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Conserved domains on  [gi|892643382|emb|CNB05085|]
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type III secretion system ATPase [Yersinia pseudotuberculosis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06820 super family cl32170
EscN/YscN/HrcN family type III secretion system ATPase;
1-202 6.66e-127

EscN/YscN/HrcN family type III secretion system ATPase;


The actual alignment was detected with superfamily member PRK06820:

Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 364.52  E-value: 6.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80
Cdd:PRK06820   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  81 SDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSC 160
Cdd:PRK06820  81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSC 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 892643382 161 GEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK06820 161 GEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGR 202
 
Name Accession Description Interval E-value
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
1-202 6.66e-127

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 364.52  E-value: 6.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80
Cdd:PRK06820   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  81 SDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSC 160
Cdd:PRK06820  81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSC 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 892643382 161 GEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK06820 161 GEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGR 202
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 15-202 1.07e-79

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 243.78  E-value: 1.07e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  15 QQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVT 91
Cdd:COG1157    5 ARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  92 PLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTG-QWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFA 170
Cdd:COG1157   85 PTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGeERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFA 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 892643382 171 AAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:COG1157  165 GSGVGKSTLLGMIARNTEADVNVIALIGERGR 196
III_secr_ATP TIGR02546
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ...
 26-202 3.50e-75

type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274191 [Multi-domain]  Cd Length: 422  Bit Score: 232.21  E-value: 3.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   26 GLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVG 102
Cdd:TIGR02546   2 PVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDpsqLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  103 ADLAGRILDGLGAPIDGGPPL---TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTL 179
Cdd:TIGR02546  82 EALLGRVLDGFGRPLDGKGELpagEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTL 161

                         170       180
                  ....*....|....*....|...
gi 892643382  180 LSMLCADSAADVMVLALIGERGR 202
Cdd:TIGR02546 162 LGMIARGASADVNVIALIGERGR 184
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 98-202 1.84e-46

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 153.87  E-value: 1.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  98 RVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGK 176
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGkGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100
                 ....*....|....*....|....*.
gi 892643382 177 STLLSMLCADSAADVMVLALIGERGR 202
Cdd:cd01136   81 STLLGMIARNTDADVNVIALIGERGR 106
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 150-202 2.02e-21

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 87.41  E-value: 2.02e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 892643382  150 GVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGR 53
 
Name Accession Description Interval E-value
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
1-202 6.66e-127

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 364.52  E-value: 6.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80
Cdd:PRK06820   1 MKLPDIARLTPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  81 SDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSC 160
Cdd:PRK06820  81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSC 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 892643382 161 GEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK06820 161 GEGQRIGIFAAAGVGKSTLLGMLCADSAADVMVLALIGERGR 202
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 15-202 1.07e-79

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 243.78  E-value: 1.07e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  15 QQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVT 91
Cdd:COG1157    5 ARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  92 PLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTG-QWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFA 170
Cdd:COG1157   85 PTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGeERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFA 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 892643382 171 AAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:COG1157  165 GSGVGKSTLLGMIARNTEADVNVIALIGERGR 196
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
13-202 1.43e-76

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 236.00  E-value: 1.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  13 LQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTP 92
Cdd:PRK07594   5 LMQRLRLKYPPPDGYCRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  93 LGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAA 172
Cdd:PRK07594  85 LRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAP 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 892643382 173 GVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK07594 165 GVGKSTLLAMLCNAPDADSNVLVLIGERGR 194
III_secr_ATP TIGR02546
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ...
 26-202 3.50e-75

type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274191 [Multi-domain]  Cd Length: 422  Bit Score: 232.21  E-value: 3.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   26 GLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVG 102
Cdd:TIGR02546   2 PVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDpsqLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  103 ADLAGRILDGLGAPIDGGPPL---TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTL 179
Cdd:TIGR02546  82 EALLGRVLDGFGRPLDGKGELpagEIETRPLDADPPPPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTL 161

                         170       180
                  ....*....|....*....|...
gi 892643382  180 LSMLCADSAADVMVLALIGERGR 202
Cdd:TIGR02546 162 LGMIARGASADVNVIALIGERGR 184
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
27-202 9.69e-60

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 193.05  E-value: 9.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  27 LRYRGPIVEIGPTLLRASLPNVAQGELCRI----EPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVG 102
Cdd:PRK06936  21 IQIRGRVTQVTGTILKAVVPGVRIGELCYLrnpdNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 103 ADLAGRILDGLGAPIDGGPPLT-GQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLS 181
Cdd:PRK06936 101 EHLLGRVLDGLGQPFDGGHPPEpAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLA 180

                        170       180
                 ....*....|....*....|.
gi 892643382 182 MLCADSAADVMVLALIGERGR 202
Cdd:PRK06936 181 SLIRSAEVDVTVLALIGERGR 201
fliI_yscN TIGR01026
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ...
 24-202 3.44e-55

ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273401 [Multi-domain]  Cd Length: 440  Bit Score: 181.03  E-value: 3.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   24 PEGLRYRGPIVEIGPTLLRASLPNVAQGELCRIEPQGM----LAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRV 99
Cdd:TIGR01026  18 LRLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSegrlVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  100 QVGADLAGRILDGLGAPIDGGPPLTGQWRE--LDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKS 177
Cdd:TIGR01026  98 KVGDGLLGRVLDGLGKPIDGKGKFLDNVETegLITAPINPLKRAPIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKS 177

                         170       180
                  ....*....|....*....|....*
gi 892643382  178 TLLSMLCADSAADVMVLALIGERGR 202
Cdd:TIGR01026 178 TLLGMIARNTEADVNVIALIGERGR 202
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 10-202 2.89e-53

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 176.11  E-value: 2.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  10 TPRLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRASLPNVAQGELCRI-EPQGML---AEVVSIEQEMALLSPFASSDGLR 85
Cdd:PRK09099   5 LSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTLGELCELrQRDGTLlqrAEVVGFSRDVALLSPFGELGGLS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  86 CGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTG-QWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQ 164
Cdd:PRK09099  85 RGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCdELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQ 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 892643382 165 RIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK09099 165 RMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGR 202
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 98-202 1.84e-46

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 153.87  E-value: 1.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  98 RVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGK 176
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGkGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100
                 ....*....|....*....|....*.
gi 892643382 177 STLLSMLCADSAADVMVLALIGERGR 202
Cdd:cd01136   81 STLLGMIARNTDADVNVIALIGERGR 106
PRK08149 PRK08149
FliI/YscN family ATPase;
11-202 2.55e-46

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 157.46  E-value: 2.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  11 PRLQQQLTRPsappegLRYRGPIVEigptllrASLPNVAQGELCRI-----EPQGM-LAEVVSIEQEMALLSPFASSDGL 84
Cdd:PRK08149   1 LRLLQRLAHP------LRIQGPIIE-------AELPDVAIGEICEIragwhSNEVIaRAQVVGFQRERTILSLIGNAQGL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  85 RCGQWVTPLGHMHRVQVGADLAGRILDGLG-------APIdggPPLT-GQWRELDCPPPSPLTRQPVEQMLTTGVRAIDG 156
Cdd:PRK08149  68 SRQVVLKPTGKPLSVWVGEALLGAVLDPTGkiverfdAPP---TVGPiSEERVIDVAPPSYAERRPIREPLITGVRAIDG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 892643382 157 ILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK08149 145 LLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGR 190
fliI PRK07721
flagellar protein export ATPase FliI;
46-202 1.20e-45

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 156.04  E-value: 1.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  46 PNVAQGELCRIEPQG-----MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGG 120
Cdd:PRK07721  35 PESSIGDVCYIHTKGggdkaIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 121 P-PLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGE 199
Cdd:PRK07721 115 AlPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGE 194


                 ...
gi 892643382 200 RGR 202
Cdd:PRK07721 195 RGR 197
fliI PRK08472
flagellar protein export ATPase FliI;
31-202 3.31e-42

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 146.75  E-value: 3.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  31 GPIVEIGPTLLRASLPNVAQGELCRIEPQ-------GMlaeVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGA 103
Cdd:PRK08472  20 GSITKISPTIIEADGLNPSVGDIVKIESSdngkeclGM---VVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 104 DLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSM 182
Cdd:PRK08472  97 NLLGRVVDPLGRPIDGkGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176

                        170       180
                 ....*....|....*....|
gi 892643382 183 LCADSAADVMVLALIGERGR 202
Cdd:PRK08472 177 IVKGCLAPIKVVALIGERGR 196
fliI PRK08972
flagellar protein export ATPase FliI;
8-202 5.66e-42

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 146.38  E-value: 5.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   8 RLTPRL---QQQLTRPSAPPEGLRYRGpiveIGPTLlRASLPNVAQGELCRIEPQG--MLAEVVSIEQEMALLSPFASSD 82
Cdd:PRK08972   6 QLLNRLkqyKVKVPPFRAVASGKLVRV----VGLTL-EATGCRAPVGSLCSIETMAgeLEAEVVGFDGDLLYLMPIEELR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  83 GLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCG 161
Cdd:PRK08972  81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGlGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 892643382 162 EGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGR 201
PRK05922 PRK05922
type III secretion system ATPase; Validated
 29-202 2.13e-39

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 139.65  E-value: 2.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  29 YR--GPIVEIGPTLLRASLPNVAQGELCRI---EPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGA 103
Cdd:PRK05922  17 YRecGLLSRVSGNLLEAQGLSACLGELCQIslsKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 104 DLAGRILDGLGAPIDGGPPL-TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSM 182
Cdd:PRK05922  97 HLLGRVLDGFGNPLDGKEQLpKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLST 176

                        170       180
                 ....*....|....*....|
gi 892643382 183 LCADSAADVMVLALIGERGR 202
Cdd:PRK05922 177 IAKGSKSTINVIALIGERGR 196
fliI PRK06002
flagellar protein export ATPase FliI;
12-202 1.01e-38

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 137.82  E-value: 1.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  12 RLQQQLTRPSAPPEGLRYRGPIVEIGPTLLRAS--LPNVAQGELCRIEPQG--MLAEVVSIEQEMALLSPFASSDGLRCG 87
Cdd:PRK06002   9 RLAALVERYAAPEPLVRIGGTVSEVTASHYRVRglSRFVRLGDFVAIRADGgtHLGEVVRVDPDGVTVKPFEPRIEIGLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  88 QWVTPLGHMhRVQVGADLAGRILDGLGAPIDGGPPLTG--QWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQR 165
Cdd:PRK06002  89 DAVFRKGPL-RIRPDPSWKGRVINALGEPIDGLGPLAPgtRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQR 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 892643382 166 IGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK06002 168 IGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGR 204
fliI PRK08927
flagellar protein export ATPase FliI;
30-202 7.51e-38

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 135.49  E-value: 7.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  30 RGPIVEIGPTLLRASLpnvaqGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGADLA 106
Cdd:PRK08927  25 RGLLVEVAGPIHALSV-----GARIVVETRGgrpVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 107 GRILDGLGAPIDGGPPLT--GQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLC 184
Cdd:PRK08927 100 GRVVNALGEPIDGKGPLPqgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLA 179

                        170
                 ....*....|....*...
gi 892643382 185 ADSAADVMVLALIGERGR 202
Cdd:PRK08927 180 RNADADVSVIGLIGERGR 197
fliI PRK05688
flagellar protein export ATPase FliI;
7-202 4.02e-37

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 133.70  E-value: 4.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   7 ARLTPRLQQQLTRPSAPPEglryrgPIVE------IGPTLLRASLpNVAQGELCRIE------PQGMLAEVVSIEQEMAL 74
Cdd:PRK05688   6 TSFAKRLEGYAEAISLPAQ------PVVEgrllrmVGLTLEAEGL-RAAVGSRCLVInddsyhPVQVEAEVMGFSGDKVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  75 LSPFASSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPVEQMLTTGVRA 153
Cdd:PRK05688  79 LMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEdWVPMDGPTINPLNRHPISEPLDVGIRS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 892643382 154 IDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK05688 159 INGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGR 207
fliI PRK06793
flagellar protein export ATPase FliI;
46-202 2.05e-33

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 123.55  E-value: 2.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  46 PNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPID---GGPP 122
Cdd:PRK06793  38 PKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNeeaENIP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 123 LtgQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK06793 118 L--QKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGR 195
fliI PRK07196
flagellar protein export ATPase FliI;
28-202 3.48e-33

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 123.08  E-value: 3.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  28 RYRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGAD 104
Cdd:PRK07196  16 RVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDetfIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 105 LAGRILDGLGAPIDGGPPLTGQWRELDCPPP-SPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSML 183
Cdd:PRK07196  96 WLGRVINGLGEPLDGKGQLGGSTPLQQQLPQiHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMI 175

                        170
                 ....*....|....*....
gi 892643382 184 CADSAADVMVLALIGERGR 202
Cdd:PRK07196 176 TRYTQADVVVVGLIGERGR 194
fliI PRK07960
flagellum-specific ATP synthase FliI;
9-202 1.51e-31

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 118.73  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   9 LTPRLQQQLT-------RPSAPPEGLRYrGPIVEIGPTLLRASLPNVAQGELCRIEPQG------MLAEVVSIEQEMALL 75
Cdd:PRK07960   1 MTTRLTRWLTtldnfeaKMAQLPAVRRY-GRLTRATGLVLEATGLQLPLGATCVIERQNgsetheVESEVVGFNGQRLFL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  76 SPFASSDGLRCGQWV-------TPLGHMHRVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTRQPVEQML 147
Cdd:PRK07960  80 MPLEEVEGILPGARVyarnisgEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPaPDTGETGALITPPFNPLQRTPIEHVL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 892643382 148 TTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:PRK07960 160 DTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGR 214
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 98-202 3.18e-26

RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410884 [Multi-domain]  Cd Length: 270  Bit Score: 101.38  E-value: 3.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  98 RVQVGADLAGRILDGLGAPIDGGPPL-TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGK 176
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIkTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                         90       100
                 ....*....|....*....|....*....
gi 892643382 177 STLLSMLCADSA---ADVMVLALIGERGR 202
Cdd:cd19476   81 TVLAMQLARNQAkahAGVVVFAGIGERGR 109
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 12-179 3.71e-25

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 101.53  E-value: 3.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  12 RLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRAS-LPNVAQGELCRIePQGMLAEVVSIEQEM---ALLSPfasSDGLRCG 87
Cdd:PRK13343  11 RIRQRIARYEPQPD-AREIGRVESVGDGIAFVSgLPDAALDELLRF-EGGSRGFAFNLEEELvgaVLLDD---TADILAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  88 QWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPL-TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRI 166
Cdd:PRK13343  86 TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLqATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRE 165

                        170
                 ....*....|...
gi 892643382 167 GIFAAAGVGKSTL 179
Cdd:PRK13343 166 LIIGDRQTGKTAI 178
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 33-198 3.10e-24

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 98.57  E-value: 3.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  33 IVEIGPTLLRASLPNVAQGELCRIEPQ--GMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGADLAGRIL 110
Cdd:PRK02118   8 ITDITGNVITVEAEGVGYGELATVERKdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382 111 DGLGAPIDGGPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAAD 190
Cdd:PRK02118  88 NGSGKPIDGGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQAEAD 167


                 ....*...
gi 892643382 191 VMVLALIG 198
Cdd:PRK02118 168 IIILGGMG 175
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 150-202 2.02e-21

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 87.41  E-value: 2.02e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 892643382  150 GVRAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGERGR 202
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGR 53
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 29-173 1.93e-19

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 85.26  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  29 YRGpIVEI-GPTLLRASLPNVAQGELCRIE-PQGML--AEVVSIEQEMALLSPFASSDGLRC-GQWVTPLGHMHRVQVGA 103
Cdd:PRK04196   4 YRT-VSEIkGPLLFVEGVEGVAYGEIVEIElPNGEKrrGQVLEVSEDKAVVQVFEGTTGLDLkDTKVRFTGEPLKLPVSE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892643382 104 DLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAG 173
Cdd:PRK04196  83 DMLGRIFDGLGRPIDGGPEiIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSG 153
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 98-198 1.75e-18

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 80.73  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  98 RVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGK 176
Cdd:cd01135    3 KLPVSEDMLGRIFNGSGKPIDGGPPiLPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82

                         90       100
                 ....*....|....*....|....*...
gi 892643382 177 STLLSMLC------ADSAADVMVLALIG 198
Cdd:cd01135   83 NELAAQIArqagvvGSEENFAIVFAAMG 110
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 80-202 2.57e-18

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


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 82.06  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  80 SSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTG-QWRELDCPPPsPLTRQ-PVEQMLTTGVRAIDGI 157
Cdd:COG0055   62 STDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAkERRPIHRPAP-PFEEQsTKTEILETGIKVIDLL 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 892643382 158 LSCGEGQRIGIFAAAGVGKSTLLSMLCADSAAD---VMVLALIGERGR 202
Cdd:COG0055  141 APYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEhggVSVFAGVGERTR 188
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 79-202 7.18e-16

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 75.14  E-value: 7.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   79 ASSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPVEQMLTTGVRAIDGI 157
Cdd:TIGR01039  58 GSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERwPIHRKAPSFEEQSTKVEILETGIKVIDLL 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 892643382  158 LSCGEGQRIGIFAAAGVGKSTLLSMLCADSAAD---VMVLALIGERGR 202
Cdd:TIGR01039 138 APYAKGGKIGLFGGAGVGKTVLIQELINNIAKEhggYSVFAGVGERTR 185
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 31-167 1.44e-15

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 73.95  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  31 GPIVEIGPTLLRAS-LPNVAQGELcrIE-PQGMLAEVVSIEQE---MALLSPFassDGLRCGQWVTPLGHMHRVQVGADL 105
Cdd:PRK09281  29 GTVISVGDGIARVYgLDNVMAGEL--LEfPGGVYGIALNLEEDnvgAVILGDY---EDIKEGDTVKRTGRILEVPVGEAL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892643382 106 AGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQR---IG 167
Cdd:PRK09281 104 LGRVVNPLGQPIDGkGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQReliIG 169
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 94-184 1.11e-14

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 71.68  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   94 GHMHRVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAA 172
Cdd:TIGR01040  71 GDILRTPVSEDMLGRVFNGSGKPIDKGPPvLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAA 150

                          90
                  ....*....|..
gi 892643382  173 GVGKSTLLSMLC 184
Cdd:TIGR01040 151 GLPHNEIAAQIC 162
ATP-synt_flagellum-secretory_path_III_N cd18117
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ...
 29-94 3.68e-14

Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-ATP synthase. Although they both are proton driven rotary molecular devices, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens, such as Salmonella and Chlamydia, also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 349741 [Multi-domain]  Cd Length: 70  Bit Score: 64.47  E-value: 3.68e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 892643382  29 YRGPIVEIGPTLLRASLPNVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLG 94
Cdd:cd18117    1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADglsILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 99-179 1.47e-12

F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 64.50  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  99 VQVGADLAGRILDGLGAPIDGGPPL-TGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGILSCGEGQRIGIFAAAGVGKS 177
Cdd:cd01132    4 VPVGEALLGRVVDALGNPIDGKGPIqTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83


                 ..
gi 892643382 178 TL 179
Cdd:cd01132   84 AI 85
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 98-202 5.83e-12

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 63.01  E-value: 5.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  98 RVQVGADLAGRILDGLGAPIDGGPPL-TGQWRELDCPPPsPLTRQPVEQ-MLTTGVRAIDGILSCGEGQRIGIFAAAGVG 175
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIkAKERWPIHREAP-EFVELSTEQeILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 892643382 176 KSTLLSML---CADSAADVMVLALIGERGR 202
Cdd:cd01133   80 KTVLIMELinnIAKAHGGYSVFAGVGERTR 109
atpA CHL00059
ATP synthase CF1 alpha subunit
 82-167 4.31e-11

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 61.13  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  82 DGLRC--GQWVTPLGHMHRVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPVEQMLTTGVRAIDGIL 158
Cdd:CHL00059  57 DGLMIqeGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGkGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMI 136

                         90
                 ....*....|..
gi 892643382 159 SCGEGQR---IG 167
Cdd:CHL00059 137 PIGRGQReliIG 148
atpB CHL00060
ATP synthase CF1 beta subunit
 80-202 7.96e-09

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 54.28  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  80 SSDGLRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPS--PLTRQPveQMLTTGVRAIDG 156
Cdd:CHL00060  77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTSPIHRSAPAfiQLDTKL--SIFETGIKVVDL 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 892643382 157 ILSCGEGQRIGIFAAAGVGKSTLLSML---CADSAADVMVLALIGERGR 202
Cdd:CHL00060 155 LAPYRRGGKIGLFGGAGVGKTVLIMELinnIAKAHGGVSVFGGVGERTR 203
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 30-95 1.71e-05

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases 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. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.


Pssm-ID: 349738 [Multi-domain]  Cd Length: 73  Bit Score: 41.53  E-value: 1.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 892643382  30 RGPIVEIGPTLLRASLPN-VAQGELCRIEPQGML------AEVVSIEQEMALLSPFASSDGLRCGQWVTPLGH 95
Cdd:cd01426    1 KGRVIRVNGPLVEAELEGeVAIGEVCEIERGDGNnetvlkAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 84-179 1.22e-04

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 41.95  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382  84 LRCGQWVTPLGHMHRVQVGADLAGRILDGLGAPIDGGppLTGQWREL----------DCPPPSPLTRQPVEQMLTTGVRA 153
Cdd:PTZ00185 102 VQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVG--LLTRSRALleseqtlgkvDAGAPNIVSRSPVNYNLLTGFKA 179

                         90       100
                 ....*....|....*....|....*.
gi 892643382 154 IDGILSCGEGQRIGIFAAAGVGKSTL 179
Cdd:PTZ00185 180 VDTMIPIGRGQRELIVGDRQTGKTSI 205
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 30-118 1.84e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 41.55  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892643382   30 RGPIVEI-GPTLLRASLPNVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHRVQVGADLAGR 108
Cdd:PRK14698    4 KGRIIRVtGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTS 83

                          90
                  ....*....|
gi 892643382  109 ILDGLGAPID 118
Cdd:PRK14698   84 IYDGIQRPLE 93
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 151-184 1.14e-03

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 38.52  E-value: 1.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 892643382 151 VRAIDGI-LSCGEGQRIGIFAAAGVGKSTLLSMLC 184
Cdd:COG1134   39 FWALKDVsFEVERGESVGIIGRNGAGKSTLLKLIA 73
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 151-184 1.50e-03

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 38.28  E-value: 1.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 892643382 151 VRAIDGI-LSCGEGQRIGIFAAAGVGKSTLLSMLC 184
Cdd:cd03220   35 FWALKDVsFEVPRGERIGLIGRNGAGKSTLLRLLA 69
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
150-199 4.37e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 37.20  E-value: 4.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 892643382 150 GVRAIDGI-LSCGEGQRIGIFAAAGVGKSTLLSMLCADSAADVMVLALIGE 199
Cdd:PRK11288  16 GVKALDDIsFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ 66
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 150-184 4.64e-03

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 36.22  E-value: 4.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 892643382 150 GVRAIDGI-LSCGEGQRIGIFAAAGVGKSTLLSMLC 184
Cdd:cd03230   12 KKTALDDIsLTVEKGEIYGLLGPNGAGKTTLIKIIL 47
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 158-184 7.74e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 35.32  E-value: 7.74e-03
                          10        20
                  ....*....|....*....|....*..
gi 892643382  158 LSCGEGQRIGIFAAAGVGKSTLLSMLC 184
Cdd:pfam00005   6 LTLNPGEILALVGPNGAGKSTLLKLIA 32
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 152-200 9.51e-03

C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.


Pssm-ID: 410872 [Multi-domain]  Cd Length: 249  Bit Score: 36.03  E-value: 9.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 892643382 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLSMLCADSAAD-----VMVLaLIGER 200
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNhpeveLIVL-LIDER 57
 
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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