGDGSISSDELSAGLtsagssadssqlfsALDSDGDGSVSSDELAAA 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48255889  257 L--------------------------SGDTQTDATSFYDRVWAAIRDKYRSealpTDLPAPS 293
Cdd:NF041410 162 LqpppppplfslssqgsssstqpsdssTASSSSNTTEALNKLIANLSKQYQS----LDNSASV 220
 
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 4.92e-45

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: 156.49  E-value: 4.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889    21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48255889    98 D---CCDGTDEynSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQ 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 ...
 376-507 1.08e-13

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: 68.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   376 KFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSWIGp 455
Cdd:pfam13015   4 SIDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQEG- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 48255889   456 dhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELM 507
Cdd:pfam13015  77 -----NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVK 123
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
199-293 5.79e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 47.75  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  199 EEQLAAAKAQ--------QEQELAADAFKELDDDMDGTVSVTELQTHP--------------ELDTDGDGALSEAEAQAL 256
Cdd:NF041410  82 SDELAAAAPPpppppdqaPSTELADDLLSALDTDGDGSISSDELSAGLtsagssadssqlfsALDSDGDGSVSSDELAAA 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48255889  257 L--------------------------SGDTQTDATSFYDRVWAAIRDKYRSealpTDLPAPS 293
Cdd:NF041410 162 LqpppppplfslssqgsssstqpsdssTASSSSNTTEALNKLIANLSKQYQS----LDNSASV 220
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 5.46e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 5.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48255889 198 WEEQLAAAKAQQEQELAADA---FKELDDDMDGTVSVTELQTH---------------PELDTDGDGALSEAEAQALL 257
Cdd:COG5126  52 REEFVAGMESLFEATVEPFAraaFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-220 5.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 117 KEKGRKERESLQQMAEvTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQK 196
Cdd:COG1196 284 EEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                        90       100
                ....*....|....*....|....
gi 48255889 197 LWEEQLAAAKAQQEQELAADAFKE 220
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAE 386
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
203-256 5.65e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 44.67  E-value: 5.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48255889  203 AAAKAQQEQELAADAFKELDDDMDGTVSVTELQTH-----------------PELDTDGDGALSEAE-AQAL 256
Cdd:NF041410  18 SSTSSARSQQFQKQLFAKLDSDGDGSVSQDELSSAlssksddgslidlselfSDLDSDGDGSLSSDElAAAA 89
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 118-279 2.83e-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: 43.30  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   118 EKGRKERESLQQMAEVTREgfrlkKILIEDWKKAREEKQKKLIELQAGKKSLED--QVEMLRTVKEEAEK----PEREAK 191
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAE-----RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAkkKAEAEAKAKAEAEAkakaEEAKAK 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   192 EQHQKLWEEQLAAAKAQQEQELAADAFKEldddmdgtvsvtelQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDR 271
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263


                  ....*...
gi 48255889   272 VWAAIRDK 279
Cdd:TIGR02794 264 YAAIIQQA 271
PRK12704 PRK12704
phosphodiesterase; Provisional
 118-213 1.25e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  118 EKGRKERESLQQMA--EVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQ 195
Cdd:PRK12704  45 EEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124

                         90       100
                 ....*....|....*....|
gi 48255889  196 KL--WEEQLAAAKAQQEQEL 213
Cdd:PRK12704 125 ELekKEEELEELIEEQLQEL 144
fliH PRK06800
flagellar assembly protein H; Validated
 130-268 5.42e-03

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 38.70  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  130 MAEVTREGFRLKKILIEdwkkAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAE------KPEREAKEQHQKLWEEQLA 203
Cdd:PRK06800  15 FSEETYELQFPKPIEVE----VEEEIQKDHEELLAQQKSLHKELNQLRQEQQKLErerqqlLADREQFQEHVQQQMKEIE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48255889  204 AAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTdgdgalSEAEAQALLSGDTQTDATSF 268
Cdd:PRK06800  91 AARQQFQKEQQETAYEWTELLWDQSFQLAEKIVNQAVDT------RLLDVLPILTGIVQTLPTSF 149
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 139-225 6.92e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 6.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 139 RLKKIL--IEDWKKAREEKQKKLIELQagkksledqvEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELA-- 214
Cdd:cd06503  31 REEKIAesLEEAEKAKEEAEELLAEYE----------EKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEqa 100

                        90
                ....*....|....*....
gi 48255889 215 --------ADAFKELDDDM 225
Cdd:cd06503 101 kaeieqekEKALAELRKEV 119
 
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 4.92e-45

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: 156.49  E-value: 4.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889    21 RGVSLTNHHFY--DESKPFTCL-DGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVC 97
Cdd:pfam12999  20 RGVSPDNLHLYqpDENGNWKCLnHSEIKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDGVC 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48255889    98 D---CCDGTDEynSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQ 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 ...
 376-507 1.08e-13

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: 68.71  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   376 KFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPklggspTSLGTWGSWIGp 455
Cdd:pfam13015   4 SIDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDD------ISIGNFKKQEG- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 48255889   456 dhdkfSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELM 507
Cdd:pfam13015  77 -----NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVK 123
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 413-471 4.12e-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: 4.12e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48255889   413 SQCYELTTNEYVYRLCPFKLVSQKPKL---GGSPTSLGTWG--SWIGPDHDK--------FSAMKYEQGTGC 471
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGqekGGSSFSLGRFSesSWAESTYDDewtkgsnrYISMIYGNGTKC 72
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
199-293 5.79e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 47.75  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  199 EEQLAAAKAQ--------QEQELAADAFKELDDDMDGTVSVTELQTHP--------------ELDTDGDGALSEAEAQAL 256
Cdd:NF041410  82 SDELAAAAPPpppppdqaPSTELADDLLSALDTDGDGSISSDELSAGLtsagssadssqlfsALDSDGDGSVSSDELAAA 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48255889  257 L--------------------------SGDTQTDATSFYDRVWAAIRDKYRSealpTDLPAPS 293
Cdd:NF041410 162 LqpppppplfslssqgsssstqpsdssTASSSSNTTEALNKLIANLSKQYQS----LDNSASV 220
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
198-257 5.46e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 5.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48255889 198 WEEQLAAAKAQQEQELAADA---FKELDDDMDGTVSVTELQTH---------------PELDTDGDGALSEAEAQALL 257
Cdd:COG5126  52 REEFVAGMESLFEATVEPFAraaFDLLDTDGDGKISADEFRRLltalgvseeeadelfARLDTDGDGKISFEEFVAAV 129
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-220 5.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 117 KEKGRKERESLQQMAEvTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQK 196
Cdd:COG1196 284 EEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                        90       100
                ....*....|....*....|....
gi 48255889 197 LWEEQLAAAKAQQEQELAADAFKE 220
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAE 386
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
203-256 5.65e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 44.67  E-value: 5.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48255889  203 AAAKAQQEQELAADAFKELDDDMDGTVSVTELQTH-----------------PELDTDGDGALSEAE-AQAL 256
Cdd:NF041410  18 SSTSSARSQQFQKQLFAKLDSDGDGSVSQDELSSAlssksddgslidlselfSDLDSDGDGSLSSDElAAAA 89
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 118-279 2.83e-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: 43.30  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   118 EKGRKERESLQQMAEVTREgfrlkKILIEDWKKAREEKQKKLIELQAGKKSLED--QVEMLRTVKEEAEK----PEREAK 191
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAE-----RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAkkKAEAEAKAKAEAEAkakaEEAKAK 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   192 EQHQKLWEEQLAAAKAQQEQELAADAFKEldddmdgtvsvtelQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDR 271
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAE--------------RKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263


                  ....*...
gi 48255889   272 VWAAIRDK 279
Cdd:TIGR02794 264 YAAIIQQA 271
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 121-220 3.43e-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: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   121 RKERESLQQMAEVTREgfrLKKiliedwKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKlweE 200
Cdd:TIGR02794  64 KKEQERQKKLEQQAEE---AEK------QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA---E 131

                          90       100
                  ....*....|....*....|
gi 48255889   201 QLAAAKAQQEQELAADAFKE 220
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQ 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-215 7.70e-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: 42.35  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889    117 KEKGRKERESLQ-QMAEVTREGFRLKKILIEDwKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHq 195
Cdd:TIGR02168  304 KQILRERLANLErQLEELEAQLEELESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL- 381

                           90       100
                   ....*....|....*....|
gi 48255889    196 klweEQLAAAKAQQEQELAA 215
Cdd:TIGR02168  382 ----ETLRSKVAQLELQIAS 397
PRK12704 PRK12704
phosphodiesterase; Provisional
 118-213 1.25e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  118 EKGRKERESLQQMA--EVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQ 195
Cdd:PRK12704  45 EEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124

                         90       100
                 ....*....|....*....|
gi 48255889  196 KL--WEEQLAAAKAQQEQEL 213
Cdd:PRK12704 125 ELekKEEELEELIEEQLQEL 144
PTZ00121 PTZ00121
MAEBL; Provisional
 117-223 1.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   117 KEKGRKERESLQQMAEVTREGFRLKKILIEDWKKA----REEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKpereAKE 192
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK----KKI 1759

                          90       100       110
                  ....*....|....*....|....*....|.
gi 48255889   193 QHQKLWEEQLAAAKAQQEQELAADAFKELDD 223
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 153-224 2.03e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48255889  153 EEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQhQKLWEEQL------AAAKAQQEQELAADAFKELDDD 224
Cdd:PRK09510  90 EELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-QKQAEEAAakaaaaAKAKAEAEAKRAAAAAKKAAAE 166
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 144-275 2.05e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 144 LIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLwEEQLAAAKAQQEQELAADAFKELDD 223
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL-SAEEAAAEAQLAELEAELAAAEAAA 212

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 48255889 224 DMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAA 275
Cdd:COG3883 213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-217 2.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 117 KEKGRKERESLQQMAEVTREGFRLKKILIE------DWKKAREEkqkkLIELQAGKKSLEDQVEMLRTVKEEAEKPEREA 190
Cdd:COG4717  97 LEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAE----LAELPERLEELEERLEELRELEEELEELEAEL 172

                        90       100
                ....*....|....*....|....*....
gi 48255889 191 KEQHQKL--WEEQLAAAKAQQEQELAADA 217
Cdd:COG4717 173 AELQEELeeLLEQLSLATEEELQDLAEEL 201
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 117-217 2.50e-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: 40.21  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   117 KEKGRKERESLQQMAEVTREGFRLKKiliedwKKAREEKQKKLIELQAgkkslEDQVEMLRTVKEEAEK---PEREAKEQ 193
Cdd:TIGR02794  93 ELEQRAAAEKAAKQAEQAAKQAEEKQ------KQAEEAKAKQAAEAKA-----KAEAEAERKAKEEAAKqaeEEAKAKAA 161

                          90       100
                  ....*....|....*....|....
gi 48255889   194 HQKLWEEQLAAAKAQQEQELAADA 217
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAEAKAKAEA 185
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 118-217 2.69e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  118 EKGRKERESLQQMAE---VTREGFRLK-----KILIEDWKKAREEKQKKLIELQAGKKSLEDQ----VEMLRTVKEEAE- 184
Cdd:PRK09510 122 EAAKQAALKQKQAEEaaaKAAAAAKAKaeaeaKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKkkaeAEAAAKAAAEAKk 201

                         90       100       110
                 ....*....|....*....|....*....|...
gi 48255889  185 KPEREAKEQHQKLWEEQLAAAKAQQEQELAADA 217
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA 234
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 152-236 2.71e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 38.77  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  152 REEKQKKLIELQAGKKSLEDQ-VEMLRTVKEEAEKPEREAKEQ-------HQKLWEEQLAAAKAQQEQELAADAFkELDD 223
Cdd:PRK14475  57 REEAQALLADVKAEREEAERQaAAMLAAAKADARRMEAEAKEKleeqikrRAEMAERKIAQAEAQAAADVKAAAV-DLAA 135

                         90
                 ....*....|...
gi 48255889  224 DMDGTVSVTELQT 236
Cdd:PRK14475 136 QAAETVLAARLAG 148
PTZ00121 PTZ00121
MAEBL; Provisional
 118-220 3.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   118 EKGRKERESLQQMAEVTREGFRLKKILIEDWKKA----REEKQKKLIELQAGKKSLEDQVEmlrtvKEEAEKPEREAKEQ 193
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKA 1690

                          90       100
                  ....*....|....*....|....*..
gi 48255889   194 HQKLWEEQLAAAKAQQEQELAADAFKE 220
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKK 1717
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 118-212 3.18e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   118 EKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTV--KEEAEKPEREAKEQhQ 195
Cdd:pfam05672  39 EEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQkqKEEAEAKAREEAER-Q 117

                          90
                  ....*....|....*..
gi 48255889   196 KLWEEQLAaakAQQEQE 212
Cdd:pfam05672 118 RQEREKIM---QQEEQE 131
PTZ00121 PTZ00121
MAEBL; Provisional
 117-217 3.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   117 KEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKklielQAGKKSLEDQVEMLRTVK--EEAEKPEREAK--E 192
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-----AAAKKKADEAKKKAEEKKkaDEAKKKAEEAKkaD 1447

                          90       100
                  ....*....|....*....|....*
gi 48255889   193 QHQKLWEEQLAAAKAQQEQELAADA 217
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKA 1472
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 149-220 3.85e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 3.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48255889  149 KKAR----EEKQK--KLIE-LQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLwEEQLAAAKAQQEQElAADAFKE 220
Cdd:PRK00409 505 EEAKkligEDKEKlnELIAsLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKL-QEEEDKLLEEAEKE-AQQAIKE 581
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-256 4.42e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  121 RKERESLQQMAEVTREgfrlkkilIEDWKKAREEkqkkLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEE 200
Cdd:COG4913  644 QERREALQRLAEYSWD--------EIDVASAERE----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL 711

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 48255889  201 QLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQAL 256
Cdd:COG4913  712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 125-217 5.41e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 5.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 125 ESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAA 204
Cdd:COG3883 122 SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                        90
                ....*....|...
gi 48255889 205 AKAQQEQELAADA 217
Cdd:COG3883 202 EAELAAAEAAAAA 214
fliH PRK06800
flagellar assembly protein H; Validated
 130-268 5.42e-03

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 38.70  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  130 MAEVTREGFRLKKILIEdwkkAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAE------KPEREAKEQHQKLWEEQLA 203
Cdd:PRK06800  15 FSEETYELQFPKPIEVE----VEEEIQKDHEELLAQQKSLHKELNQLRQEQQKLErerqqlLADREQFQEHVQQQMKEIE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48255889  204 AAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTdgdgalSEAEAQALLSGDTQTDATSF 268
Cdd:PRK06800  91 AARQQFQKEQQETAYEWTELLWDQSFQLAEKIVNQAVDT------RLLDVLPILTGIVQTLPTSF 149
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 116-213 5.84e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 39.25  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   116 CKEKGRKERESLQQMAEVTREGfrlkkiliedwKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQ 195
Cdd:pfam15558  57 QQSQEQWQAEKEQRKARLGREE-----------RRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQ 125

                          90       100
                  ....*....|....*....|..
gi 48255889   196 ----KLWEEQLAAAKAQQEQEL 213
Cdd:pfam15558 126 eqrlKEKEEELQALREQNSLQL 147
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 114-208 6.28e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 37.59  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  114 NTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKklIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQ 193
Cdd:PRK14473  35 NLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAK--IVAQAQERARAQEAEIIAQARREAEKIKEEARAQ 112

                         90
                 ....*....|....*
gi 48255889  194 HQKLWEEQLAAAKAQ 208
Cdd:PRK14473 113 AEQERQRMLSELKSQ 127
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 121-211 6.66e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 38.86  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889   121 RKERES--LQQMAEVTREGFRLKkiliEDWKKAREEKQKKLiELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLW 198
Cdd:pfam15558  18 KEEQRMreLQQQAALAWEELRRR----DQKRQETLERERRL-LLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEK 92

                          90
                  ....*....|...
gi 48255889   199 EEQLAAAKAQQEQ 211
Cdd:pfam15558  93 ESRWREQAEDQEN 105
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 139-225 6.92e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 6.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 139 RLKKIL--IEDWKKAREEKQKKLIELQagkksledqvEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELA-- 214
Cdd:cd06503  31 REEKIAesLEEAEKAKEEAEELLAEYE----------EKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEqa 100

                        90
                ....*....|....*....
gi 48255889 215 --------ADAFKELDDDM 225
Cdd:cd06503 101 kaeieqekEKALAELRKEV 119
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-217 7.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 118 EKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKpEREAKEQHQKL 197
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE-RLEELEEELAE 327

                        90       100
                ....*....|....*....|
gi 48255889 198 WEEQLAAAKAQQEQELAADA 217
Cdd:COG1196 328 LEEELEELEEELEELEEELE 347
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 118-222 7.78e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889  118 EKGRKERESLQQMAEvtregfRLKKILIEDWKKAREEKQKKLIELQ--------AGKKSLEDQVEMLRTV--KEEAEKPE 187
Cdd:PRK00409 533 EQKAEEAEALLKEAE------KLKEELEEKKEKLQEEEDKLLEEAEkeaqqaikEAKKEADEIIKELRQLqkGGYASVKA 606

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 48255889  188 REAKEQHQKLWEEQLAAAKAQQEQELAADAFKELD 222
Cdd:PRK00409 607 HELIEARKRLNKANEKKEKKKKKQKEKQEELKVGD 641
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 154-295 8.36e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48255889 154 EKQKKLI-ELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLwEEQLAAAKAQQEQeLAADAFKELDDDMDGTVSVT 232
Cdd:COG3883 129 DADADLLeELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL-EAQQAEQEALLAQ-LSAEEAAAEAQLAELEAELA 206

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48255889 233 ELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAP 295
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAA 269
 
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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