|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
1-577 |
0e+00 |
|
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440769 [Multi-domain] Cd Length: 583 Bit Score: 1124.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 1 MIQGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGML 80
Cdd:COG1155 2 MTKGKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLERIREKTGIYITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEF-GFTHKILVPPDVRGRVKE 159
Cdd:COG1155 82 GNIFDGIQRPLDKIAEKSGDFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQETpLIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 160 VKPAGEYTVEEPVVVLEDGT----ELKMYHTWPVRRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKT 235
Cdd:COG1155 162 IAPEGEYTVEDTIAVLEDEDgeehELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 236 VTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRD 315
Cdd:COG1155 242 VTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 316 QGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLGGEEGAVTIVGAVSPPGGDMSEPV 395
Cdd:COG1155 322 MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 396 TQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPELRDAISELLQREAGLQEIVQLVGPDA 475
Cdd:COG1155 402 TQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVDPDWSELRNEAMDLLQEEAELQEIVRLVGEDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 476 LQDAERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGRARYVS 555
Cdd:COG1155 482 LPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKELPLREKIARMKYSP 561
|
570 580
....*....|....*....|..
3J0J_C 556 EEEFPAYFEEAMKEIQGAFKAL 577
Cdd:COG1155 562 ENELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-577 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 1109.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 1 MIQGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGML 80
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLERIREKTGIYITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFG-FTHKILVPPDVRGRVKE 159
Cdd:PRK04192 82 GSIFDGIQRPLDELAEKSGDFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQETPsIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 160 VKPAGEYTVEEPVVVLED----GTELKMYHTWPVRRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKT 235
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLEDedgeGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 236 VTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRD 315
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 316 QGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLGGEEGAVTIVGAVSPPGGDMSEPV 395
Cdd:PRK04192 322 MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 396 TQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPELRDAISELLQREAGLQEIVQLVGPDA 475
Cdd:PRK04192 402 TQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 476 LQDAERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGRARYVS 555
Cdd:PRK04192 482 LPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILELEVRDRIARLKYIP 561
|
570 580
....*....|....*....|..
3J0J_C 556 EEEFPAYFEEAMKEIQGAFKAL 577
Cdd:PRK04192 562 ENEYLEKIDEIFEKLEEELEEL 583
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
4-575 |
0e+00 |
|
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130115 [Multi-domain] Cd Length: 578 Bit Score: 957.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGI 83
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 84 YDGIQRPLERIREKTGIYITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFG-FTHKILVPPDVRGRVKEVKP 162
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGDFIARGVDAPGLDRDKKWHFKPTVKEGDKVEGGDIIGVVPETSlIEHKILVPPNVEGEIVEIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 163 AGEYTVEEPVVVLE-DG-TELKMYHTWPVRRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQS 240
Cdd:TIGR01043 162 EGDYTVEDTIAVVDtDGdEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVTQHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 241 LAKWSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSV 320
Cdd:TIGR01043 242 LAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 321 ALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLGGEE--GAVTIVGAVSPPGGDMSEPVTQS 398
Cdd:TIGR01043 322 ALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEErvGSVTVIGAVSPPGGDFSEPVTQN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 399 TLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPELRDAISELLQREAGLQEIVQLVGPDALQD 478
Cdd:TIGR01043 402 TLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLVGPDALPE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 479 AERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGRARYVSEEE 558
Cdd:TIGR01043 482 RQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKLEVKEEIGRMKYEPDND 561
|
570
....*....|....*..
3J0J_C 559 FPAYFEEAMKEIQGAFK 575
Cdd:TIGR01043 562 ILAKIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
70-431 |
0e+00 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. 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.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 566.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 70 PLAVELGPGMLNGIYDGIQRPLERIREKTGIYITRGVvvhaldrekkwawtpmvkpgdevrggmvlgtvpefgfthkilv 149
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPRGV------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 150 ppdvrgrvkevkpageytveepvvvledgtelkMYHTWPVRRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGP 229
Cdd:cd01134 38 ---------------------------------NVQRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGP 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 230 FGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTI 309
Cdd:cd01134 85 FGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 310 AEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLG--GEEGAVTIVGAVSPP 387
Cdd:cd01134 165 AEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGspGREGSVTIVGAVSPP 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....
3J0J_C 388 GGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLF 431
Cdd:cd01134 245 GGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
235-553 |
7.95e-149 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 454.48 E-value: 7.95e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 235 TVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFR 314
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 315 DQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLGGEE--GAVTIVGAVSPPGGDMS 392
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYrvGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 393 EPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPELRDAISELLQREAGLQEIVQLVG 472
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVG 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 473 PDALQDAERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGRAR 552
Cdd:PRK14698 910 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLPVREEIGRMK 989
|
.
3J0J_C 553 Y 553
Cdd:PRK14698 990 F 990
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
208-429 |
2.32e-99 |
|
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: 300.43 E-value: 2.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 208 GMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPEltdpktgGPLMHRTVL 287
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG-------SGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 288 IANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGK 367
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
3J0J_C 368 VItlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYS 429
Cdd:pfam00006 154 VK---GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
146-430 |
2.43e-93 |
|
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: 287.04 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 146 KILVPPDVRGRVKEVkpageytVEEPvvvLEDGTELKMYHTWPVRRARP--VQRkLDPNTPFLTGMRILDVLFPVAMGGT 223
Cdd:cd19476 1 SVPVGPELLGRILDG-------LGEP---LDGLPPIKTKQRRPIHLKAPnpIER-LPPEEPLQTGIKVIDLLAPYGRGQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 224 AAIPGPFGSGKTVTQQSLAKWS---NADVVVYVGCGERGNEMTDVLVEFPELTDpktggplMHRTVLIANTSNMPVAARE 300
Cdd:cd19476 70 IGIFGGSGVGKTVLAMQLARNQakaHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 301 ASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVITLGgeeGAVTI 380
Cdd:cd19476 143 RVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGG---GSITA 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
3J0J_C 381 VGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSL 430
Cdd:cd19476 220 IPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
3-241 |
9.46e-86 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 287.30 E-value: 9.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 3 QGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGMLNG 82
Cdd:PRK14698 4 KGRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 83 IYDGIQRPLERIREKTGIYITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFG-FTHKILVPPDVRGRVKEVK 161
Cdd:PRK14698 84 IYDGIQRPLEVIREKSGDFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVPETSiITHKIMVPPGIEGEIVEIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 162 PAGEYTVEEPVVVLEDGT----ELKMYHTWPVRRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVT 237
Cdd:PRK14698 164 DEGEYTIEEVIAKVKTPSgeikELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVD 243
|
....
3J0J_C 238 QQSL 241
Cdd:PRK14698 244 GDTL 247
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
84-199 |
3.62e-65 |
|
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.
Pssm-ID: 465299 [Multi-domain] Cd Length: 120 Bit Score: 208.41 E-value: 3.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 84 YDGIQRPLERIREKTGIYITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFGF-THKILVPPDVRGRVKEVKP 162
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGSFIPRGVDVPALDREKKWEFTPTVKVGDKVSGGDILGTVQETSLiEHKIMVPPGVSGTVTEIAP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
3J0J_C 163 AGEYTVEEPVVVLEDG---TELKMYHTWPVRRARPVQRKL 199
Cdd:pfam16886 81 EGEYTVEDTIAEVEDEgkeKELTMMQKWPVRRPRPYKEKL 120
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
447-551 |
4.15e-58 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 189.14 E-value: 4.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 447 YPELRDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKMILAFYKEA 526
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*
3J0J_C 527 EAAIKRGVSIDEILQLPVLERIGRA 551
Cdd:cd18111 81 LEALEKGVPLSKILELPVREKIARM 105
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
4-508 |
7.76e-48 |
|
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: 172.50 E-value: 7.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKGmLGARMYDICKV---GEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGML 80
Cdd:TIGR02546 7 GRVTEVSGTLLKAVL-PGARVGELCLIrrrDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRVGEALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLERIREKtgiyitrgvvvhaldrekkwawtpmvkPGDEVRGGMVLGTvpefgfthkilvPPDvrgrvkev 160
Cdd:TIGR02546 86 GRVLDGFGRPLDGKGEL---------------------------PAGEIETRPLDAD------------PPP-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 161 kpageytveepvvvledgtelkmyhtwPVRRaRPVQRkldpntPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQS 240
Cdd:TIGR02546 119 ---------------------------PMSR-QPIDQ------PLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKSTLLGM 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 241 LAKWSNADVVVYVGCGERGNEMTdvlvEFPELTdpkTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSV 320
Cdd:TIGR02546 165 IARGASADVNVIALIGERGREVR----EFIEHH---LGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRV 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 321 ALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQSTL 400
Cdd:TIGR02546 238 LLMMDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGN-----GEKGSITALYTVLVEGDDMNDPIADEVR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 401 RIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALdpwyrenVAEDYPELRDAISELLQREAGLQEIVQL----VGPDAl 476
Cdd:TIGR02546 313 SILDGHIVLSRALAERNHYPAIDVLASLSRVMSQV-------VSTEHRRAAGKLRRLLATYKEVELLIRLgeyqPGSDP- 384
|
490 500 510
....*....|....*....|....*....|..
3J0J_C 477 qDAERLVIEVGRIIRedFLQQNayheVDAYCS 508
Cdd:TIGR02546 385 -ETDDAIDKIDAIRA--FLRQS----TDEYSP 409
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
4-423 |
3.12e-44 |
|
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: 162.93 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKGmLGARMYDICKV----GEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGM 79
Cdd:TIGR01026 25 GRVTKVKGLLIEAVG-PQASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 80 LNGIYDGIQRPLErirEKTGIYitrgvvvhaldrekkwawtpmvkpgDEVRGGMVlgtvpefgfthkILVPPDvrgrvke 159
Cdd:TIGR01026 104 LGRVLDGLGKPID---GKGKFL-------------------------DNVETEGL------------ITAPIN------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 160 vkpageytveepvvvledgtelkmyhtwPVRRArPVQRKLDpntpflTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQ 239
Cdd:TIGR01026 137 ----------------------------PLKRA-PIREILS------TGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 240 SLAKWSNADVVVYVGCGERGNEMtdvlvefPELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFS 319
Cdd:TIGR01026 182 MIARNTEADVNVIALIGERGREV-------REFIEHDLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKD 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 320 VALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQST 399
Cdd:TIGR01026 255 VLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGA-----SGKGSITAFYTVLVEGDDMNEPIADSV 329
|
410 420
....*....|....*....|....
3J0J_C 400 LRIVGAFWRLDASLAFRRHFPAIN 423
Cdd:TIGR01026 330 RGILDGHIVLSRALAQRGHYPAID 353
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-445 |
2.06e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 155.36 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIaGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGI 83
Cdd:PRK06820 31 GPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 84 YDGIQRPLERIREKTGiyitrgvvvhaldrekkwAWTPMVKPgdevrggmvlgtvpefgfthkilvPPDvrgrvkevkpa 163
Cdd:PRK06820 110 LDGLGAPIDGGPPLTG------------------QWRELDCP------------------------PPS----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 164 geytveepvvvledgtelkmyhtwpvrrarPVQRKLdPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAK 243
Cdd:PRK06820 137 ------------------------------PLTRQP-IEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 244 WSNADVVVYVGCGERGNEMTdvlvEFPELT-DPKTggplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVAL 322
Cdd:PRK06820 186 DSAADVMVLALIGERGREVR----EFLEQVlTPEA----RARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 323 MADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRI 402
Cdd:PRK06820 258 MADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-----SDRGSITAFYTVLVEGDDMNEPVADEVRSL 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....
3J0J_C 403 VGAFWRLDASLAFRRHFPAINWNGSYS-LFTSALDPWYRENVAE 445
Cdd:PRK06820 333 LDGHIVLSRRLAGAGHYPAIDIAASVSrIMPQIVSAGQLAMAQK 376
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
146-423 |
3.98e-40 |
|
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: 146.94 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 146 KILVPPDVRGRVkeVKPAGEytveepvvVLEDGTELKMYHTWPVRRARP---VQRKLDpnTPFLTGMRILDVLFPVAMGG 222
Cdd:cd01136 1 SIPVGDGLLGRV--IDALGE--------PLDGKGLPDEPERRPLIAAPPnplKRAPIE--QPLPTGVRAIDGLLTCGEGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 223 TAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEmtdvLVEFPELTdpkTGGPLMHRTVLIANTSNMPVAAREAS 302
Cdd:cd01136 69 RIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE----VREFIEKD---LGEEGLKRSVLVVATSDESPLLRVRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 303 IYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVG 382
Cdd:cd01136 142 AYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN-----GEKGSITAFY 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
3J0J_C 383 AVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAIN 423
Cdd:cd01136 217 TVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAID 257
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
2-520 |
8.36e-40 |
|
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: 150.57 E-value: 8.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 2 IQGVIQKIAGPAVIAKGmLGARMYDICKV---GEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPG 78
Cdd:COG1157 19 VSGRVTRVVGLLIEAVG-PDASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 79 MLngiydgiqrplerirektgiyitrgvvvhaldrekkwawtpmvkpgdevrggmvlgtvpefgfthkilvppdvrGRVk 158
Cdd:COG1157 98 LL--------------------------------------------------------------------------GRV- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 159 eVKPAGEytveepvvVLEDGTELKMYHTWPVRRAR--PVQRKldP-NTPFLTGMRILDVLFPVAMG---GTAAipGPfGS 232
Cdd:COG1157 103 -LDGLGR--------PLDGKGPLPGEERRPLDAPPpnPLERA--RiTEPLDTGVRAIDGLLTVGRGqriGIFA--GS-GV 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 233 GKTVTQQSLAKWSNADVVVyVG-CGERGNEMTdvlvEFPE--LtdpktGGPLMHRTVLIANTSNMPVAAREASIYVGVTI 309
Cdd:COG1157 169 GKSTLLGMIARNTEADVNV-IAlIGERGREVR----EFIEddL-----GEEGLARSVVVVATSDEPPLMRLRAAYTATAI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 310 AEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGG 389
Cdd:COG1157 239 AEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN-----GGKGSITAFYTVLVEGD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 390 DMSEPVTQsTLR------IVgafwrLDASLAFRRHFPAINWNGSYS-LFTSALDPWYRENVAedypELRDAISellqrea 462
Cdd:COG1157 314 DMNDPIAD-AVRgildghIV-----LSRKLAERGHYPAIDVLASISrVMPDIVSPEHRALAR----RLRRLLA------- 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3J0J_C 463 glqeivqlvgpdALQDAERLvIEVG-----------RIIR-----EDFLQQNayheVDAYCSMKKAYGIMKMIL 520
Cdd:COG1157 377 ------------RYEENEDL-IRIGayqpgsdpeldEAIAlipaiEAFLRQG----MDERVSFEESLAQLAELL 433
|
|
| FliI_clade3 |
TIGR03498 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
4-429 |
9.19e-40 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively.
Pssm-ID: 163293 [Multi-domain] Cd Length: 418 Bit Score: 150.15 E-value: 9.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKGMLG-ARMYDICKV---GEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGM 79
Cdd:TIGR03498 1 GRVTAVTGLLIEVRGLSRaVRLGDRCAIrarDGRPVLAEVVGFNGDRVLLMPFEPLEGVGLGCAVFAREGPLAVRPHPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 80 LngiydgiqrplerirektgiyitrGVVVHALdrekkwawtpmvkpGDEVRGGMVL--GTVPEFGFTHKIlvPPDVRGRV 157
Cdd:TIGR03498 81 L------------------------GRVINAL--------------GEPIDGKGPLpqGERRYPLRASPP--PAMSRARV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 158 KEvkpageytveepvvvledgtelkmyhtwpvrrarpvqrkldpntPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVT 237
Cdd:TIGR03498 121 GE--------------------------------------------PLDTGVRVIDTFLPLCRGQRLGIFAGSGVGKSTL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 238 QQSLAKWSNADVVVYVGCGERGNEmtdvLVEFPELTdpkTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQG 317
Cdd:TIGR03498 157 LSMLARNTDADVVVIALVGERGRE----VREFLEDD---LGEEGLKRSVVVVATSDESPLMRRQAAYTATAIAEYFRDQG 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 318 FSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVItlgGEEGAVTIVGAVSPPGGDMSEPVTQ 397
Cdd:TIGR03498 230 KDVLLLMDSVTRFAMAQREIGLAAGEPPVARGYTPSVFSELPRLLERAGPGA---EGKGSITGIFTVLVDGDDHNEPVAD 306
|
410 420 430
....*....|....*....|....*....|..
3J0J_C 398 STLRIVGAFWRLDASLAFRRHFPAINWNGSYS 429
Cdd:TIGR03498 307 AVRGILDGHIVLDRAIAERGRYPAINVLASVS 338
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
4-455 |
4.97e-37 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 142.23 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKGmLGARMYDICKV-GEEGLV--GEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGML 80
Cdd:TIGR03496 1 GRVTRVVGLVLEAVG-LRAPVGSRCEIeSSDGDPieAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLERirektgiyitRGvvvhALDREKKWAwtpmvkpgdevrggmvLGTVPefgfthkilVPPDVRGRVKEv 160
Cdd:TIGR03496 80 GRVIDGLGRPLDG----------KG----PLDAGERVP----------------LYAPP---------INPLKRAPIDE- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 161 kpageytveepvvvledgtelkmyhtwpvrrarpvqrkldpntPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQS 240
Cdd:TIGR03496 120 -------------------------------------------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGM 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 241 LAKWSNADVVVyVG-CGERGNEmtdvLVEFPELTDPKTGgplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFS 319
Cdd:TIGR03496 157 MARYTEADVVV-VGlIGERGRE----VKEFIEDILGEEG---LARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 320 VALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVG--AVSPPGGDMSEPV-- 395
Cdd:TIGR03496 229 VLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAfyTVLVEGDDQQDPIad 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 396 -TQSTL--RIVgafwrLDASLAFRRHFPAINWNGSYS-LFTSALDPWYRENVAE------DYPELRDAIS 455
Cdd:TIGR03496 304 aARAILdgHIV-----LSRELAEQGHYPAIDILASISrVMPDVVSPEHRQAARRfkqllsRYQENRDLIS 368
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
142-423 |
1.47e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 138.73 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 142 GFTHKILVPPDVRGRVKEvkpageyTVEEPVvvleDGTELKMYHTW-PVRRA--RPVQRKLdPNTPFLTGMRILDVLFPV 218
Cdd:PRK06936 92 GTMHQVGVGEHLLGRVLD-------GLGQPF----DGGHPPEPAAWyPVYADapAPMSRRL-IETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 219 AMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlvEFPEltdPKTGGPLMHRTVLIANTSNMPVAA 298
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVR----EFIE---SDLGEEGLRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 299 REASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAV 378
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-----SDKGSI 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3J0J_C 379 TIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAIN 423
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAID 352
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
129-498 |
1.13e-34 |
|
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: 136.39 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 129 VRGGMVLGTvpefgfTHKILVP--PDVRGRVKEVkpageytVEEPVVVLEdgtELKMYHTWPVRRARPVQRKLDPNTPFL 206
Cdd:TIGR01039 64 VRGLEVIDT------GAPISVPvgKETLGRIFNV-------LGEPIDEKG---PIPAKERWPIHRKAPSFEEQSTKVEIL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 207 -TGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSL----AKwSNADVVVYVGCGERGNEMTDVLVEFPEltdpktgGPL 281
Cdd:TIGR01039 128 eTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-EHGGYSVFAGVGERTREGNDLYHEMKE-------SGV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 282 MHRTVLIANTSNMPVAAREASIYVGVTIAEYFRD-QGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAA 360
Cdd:TIGR01039 200 IDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 361 FYERagkvITlGGEEGAVTIVGAVSPPGGDMSEPVTQSTlrivgaFWRLDASLAFRRH------FPAINWNGSYSlftSA 434
Cdd:TIGR01039 280 LQER----IT-STKTGSITSVQAVYVPADDLTDPAPATT------FAHLDATTVLSRKiaelgiYPAVDPLDSTS---RL 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
3J0J_C 435 LDPwyrENVAEDYPELRDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIrEDFLQQN 498
Cdd:TIGR01039 346 LDP---SVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRI-QRFLSQP 405
|
|
| ATP-synt_V_A-type_alpha_N |
cd18119 |
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ... |
3-68 |
1.78e-34 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 124.56 E-value: 1.78e-34
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3J0J_C 3 QGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTG 68
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTG 66
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-478 |
2.28e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 129.30 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 4 GVIQKIAGPAVIAKgMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGI 83
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 84 YDGIQRPLErirektgiyitrgvvvhaldrekkwawtpmvkpgdevrgGMVLgtvpefgfthkilvpPDVrgrvkevkPA 163
Cdd:PRK07594 102 IDGFGRPLD---------------------------------------GREL---------------PDV--------CW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 164 GEYTVEEPvvvledgtelkmyhtwPVRRARPVQRkldpntPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAK 243
Cdd:PRK07594 120 KDYDAMPP----------------PAMVRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 244 WSNADVVVYVGCGERGNEMTdvlvEFPELTDPKTGgplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALM 323
Cdd:PRK07594 178 APDADSNVLVLIGERGREVR----EFIDFTLSEET---RKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 324 ADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIV 403
Cdd:PRK07594 251 ADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM-----GEKGSITAFYTVLVEGDDMNEPLADEVRSLL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 404 GAFWRLDASLAFRRHFPAINWNGSYS-LFTSALDPWYRENVAedypELRDAIS-----ELLQREAGLQEivqlvGPDALQ 477
Cdd:PRK07594 326 DGHIVLSRRLAERGHYPAIDVLATLSrVFPVVTSHEHRQLAA----ILRRCLAlyqevELLIRIGEYQR-----GVDTDT 396
|
.
3J0J_C 478 D 478
Cdd:PRK07594 397 D 397
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
190-497 |
2.27e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 126.26 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 190 RRARPVQRKLDPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlvef 269
Cdd:PRK08149 120 VAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVT------ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 270 pELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEG 349
Cdd:PRK08149 194 -EFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 350 YPPYLAARLAAFYERAGKVITlggeeGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYS 429
Cdd:PRK08149 273 YPASVFDSLPRLLERPGATLA-----GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVS 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3J0J_C 430 -LFTSALDPWYRENVAedypelrdAISELLQREAGLQEIVQL----VGPDALQD-AERLvievgRIIREDFLQQ 497
Cdd:PRK08149 348 rVFGQVTDPKHRQLAA--------AFRKLLTRLEELQLFIDLgeyrRGENADNDrAMDK-----RPALEAFLKQ 408
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
177-423 |
2.56e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 126.38 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 177 DGTEL-KMYHTWPVRRARPVQRKLDP-NTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVG 254
Cdd:PRK07721 112 DGSALpKGLAPVSTDQDPPNPLKRPPiREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 255 CGERGNEMTdvlvEFPEltdpKTGGPL-MHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEA 333
Cdd:PRK07721 192 IGERGREVR----EFIE----RDLGPEgLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 334 LREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASL 413
Cdd:PRK07721 264 QREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-----NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQL 338
|
250
....*....|
3J0J_C 414 AFRRHFPAIN 423
Cdd:PRK07721 339 ANKGQYPAIN 348
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
194-497 |
1.01e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 116.02 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 194 PVQRKLdPNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlvEFPELT 273
Cdd:PRK09099 137 PMSRRM-VEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREVR----EFIELI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 274 DPKTGgplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPY 353
Cdd:PRK09099 212 LGEDG---MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 354 LAARLAAFYERAGKvitlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTS 433
Cdd:PRK09099 289 VFAELPRLLERAGM-----GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMP 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3J0J_C 434 ALdpwyrenVAEDYPELRDAISELLQREAGLQEIVQL----VGPDALQDAERLVIEVGRiireDFLQQ 497
Cdd:PRK09099 364 QV-------VPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADEAIAKIDAIR----DFLSQ 420
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
190-429 |
1.76e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 115.48 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 190 RRARpVQrkldpnTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEf 269
Cdd:PRK06002 141 TRAR-VE------TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 270 peltdpkTGGPLMHRTVLIANTSN-MPVAAREASIyVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEE 348
Cdd:PRK06002 213 -------TLADNLKKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVAR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 349 GYPPYLAARLAAFYERAGKvitlgGEEGAVTIVG--AVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNG 426
Cdd:PRK06002 285 GYPPSVFSELPRLLERAGP-----GAEGGGSITGifSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLA 359
|
...
3J0J_C 427 SYS 429
Cdd:PRK06002 360 SIS 362
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
162-497 |
2.43e-27 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 115.52 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 162 PAGEYTVE-------EPVVVLEDgteLKMYHTWPVRRARPVQRKLDPN-TPFLTGMRILDVLFPVAMGGTAAIPGPFGSG 233
Cdd:CHL00060 97 PVGGATLGrifnvlgEPVDNLGP---VDTRTTSPIHRSAPAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 234 KTVTQQSL----AKwSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAAReasIYVG--- 306
Cdd:CHL00060 174 KTVLIMELinniAK-AHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGAR---MRVGlta 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 307 VTIAEYFRDQGFS-VALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERagkvITlGGEEGAVTIVGAVS 385
Cdd:CHL00060 250 LTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSIQAVY 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 386 PPGGDMSEPVTQSTlrivgaFWRLDAS------LAFRRHFPAINWNGSYSLFtsaLDPWYrenVAEDYPELRDAISELLQ 459
Cdd:CHL00060 325 VPADDLTDPAPATT------FAHLDATtvlsrgLAAKGIYPAVDPLDSTSTM---LQPRI---VGEEHYETAQRVKQTLQ 392
|
330 340 350
....*....|....*....|....*....|....*...
3J0J_C 460 REAGLQEIVQLVGPDALQDAERLVIEVGRIIrEDFLQQ 497
Cdd:CHL00060 393 RYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 429
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
188-429 |
2.89e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.80 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 188 PVRRaRPVQRKLDpntpflTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVyVG-CGERGNEMTdvl 266
Cdd:PRK08972 136 PLSR-RPITEPLD------VGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIV-VGlVGERGREVK--- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 267 vEFPELTDPKTGgplMHRTVLIA---NTSN-MPVAAREASiyvgVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLE 342
Cdd:PRK08972 205 -EFIEEILGEEG---RARSVVVAapaDTSPlMRLKGCETA----TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 343 EMPAEEGYPPYLAARLAAFYERAGKvitlGGE-EGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPA 421
Cdd:PRK08972 277 EPPATKGYPPSVFAKLPALVERAGN----GGPgQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPA 352
|
....*...
3J0J_C 422 INWNGSYS 429
Cdd:PRK08972 353 IDIEASIS 360
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
191-423 |
6.68e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 113.54 E-value: 6.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 191 RARpVQRKLDpntpflTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlvEFP 270
Cdd:PRK08927 135 RAR-VGEPLD------LGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQ----EFL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 271 ELTDPKTGgplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGY 350
Cdd:PRK08927 204 QDDLGPEG---LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGY 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3J0J_C 351 PPYLAARLAAFYERAGKvitlgGEEGAVTIVG--AVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAIN 423
Cdd:PRK08927 281 TPTVFAELPRLLERAGP-----GPIGEGTITGlfTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAIN 350
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
146-437 |
5.60e-26 |
|
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: 107.69 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 146 KILVPPDVRGRVKEVkpageytVEEPVvvlEDGTELKMYHTWPVRRARPVQRKLDP-NTPFLTGMRILDVLFPVAMGGTA 224
Cdd:cd01133 1 SVPVGEETLGRIFNV-------LGEPI---DERGPIKAKERWPIHREAPEFVELSTeQEILETGIKVVDLLAPYAKGGKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 225 AIPGPFGSGKTVTQQSL----AKwSNADVVVYVGCGERGNEMTDVLVEFPELTDPKTGGplMHRTVLIANTSNMPVAARE 300
Cdd:cd01133 71 GLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 301 ASIYVGVTIAEYFRDQ-GFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERagkvITlGGEEGAVT 379
Cdd:cd01133 148 RVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER----IT-STKKGSIT 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
3J0J_C 380 IVGAVSPPGGDMSEPVTQSTlrivgaFWRLDASLAFRRH------FPAINWNGSYSlftSALDP 437
Cdd:cd01133 223 SVQAVYVPADDLTDPAPATT------FAHLDATTVLSRGiaelgiYPAVDPLDSTS---RILDP 277
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
194-435 |
3.40e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 108.72 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 194 PVQRKldPNTPFL-TGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDvlveFPEL 272
Cdd:PRK07960 149 PLQRT--PIEHVLdTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKD----FIEN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 273 TDPKTGgplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPP 352
Cdd:PRK07960 223 ILGAEG---RARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 353 YLAARLAAFYERAGKVITLGgeeGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFT 432
Cdd:PRK07960 300 SVFAKLPALVERAGNGISGG---GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
|
...
3J0J_C 433 SAL 435
Cdd:PRK07960 377 TAL 379
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
145-498 |
1.09e-22 |
|
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: 101.32 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 145 HKILVP--PDVRGRVKEVkpageytVEEPVvvlEDGTELKMYHTWPVRRARPVQRKLDPNT-PFLTGMRILDVLFPVAMG 221
Cdd:COG0055 77 APISVPvgEATLGRIFNV-------LGEPI---DGKGPIEAKERRPIHRPAPPFEEQSTKTeILETGIKVIDLLAPYAKG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 222 GTAAIPGPFGSGKTVTQQSL----AKWSNAdVVVYVGCGERGNEMTDVLVEFPEltdpkTGgpLMHRTVLIANTSNMPVA 297
Cdd:COG0055 147 GKIGLFGGAGVGKTVLIMELihniAKEHGG-VSVFAGVGERTREGNDLYREMKE-----SG--VLDKTALVFGQMNEPPG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 298 AREASIYVGVTIAEYFRD-QGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERagkvITlGGEEG 376
Cdd:COG0055 219 ARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQER----IT-STKKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 377 AVTIVGAVSPPGGDMSEPVTQSTlrivgaFWRLDASLAFRRH------FPAINWNGSYSlftSALDPWYrenVAEDYPEL 450
Cdd:COG0055 294 SITSVQAVYVPADDLTDPAPATT------FAHLDATTVLSRKiaelgiYPAVDPLDSTS---RILDPLI---VGEEHYRV 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
3J0J_C 451 RDAISELLQREAGLQEIVQLVGPDALQDAERLVieVGR---IIRedFLQQN 498
Cdd:COG0055 362 AREVQRILQRYKELQDIIAILGMDELSEEDKLT--VARarkIQR--FLSQP 408
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
188-429 |
1.14e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 100.96 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 188 PVRRArPVQRKLDpntpflTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlv 267
Cdd:PRK05688 142 PLNRH-PISEPLD------VGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVK---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 268 efpELTDPKTGGPLMHRTVLIANTSN-MPVAAREASIYVgVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPA 346
Cdd:PRK05688 211 ---EFIEHILGEEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 347 EEGYPPYLAARLAAFYERAGKvitlgGEE--GAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINW 424
Cdd:PRK05688 287 TKGYPPSVFAKLPKLVERAGN-----AEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDI 361
|
....*
3J0J_C 425 NGSYS 429
Cdd:PRK05688 362 EASIS 366
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
147-398 |
1.74e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 100.14 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 147 ILVPPDVRGRVkeVKPAGEytveepvvVLEDGTELKMYHTWPVRRA--RPVQRKLdPNTPFLTGMRILDVLFPVAMGGTA 224
Cdd:PRK08472 92 IPVGRNLLGRV--VDPLGR--------PIDGKGAIDYERYAPIMKApiAAMKRGL-IDEVFSVGVKSIDGLLTCGKGQKL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 225 AIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMtdvlvefPELTDPKTGGPLmHRTVLIANTSNMPVAAREASIY 304
Cdd:PRK08472 161 GIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREI-------PEFIEKNLGGDL-ENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 305 VGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKvitlggEE--GAVTIVG 382
Cdd:PRK08472 233 CAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK------EEgkGSITAFF 306
|
250
....*....|....*..
3J0J_C 383 AVSPPGGDMSEPVT-QS 398
Cdd:PRK08472 307 TVLVEGDDMSDPIAdQS 323
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
6-500 |
1.81e-21 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 97.52 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 6 IQKIAGPAVIAKGMLGARMYDICKV----GEEGLvGEIIRLDGDTAFVQVYEDTSGLKVGEPVVS-TGLPLAVELGPGML 80
Cdd:COG1156 9 ISEIAGPLLFVEGVEGVGYGELVEIelpdGERRR-GQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLErirektgiyitrgvvvhaldrekkwawtpmvkpgdevrGGmvlgtvPEfgfthkilVPPDVRGRVkev 160
Cdd:COG1156 88 GRVFNGLGRPID--------------------------------------GG------PP--------IIPEKRLDI--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 161 kpageytveepvvvleDGTELKmyhtwPVRRARPvqrkldpNTPFLTGMRILDVLFPVAMGGTAAIpgpF-GSG------ 233
Cdd:COG1156 113 ----------------NGSPIN-----PVAREYP-------REFIQTGISAIDGLNTLVRGQKLPI---FsGSGlphnel 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 234 --KTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPEltdpkTGGplMHRTVLIANTSNMPVAAREASIYVGVTIAE 311
Cdd:COG1156 162 aaQIARQAKVRGEEEKFAVVFAAMGITHDEANFFREEFEE-----TGA--LDRVVMFLNLADDPAIERIITPRMALTAAE 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 312 YFR-DQGFSV-ALMADSTSrWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVItlgGEEGAVTIVGAVSPPGG 389
Cdd:COG1156 235 YLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK---GRKGSITQIPILTMPND 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 390 DMSEPV-------TQStlRIVgafwrLDASLAFRRHFPAINWNGSYS-LFTSALDPWY-RenvaEDYPELRDAISELLQR 460
Cdd:COG1156 311 DITHPIpdltgyiTEG--QIV-----LSRDLHRKGIYPPIDVLPSLSrLMKDGIGEGKtR----EDHADVANQLYAAYAR 379
|
490 500 510 520
....*....|....*....|....*....|....*....|
3J0J_C 461 EAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAY 500
Cdd:COG1156 380 GQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFD 419
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
205-458 |
1.81e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 97.36 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 205 FLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEfpELtdpktGGPLMHR 284
Cdd:PRK06793 140 FETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--EL-----GEEGMRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 285 TVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAeEGYPPYLAARLAAFYER 364
Cdd:PRK06793 213 SVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLER 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 365 AGKVitlggEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYSLFTsaldpwyRENVA 444
Cdd:PRK06793 292 SGKT-----QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM-------EEIVS 359
|
250
....*....|....
3J0J_C 445 EDYPELRDAISELL 458
Cdd:PRK06793 360 PNHWQLANEMRKIL 373
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
188-501 |
3.32e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 96.50 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 188 PVRRaRPVqrkldpNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTdvlv 267
Cdd:PRK07196 129 PLQR-RAV------DTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVK---- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 268 efpELTDPKTGGPLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAE 347
Cdd:PRK07196 198 ---EFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPAT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 348 EGYPPYLAARLAAFYERAGKvitlGGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGS 427
Cdd:PRK07196 275 KGYPPSAFSIIPRLAESAGN----SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQS 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3J0J_C 428 YSLFTSALdpwyrenVAEDYPELRDAISELLQREAGLQEIVQLVG--PDALQDAERLVIEVGRIirEDFLQQNAYH 501
Cdd:PRK07196 351 ISRCMSQV-------IGSQQAKAASLLKQCYADYMAIKPLIPLGGyvAGADPMADQAVHYYPAI--TQFLRQEVGH 417
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
194-429 |
1.35e-20 |
|
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: 92.29 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 194 PVQRKLdPNTPFLTGMRILDVLFPVAMGgtAAIPGPFGSG--------KTVTQQSLAKWSNADVVVYVGCGergneMTDV 265
Cdd:cd01135 43 PVARIY-PEEMIQTGISAIDVMNTLVRG--QKLPIFSGSGlphnelaaQIARQAGVVGSEENFAIVFAAMG-----VTME 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 266 LVEFPELTDPKTGGplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFR-DQGFSV-ALMADSTSrWAEALREISSRLEE 343
Cdd:cd01135 115 EARFFKDDFEETGA--LERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVlVILTDMTN-YAEALREVSAAREE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 344 MPAEEGYPPYLAARLAAFYERAGKVItlgGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAIN 423
Cdd:cd01135 192 VPGRRGYPGYMYTDLATIYERAGRVE---GRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPID 268
|
....*.
3J0J_C 424 WNGSYS 429
Cdd:cd01135 269 VLPSLS 274
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
205-384 |
1.41e-20 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 94.59 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 205 FLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPEltdpktgGPLMHR 284
Cdd:PRK05922 141 FPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKE-------GLAAQR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 285 TVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAAFYER 364
Cdd:PRK05922 214 TIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTER 293
|
170 180
....*....|....*....|
3J0J_C 365 AGKvitlgGEEGAVTIVGAV 384
Cdd:PRK05922 294 AGN-----NDKGSITALYAI 308
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
6-497 |
1.63e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 94.51 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 6 IQKIAGPAVIAKGMLGARMYDICKV----GEEgLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVS-TGLPLAVELGPGML 80
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGEIVEIelpnGEK-RRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 81 NGIYDGIQRPLERIrektgiyitrgvvvhaldrekkwawtPMVKPGDEVrggmvlgtvpefgfthkilvppDVRGrvkev 160
Cdd:PRK04196 86 GRIFDGLGRPIDGG--------------------------PEIIPEKRL----------------------DING----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 161 kpageytveEPVVvledgtelkmyhtwPVRRARP---VQrkldpntpflTGMRILDVLFPVAMGGTAAIpgpF-GSG--- 233
Cdd:PRK04196 113 ---------APIN--------------PVAREYPeefIQ----------TGISAIDGLNTLVRGQKLPI---FsGSGlph 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 234 -----KTVTQQSLAKWSNADVVVYVGCGERGNEMTDVLVEFPEltdpkTGGplMHRTVLIANTSNMPVAAREASIYVGVT 308
Cdd:PRK04196 157 nelaaQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEE-----TGA--LERSVVFLNLADDPAIERILTPRMALT 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 309 IAEYFR-DQGFSV-ALMADSTSrWAEALREISSRLEEMPAEEGYPPYLAARLAAFYERAGKVItlgGEEGAVTIVGAVSP 386
Cdd:PRK04196 230 AAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK---GKKGSITQIPILTM 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 387 PGGDMSEPVTQST-----LRIVgafwrLDASLAFRRHFPAINWNGSYS-LFTSALDPWYREnvaEDYPELRDAISELLQR 460
Cdd:PRK04196 306 PDDDITHPIPDLTgyiteGQIV-----LSRELHRKGIYPPIDVLPSLSrLMKDGIGEGKTR---EDHKDVANQLYAAYAR 377
|
490 500 510
....*....|....*....|....*....|....*..
3J0J_C 461 EAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQ 497
Cdd:PRK04196 378 GKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
282-518 |
6.75e-17 |
|
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: 83.62 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 282 MHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQ-GFSVALMADSTSRWAEALREISSRLEEMPAEEGYPPYLAARLAA 360
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 361 FYERAGKVitlGGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNGSYS-LFTSALDpwy 439
Cdd:TIGR01040 290 IYERAGRV---EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSrLMKSAIG--- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 440 rENVA-EDYPELRDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAYHEVDAYCSMKKAYGIMKM 518
Cdd:TIGR01040 364 -EGMTrKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRI 442
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
202-392 |
1.08e-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: 68.74 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 202 NTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKT-VTQQSLAKWSNADVV-VYVGCGERGNEMTDVlVEFPELTDPktgg 279
Cdd:cd01132 50 NEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTIINQKGKKVYcIYVAIGQKRSTVAQI-VKTLEEHGA---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 280 plMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYP---PYLAA 356
Cdd:cd01132 125 --MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPgdvFYLHS 202
|
170 180 190
....*....|....*....|....*....|....*.
3J0J_C 357 RLaafYERAGKVITLGGeEGAVTIVGAVSPPGGDMS 392
Cdd:cd01132 203 RL---LERAAKLSDELG-GGSLTALPIIETQAGDVS 234
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
202-434 |
1.15e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.45 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 202 NTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKT------------VTQQSLAKwsNADVVVYVGCGERGNEMTDVLVEF 269
Cdd:PTZ00185 170 NYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqvrINQQILSK--NAVISIYVSIGQRCSNVARIHRLL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 270 peltdpKTGGPLMHRTVLIAnTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEG 349
Cdd:PTZ00185 248 ------RSYGALRYTTVMAA-TAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 350 YPP---YLAARLaafYERAGkVITLGGEEGAVTIVGAVSPPGGDMSEPVTQSTLRIVGAFWRLDASLAFRRHFPAINWNG 426
Cdd:PTZ00185 321 YPGdvfYLHSRL---LERAA-MLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGL 396
|
....*...
3J0J_C 427 SYSLFTSA 434
Cdd:PTZ00185 397 SVSRVGSS 404
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
126-368 |
1.27e-12 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 70.33 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 126 GDEVRGgmvLGTVPEfgfthkILVPPDVRGRVkeVKPAGEytveepvvVLEDGTELKMYHTWPVRRARP--VQRKLdPNT 203
Cdd:PRK13343 85 GTEVRR---TGRVLE------VPVGDGLLGRV--IDPLGR--------PLDGGGPLQATARRPLERPAPaiIERDF-VTE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 204 PFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTvtqqSLA-------KWSNAdVVVYVGCGERGN---EMTDVLVEFpelt 273
Cdd:PRK13343 145 PLQTGIKVVDALIPIGRGQRELIIGDRQTGKT----AIAidaiinqKDSDV-ICVYVAIGQKASavaRVIETLREH---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 274 dpktGGplMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPP- 352
Cdd:PRK13343 216 ----GA--LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGd 289
|
250
....*....|....*...
3J0J_C 353 --YLAARLaafYERAGKV 368
Cdd:PRK13343 290 ifYLHSRL---LERAAKL 304
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
34-399 |
3.11e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.91 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 34 GLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGIYDGIQRPLERirektgiyitrgvvvhaldr 113
Cdd:PRK02118 37 SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 114 ekkwawtpmvkpGDEVRGGMVlgtvpefgfthkilvppDVRGrvkevkpageytveePVVvledgtelkmyhtwpvrraR 193
Cdd:PRK02118 97 ------------GPELEGEPI-----------------EIGG---------------PSV-------------------N 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 194 PVQRKLdPNTPFLTGMRILDVL--------FPVAmggtaAIPG-PFgsgktvtQQSLAKWSN---ADVVVYVGCGERGNE 261
Cdd:PRK02118 114 PVKRIV-PREMIRTGIPMIDVFntlvesqkIPIF-----SVSGePY-------NALLARIALqaeADIIILGGMGLTFDD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 262 MTDVLVEFpeltdpKTGGpLMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFS--VALMADSTSrWAEALREISS 339
Cdd:PRK02118 181 YLFFKDTF------ENAG-ALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKkvLVLLTDMTN-FADALKEISI 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 340 RLEEMPAEEGYPPYLAARLAAFYERAgkVITLGGeeGAVTIVGAVSPPGGDMSEPVTQST 399
Cdd:PRK02118 253 TMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG--GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-68 |
7.79e-12 |
|
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: 60.64 E-value: 7.79e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3J0J_C 6 IQKIAGPAVIAKGMLGAR--MYDICKVG----EEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTG 68
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVElvefGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
203-392 |
1.13e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 67.30 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 203 TPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKT-VTQQSLAKWSNADVV-VYVGCGERGNEMTDVLVEFPEltdpktgGP 280
Cdd:CHL00059 123 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQNVIcVYVAIGQKASSVAQVVTTLQE-------RG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 281 LMHRTVLIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPP---YLAAR 357
Cdd:CHL00059 196 AMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSR 275
|
170 180 190
....*....|....*....|....*....|....*.
3J0J_C 358 LaafYERAGKVIT-LGgeEGAVTIVGAVSPPGGDMS 392
Cdd:CHL00059 276 L---LERAAKLSSqLG--EGSMTALPIVETQAGDVS 306
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-68 |
2.11e-10 |
|
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: 56.94 E-value: 2.11e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3J0J_C 3 QGVIQKIAGPAVIAKGMLGARMYDICKVG------EEGLVGEIIRLDGDTAFVQVYEDTSGLKVGEPVVSTG 68
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTG 72
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
449-500 |
1.25e-06 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of 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, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that 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: 349744 [Multi-domain] Cd Length: 70 Bit Score: 46.28 E-value: 1.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
3J0J_C 449 ELRDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREdFLQQNAY 500
Cdd:cd01429 3 AVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQF 53
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
304-373 |
1.57e-06 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 50.83 E-value: 1.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3J0J_C 304 YVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGYPP---YLAARLaafYERAGKVIT-LGG 373
Cdd:PRK09281 240 YAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDeLGG 310
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
6-58 |
8.12e-05 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349742 [Multi-domain] Cd Length: 72 Bit Score: 40.88 E-value: 8.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
3J0J_C 6 IQKIAGPAVIAKGMLGARMYDICKV----GEEGLvGEIIRLDGDTAFVQVYEDTSGL 58
Cdd:cd18118 5 VSEINGPLVIVEGVKGVKYGEIVEItlpdGEVRR-GQVLEVSGDKAVVQVFEGTSGL 60
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
209-427 |
4.49e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 39.68 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 209 MRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNAD------VVVYVgcGERGNEMTDvlvefpeltdpktggplM 282
Cdd:PRK12608 121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANhpevhlMVLLI--DERPEEVTD-----------------M 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3J0J_C 283 HRTV---LIANTSNMPVAAREASIYVGVTIAEYFRDQGFSVALMADSTSRWAEAL--------REISSRLEEMPAEEGYP 351
Cdd:PRK12608 182 RRSVkgeVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYnnevessgRTLSGGVDARALQRPKR 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3J0J_C 352 PYLAARLAAfyeragkvitlggEEGAVTIVG-AVSPPGGDMSEpVTQSTLRIVGAF-WRLDASLAFRRHFPAINWNGS 427
Cdd:PRK12608 262 LFGAARNIE-------------EGGSLTIIAtALVDTGSRMDE-VIFEEFKGTGNMeIVLDRELADKRVFPAIDIAKS 325
|
|
| |
