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Conserved domains on  [gi|532165038|gb|AGT80002|]
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type III secretion apparatus H+-transporting two-sector ATPase, partial [Xanthomonas citri pv. mangiferaeindicae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09099 super family cl31593
type III secretion system ATPase; Provisional
 1-139 2.17e-78

type III secretion system ATPase; Provisional


The actual alignment was detected with superfamily member PRK09099:

Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 238.13  E-value: 2.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK09099  23 RRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK09099 103 ALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLG 161
 
Name Accession Description Interval E-value
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 1-139 2.17e-78

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 238.13  E-value: 2.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK09099  23 RRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK09099 103 ALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLG 161
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-139 1.93e-55

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: 178.69  E-value: 1.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLqRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:COG1157   18 RVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPV-LAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:COG1157   97 GLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVG 155
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 76-139 7.80e-21

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: 84.92  E-value: 7.80e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532165038  76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:cd01136    2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCG 65
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 3-135 2.38e-13

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: 65.51  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038    3 YGKVVELVGIMLKVAGVQVSLGEV-----CELRQRDGTLLQRAEVVG--FSRDLALlapfGELVGLSRETRVIGLGRPLA 75
Cdd:TIGR01039   2 KGKVVQVIGPVVDVEFEQGELPRIynalkVQNRAESELTLEVAQHLGddTVRTIAM----GSTDGLVRGLEVIDTGAPIS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532165038   76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDpmrrrLIEQP-----MPTGVRIVDGL 135
Cdd:TIGR01039  78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPS-----FEEQStkveiLETGIKVIDLL 137
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 6-71 5.77e-03

ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 33.67  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038    6 VVELVGIMLKVA-GVQVSLGEVCELRQR--DGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLG 71
Cdd:pfam02874   1 IVQVIGPVVDVEfGIGRLPGLLNALEVElvEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
 
Name Accession Description Interval E-value
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 1-139 2.17e-78

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 238.13  E-value: 2.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK09099  23 RRTGKVVEVIGTLLRVSGLDVTLGELCELRQRDGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK09099 103 ALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLG 161
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-139 1.93e-55

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: 178.69  E-value: 1.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLqRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:COG1157   18 RVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPV-LAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:COG1157   97 GLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVG 155
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
4-139 8.19e-43

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 146.05  E-value: 8.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   4 GKVVELVGIMLK--VAGVQVslGEVCELRQRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPA 81
Cdd:PRK06936  25 GRVTQVTGTILKavVPGVRI--GELCYLRNPDNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEH 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  82 LLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK06936 103 LLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
fliI PRK07721
flagellar protein export ATPase FliI;
1-139 6.04e-33

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 119.83  E-value: 6.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELR-QRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVG 79
Cdd:PRK07721  17 KRYGKVSRVIGLMIESKGPESSIGDVCYIHtKGGGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVG 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  80 PALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK07721  97 SGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVG 156
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
1-139 1.26e-28

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 108.36  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDgtllQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK06820  28 RYRGPIVEIGPTLLRASLPGVAQGELCRIEPQG----MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGA 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDtWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK06820 104 DLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCG 161
fliI PRK08972
flagellar protein export ATPase FliI;
4-139 1.52e-28

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 107.86  E-value: 1.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   4 GKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLqrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPALL 83
Cdd:PRK08972  27 GKLVRVVGLTLEATGCRAPVGSLCSIETMAGELE--AEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLL 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 532165038  84 GRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK08972 105 GRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
fliI PRK05688
flagellar protein export ATPase FliI;
4-139 6.86e-27

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 103.66  E-value: 6.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   4 GKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQR--AEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPA 81
Cdd:PRK05688  29 GRLLRMVGLTLEAEGLRAAVGSRCLVINDDSYHPVQveAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMS 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  82 LLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK05688 109 MLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVG 166
fliI PRK08472
flagellar protein export ATPase FliI;
2-139 3.82e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 98.60  E-value: 3.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   2 RYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPA 81
Cdd:PRK08472  18 RFGSITKISPTIIEADGLNPSVGDIVKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRN 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  82 LLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK08472  98 LLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCG 155
PRK08149 PRK08149
FliI/YscN family ATPase;
21-139 3.15e-24

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 96.22  E-value: 3.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  21 VSLGEVCELRQ--RDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPS---D 95
Cdd:PRK08149  25 VAIGEICEIRAgwHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVerfD 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 532165038  96 GQGAIACD-TWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK08149 105 APPTVGPIsEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCG 149
fliI PRK07196
flagellar protein export ATPase FliI;
1-139 1.55e-23

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 94.19  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK07196  16 RVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFIE-AQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGD 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIACDTwiPIQAQAP--DPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK07196  95 SWLGRVINGLGEPLDGKGQLGGST--PLQQQLPqiHPLQRRAVDTPLDVGVNAINGLLTIG 153
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
1-139 7.70e-23

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 92.32  E-value: 7.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTllqrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK07594  20 CRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEEL----AEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQgAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK07594  96 ALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCG 153
PRK05922 PRK05922
type III secretion system ATPase; Validated
 1-139 1.87e-22

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 91.12  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCEL-RQRDGTLLqrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVG 79
Cdd:PRK05922  18 RECGLLSRVSGNLLEAQGLSACLGELCQIsLSKSPPIL--AEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLS 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  80 PALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK05922  96 DHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLG 155
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 1-138 1.04e-21

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 89.11  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQ-VSLGEVCELRQRDGTLlQRAEVVGFSRDLALLAPFGELVGLS-RETRVIGLGRPLAVPV 78
Cdd:PRK04196   2 KEYRTVSEIKGPLLFVEGVEgVAYGEIVEIELPNGEK-RRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  79 GPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTL 138
Cdd:PRK04196  81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTL 140
fliI PRK07960
flagellum-specific ATP synthase FliI;
1-139 2.24e-21

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 88.30  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLQ--RAEVVGFSRDLALLAPFGELVGLSRETRVI-------GLG 71
Cdd:PRK07960  26 RRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHevESEVVGFNGQRLFLMPLEEVEGILPGARVYarnisgeGLQ 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  72 RPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK07960 106 SGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVG 173
fliI PRK08927
flagellar protein export ATPase FliI;
3-138 4.91e-21

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 87.34  E-value: 4.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   3 YGKVVELVGIMLKVAGVQ--VSLGEVCELRQRDGTLLQrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK08927  18 YGRVVAVRGLLVEVAGPIhaLSVGARIVVETRGGRPVP-CEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSR 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038  81 ALLGRVLDGLGEPSDGQGAIA-CDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTL 138
Cdd:PRK08927  97 AWLGRVVNALGEPIDGKGPLPqGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTC 155
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 76-139 7.80e-21

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: 84.92  E-value: 7.80e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532165038  76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:cd01136    2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCG 65
ATP-synt_flagellum-secretory_path_III_N cd18117
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ...
 2-72 8.68e-21

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: 79.88  E-value: 8.68e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532165038   2 RYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGtLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGR 72
Cdd:cd18117    1 VYGRVVRVVGLLLEAVGPQAPIGELCLIETADG-LSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 65-139 3.80e-19

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 82.27  E-value: 3.80e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532165038  65 TRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK13343  86 TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 55-139 6.30e-19

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


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 81.62  E-value: 6.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  55 FGELVGLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDG 134
Cdd:COG0056   76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155


                 ....*
gi 532165038 135 LMTLG 139
Cdd:COG0056  156 MIPIG 160
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 1-138 7.89e-19

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 81.23  E-value: 7.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQVSLGEVCELRQRDGTLLqrAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGP 80
Cdd:PRK02118   3 KIYTKITDITGNVITVEAEGVGYGELATVERKDGSSL--AQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  81 ALLGRVLDGLGEPSDGqGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTL 138
Cdd:PRK02118  81 SLLGRRFNGSGKPIDG-GPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTL 137
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 55-135 2.53e-18

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 79.72  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  55 FGELVGLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDG 134
Cdd:PRK09281  76 LGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDA 155


                 .
gi 532165038 135 L 135
Cdd:PRK09281 156 M 156
fliI PRK06002
flagellar protein export ATPase FliI;
1-133 1.53e-15

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 71.95  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038   1 RRYGKVVELVGIMLKVAGVQ--VSLGEVCELRQRDGTllQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGrPLAVPV 78
Cdd:PRK06002  25 RIGGTVSEVTASHYRVRGLSrfVRLGDFVAIRADGGT--HLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRP 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 532165038  79 GPALLGRVLDGLGEPSDGQGAIAC-DTWIPIQAQAPDPMRRRLIEQPMPTGVRIVD 133
Cdd:PRK06002 102 DPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVID 157
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 76-139 2.29e-15

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: 70.18  E-value: 2.29e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532165038  76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:cd19476    2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYG 65
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 60-133 4.95e-15

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: 70.12  E-value: 4.95e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532165038  60 GLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVD 133
Cdd:COG0055   65 GLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVID 138
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 74-139 8.29e-15

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: 68.74  E-value: 8.29e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532165038  74 LAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIG 67
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 3-135 2.38e-13

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: 65.51  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038    3 YGKVVELVGIMLKVAGVQVSLGEV-----CELRQRDGTLLQRAEVVG--FSRDLALlapfGELVGLSRETRVIGLGRPLA 75
Cdd:TIGR01039   2 KGKVVQVIGPVVDVEFEQGELPRIynalkVQNRAESELTLEVAQHLGddTVRTIAM----GSTDGLVRGLEVIDTGAPIS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532165038   76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDpmrrrLIEQP-----MPTGVRIVDGL 135
Cdd:TIGR01039  78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPS-----FEEQStkveiLETGIKVIDLL 137
atpA CHL00059
ATP synthase CF1 alpha subunit
 65-139 7.19e-12

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 61.13  E-value: 7.19e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532165038  65 TRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:CHL00059  65 SSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIG 139
atpB CHL00060
ATP synthase CF1 beta subunit
 60-113 7.50e-11

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 58.51  E-value: 7.50e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 532165038  60 GLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAP 113
Cdd:CHL00060  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP 133
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 73-138 1.28e-10

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: 57.23  E-value: 1.28e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532165038  73 PLAVPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTL 138
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTL 66
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 76-133 6.06e-09

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: 52.61  E-value: 6.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 532165038  76 VPVGPALLGRVLDGLGEPSDGQGAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVD 133
Cdd:cd01133    2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVD 59
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 3-72 5.16e-07

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: 44.23  E-value: 5.16e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532165038   3 YGKVVELVGIMLKVAGV-QVSLGEVCELRQRDG--TLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGR 72
Cdd:cd01426    1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
fliI PRK06793
flagellar protein export ATPase FliI;
18-139 1.00e-05

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 43.81  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038  18 GVQVSLGEVCELrqrdGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPALLGRVLDGLGEPSDGQ 97
Cdd:PRK06793  37 GPKAKIGDVCFV----GEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEE 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 532165038  98 GAIACDTWIPIQAQAPDPMRRRLIEQPMPTGVRIVDGLMTLG 139
Cdd:PRK06793 113 AENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIG 154
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 4-93 1.23e-03

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 37.69  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532165038    4 GKVVELVGIMLKVAGVQ-VSLGEVCelrqRDGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLGRPLAVPVGPAL 82
Cdd:PRK14698    5 GRIIRVTGPLVIADGMKgAKMYEVV----RVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGL 80

                          90
                  ....*....|.
gi 532165038   83 LGRVLDGLGEP 93
Cdd:PRK14698   81 LTSIYDGIQRP 91
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 6-71 5.77e-03

ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 33.67  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532165038    6 VVELVGIMLKVA-GVQVSLGEVCELRQR--DGTLLQRAEVVGFSRDLALLAPFGELVGLSRETRVIGLG 71
Cdd:pfam02874   1 IVQVIGPVVDVEfGIGRLPGLLNALEVElvEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
 
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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