|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
1-581 |
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: 911.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 1 MLTKGTVKGIISNLVIVEVEGPVTQNEIAYIDHEgtRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGP 80
Cdd:COG1155 1 MMTKGKIVKINGPLVTAEGMGGAKMYEVVYVGEE--RLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 81 GLLQRNLDGLENDLDKM---DGVFLKRGEYTFPLDEEKLWHFKPIAKEGDKVRAGSWLGEVDEN-YQPHKIMVPFSMKGE 156
Cdd:COG1155 79 GLLGNIFDGIQRPLDKIaekSGDFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQETpLIEHKIMVPPGVSGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 157 yrIVRIIGEGDYNIYEKIAVVEDNEGNVTELNMIQRWPVKVPITeYSEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGA 236
Cdd:COG1155 159 --VKEIAPEGEYTVEDTIAVLEDEDGEEHELTMYQKWPVRRPRP-YKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 237 FGTGKTVLQHSISKQAEADIVIIAACGERANEVVEIFTEFPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTI 316
Cdd:COG1155 236 FGTGKTVTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 317 GEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVILNNGKEGSITFIGTVSPAGG 396
Cdd:COG1155 316 AEYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 397 NLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYFEypEFQDYISSEVSSDWVEKVSEIKTRLLRGKEIAEQ 476
Cdd:COG1155 396 DFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLD--DLAEWYDENVDPDWSELRNEAMDLLQEEAELQEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 477 INILGDDGVPVEYHITFWKSEFIDYIILQQDAFDDIDAVTSIERQKNILDLVTEVCRTKFEFEKFTEVADFFKE--LINI 554
Cdd:COG1155 474 VRLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKElpLREK 553
|
570 580
....*....|....*....|....*....
gi 769968640 555 GKQMNYSEFES--DSFYGYVNQLKEKISN 581
Cdd:COG1155 554 IARMKYSPENEllEKFDELEKEIDEEIEE 582
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-581 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 871.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 1 MLTKGTVKGIISNLVIVEVEGPVTQNEIAYIDHEgtRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGP 80
Cdd:PRK04192 1 MMTKGKIVRVSGPLVVAEGMGGARMYEVVRVGEE--GLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 81 GLLQRNLDGLENDLDKMD---GVFLKRGEYTFPLDEEKLWHFKPIAKEGDKVRAGSWLGEVDEN-YQPHKIMVPFSMKGE 156
Cdd:PRK04192 79 GLLGSIFDGIQRPLDELAeksGDFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQETpSIEHKIMVPPGVSGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 157 yrIVRIIGEGDYNIYEKIAVVEDNEGNVTELNMIQRWPVKVPITeYSEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGA 236
Cdd:PRK04192 159 --VKEIVSEGDYTVDDTIAVLEDEDGEGVELTMMQKWPVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 237 FGTGKTVLQHSISKQAEADIVIIAACGERANEVVEIFTEFPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTI 316
Cdd:PRK04192 236 FGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 317 GEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVILNNGKEGSITFIGTVSPAGG 396
Cdd:PRK04192 316 AEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 397 NLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYFEypEFQDYISSEVSSDWVEKVSEIKTRLLRGKEIAEQ 476
Cdd:PRK04192 396 DFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLD--QVAPWWEENVDPDWRELRDEAMDLLQREAELQEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 477 INILGDDGVPVEYHITFWKSEFIDYIILQQDAFDDIDAVTSIERQKNILDLVTEVCRTKFEFEKF---------TEVADF 547
Cdd:PRK04192 474 VRLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKgvpvseileLEVRDR 553
|
570 580 590
....*....|....*....|....*....|....
gi 769968640 548 FKELINIGKQMnYSEFESDSFYGYVNQLKEKISN 581
Cdd:PRK04192 554 IARLKYIPENE-YLEKIDEIFEKLEEELEELIAE 586
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
73-438 |
2.63e-152 |
|
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: 438.93 E-value: 2.63e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 73 MLEVVLGPGLLQRNLDGLENDLDKM---DGVFLKRGEYTfpldeeklwhfkpiakegdkvragswlgevdenyqphkimv 149
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIaetGSIFIPRGVNV----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 150 pfsmkgeyrivriigegdyniyekiavvednegnvtelnmiQRWPVKVPITeYSEKPRPYKLLETGVRSIDTLNPIVEGG 229
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 230 TGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVVEIFTEFPELVDPHTGRKLMERTIIVANTSNMPVAAREAS 309
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREAS 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 310 VYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVILNN--GKEGSITF 387
Cdd:cd01134 158 IYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGspGREGSVTI 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 769968640 388 IGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKY 438
Cdd:cd01134 238 VGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
215-436 |
3.39e-92 |
|
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: 282.32 E-value: 3.39e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 215 GVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVVEIFTEFPElvdphtgRKLMERTII 294
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG-------SGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 295 VANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGH 374
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769968640 375 VilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYS 436
Cdd:pfam00006 154 V---KGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
242-525 |
6.99e-77 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 263.42 E-value: 6.99e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 242 TVLQHSISKQAEADIVIIAACGERANEVVEIFTEFPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYR 321
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 322 SMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVIL--NNGKEGSITFIGTVSPAGGNLK 399
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgSDYRVGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 400 EPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYFEypEFQDYISSEVSSDWVEKVSEIKTRLLRGKEIAEQINI 479
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVD--AVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 769968640 480 LGDDGVPVEYHITFWKSEFIDYIILQQDAFDDIDAVTSIERQKNIL 525
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMM 953
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
186-438 |
2.12e-76 |
|
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: 243.52 E-value: 2.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 186 ELNMIQRWPVKVPITEYSEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSI---SKQAEADIVIIAAC 262
Cdd:cd19476 25 PIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLarnQAKAHAGVVVFAGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 263 GERANEVVEIFTEFPELvdphtgrKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALR 342
Cdd:cd19476 105 GERGREVNDLYEEFTKS-------GAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 343 EMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRAD 422
Cdd:cd19476 178 EMSALLGEPPGREGYPPYLFTKLATLYERAGKV---KDGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELAR 254
|
250
....*....|....*.
gi 769968640 423 KKRYPAINPIDSYSKY 438
Cdd:cd19476 255 KGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
88-210 |
6.96e-47 |
|
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: 160.26 E-value: 6.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 88 DGLENDLDKM---DGVFLKRGEYTFPLDEEKLWHFKPIAKEGDKVRAGSWLGEVDENYQ-PHKIMVPFSMKGEyrIVRII 163
Cdd:pfam16886 2 DGIQRPLEKIaekSGSFIPRGVDVPALDREKKWEFTPTVKVGDKVSGGDILGTVQETSLiEHKIMVPPGVSGT--VTEIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 769968640 164 GEGDYNIYEKIAVVEDnEGNVTELNMIQRWPVKvpiteyseKPRPYK 210
Cdd:pfam16886 80 PEGEYTVEDTIAEVED-EGKEKELTMMQKWPVR--------RPRPYK 117
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
1-284 |
1.21e-42 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 164.42 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 1 MLTKGTVKGIISNLVIVEVEGPVTQNEIAYIDHEGtrLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGP 80
Cdd:PRK14698 1 MPAKGRIIRVTGPLVIADGMKGAKMYEVVRVGELG--LIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 81 GLLQRNLDGLENDLD---KMDGVFLKRGEYTFPLDEEKLWHFKPIAKEGDKVRAGSWLGEVDE-NYQPHKIMVPFSMKGE 156
Cdd:PRK14698 79 GLLTSIYDGIQRPLEvirEKSGDFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVPEtSIITHKIMVPPGIEGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 157 yrIVRIIGEGDYNIYEKIAVVEDNEGNVTELNMIQRWPVKVPiTEYSEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGA 236
Cdd:PRK14698 159 --IVEIADEGEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVK-RPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 769968640 237 FGTGKTVLQHSISKQAEADIVIIAACGE----RANEVVEIFTEFPELVDPHT 284
Cdd:PRK14698 236 FGSGKCVDGDTLILTKEFGLIKIKDLYEildgKGKKTVEGNEEWTELEEPIT 287
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
191-437 |
3.98e-42 |
|
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: 152.33 E-value: 3.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 191 QRWPVKVPITEYSEKPRPYKLLETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTVLQHSISKQAEADIVIIAACGERANEV 269
Cdd:cd01136 30 ERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQrIGIFAGS-GVGKSTLLGMIARNTDADVNVIALIGERGREV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 270 VEiFTEFpelvdpHTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLE 349
Cdd:cd01136 109 RE-FIEK------DLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 350 ELPGPDAFPMDLSVVISNFYGRAGhvilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAI 429
Cdd:cd01136 182 EPPTRRGYPPSVFALLPRLLERAG-----NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAI 256
|
....*...
gi 769968640 430 NPIDSYSK 437
Cdd:cd01136 257 DVLASISR 264
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
5-436 |
3.02e-39 |
|
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: 149.03 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 5 GTVKGIISNLVivEVEGP-VTQNEIAYI-DHEGTRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGPGL 82
Cdd:COG1157 21 GRVTRVVGLLI--EAVGPdASIGELCEIeTADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 83 LQRNLDGLENDLDKMDGVflkRGEYTFPLDEEklwhfkPIAkegdkvragswlgevdenyqPHkimvpfsmkgeyrivri 162
Cdd:COG1157 99 LGRVLDGLGRPLDGKGPL---PGEERRPLDAP------PPN--------------------PL----------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 163 igegdyniyekiavvednegnvtelnmiQRWPVKVPiteysekprpyklLETGVRSIDTLNPIVEG-------GTGfipg 235
Cdd:COG1157 133 ----------------------------ERARITEP-------------LDTGVRAIDGLLTVGRGqrigifaGSG---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 236 afgTGKTVLQHSISKQAEADIVIIAACGERANEVveifTEFpelVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMT 315
Cdd:COG1157 168 ---VGKSTLLGMIARNTEADVNVIALIGERGREV----REF---IEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 316 IGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPG-----PDAFPMdlsvvISNFYGRAGhvilnNGKEGSITFIGT 390
Cdd:COG1157 238 IAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPAtrgypPSVFAL-----LPRLLERAG-----NGGKGSITAFYT 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 769968640 391 VSPAGGNLKEPVTENtkkvARcfyA-------LEQDRADKKRYPAINPIDSYS 436
Cdd:COG1157 308 VLVEGDDMNDPIADA----VR---GildghivLSRKLAERGHYPAIDVLASIS 353
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-437 |
3.30e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 149.19 E-value: 3.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 5 GTVKGIISNLVIVEVEGpVTQNEIAYIDHEGtrLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGPGLLQ 84
Cdd:PRK06820 31 GPIVEIGPTLLRASLPG-VAQGELCRIEPQG--MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 85 RNLDGLEndlDKMDGvflkrgeytFPLDEeklwhfkpiakegdkvragswlGEVDENYQPhkimVPfsmkgeyrivriig 164
Cdd:PRK06820 108 RILDGLG---APIDG---------GPPLT----------------------GQWRELDCP----PP-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 165 egdyniyekiavvednegnvtelNMIQRWPVKVPITeysekprpyklleTGVRSIDTLNPIVEGGTGFIPGAFGTGKTVL 244
Cdd:PRK06820 136 -----------------------SPLTRQPIEQMLT-------------TGIRAIDGILSCGEGQRIGIFAAAGVGKSTL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 245 QHSISKQAEADIVIIAACGERANEVveifTEFPELVDPHTGRklmERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMG 324
Cdd:PRK06820 180 LGMLCADSAADVMVLALIGERGREV----REFLEQVLTPEAR---ARTVVVVATSDRPALERLKGLSTATTIAEYFRDRG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 325 LKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGhvilnNGKEGSITFIGTVSPAGGNLKEPVTE 404
Cdd:PRK06820 253 KKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-----NSDRGSITAFYTVLVEGDDMNEPVAD 327
|
410 420 430
....*....|....*....|....*....|...
gi 769968640 405 NTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK06820 328 EVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSR 360
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
5-437 |
1.56e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 127.15 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 5 GTVKGIISnlVIVEVEGPVTQ-NEIAYIdHEGTR----LMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLG 79
Cdd:PRK07721 20 GKVSRVIG--LMIESKGPESSiGDVCYI-HTKGGgdkaIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 80 PGLLQRNLDGLENDLDkmdGVFLKRGEYTFPLDEEKlwhfkpiakegdkvragswlgevdenyqphkimvPfsmkgeyri 159
Cdd:PRK07721 97 SGLIGQVLDALGEPLD---GSALPKGLAPVSTDQDP----------------------------------P--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 160 vriigegdyniyekiavvednegnvtelNMIQRWPVKVPiteysekprpyklLETGVRSIDTLNPIvegGTGFIPGAF-- 237
Cdd:PRK07721 131 ----------------------------NPLKRPPIREP-------------MEVGVRAIDSLLTV---GKGQRVGIFag 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 238 -GTGKTVLQHSISKQAEADIVIIAACGERANEVveiftefPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTI 316
Cdd:PRK07721 167 sGVGKSTLMGMIARNTSADLNVIALIGERGREV-------REFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 317 GEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGhvilNNGKeGSITFIGTVSPAGG 396
Cdd:PRK07721 240 AEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNAS-GSITAFYTVLVDGD 314
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 769968640 397 NLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
191-437 |
1.51e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 124.48 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 191 QRWPVkvpiteYSEKPRPY--KLLET----GVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGE 264
Cdd:PRK06936 125 AWYPV------YADAPAPMsrRLIETplslGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 265 RANEVveiftefPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREM 344
Cdd:PRK06936 199 RGREV-------REFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 345 SNRLEELPGPDAFPMDLSVVISNFYGRAGhvilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKK 424
Cdd:PRK06936 272 GLAAGEPPTRRGYPPSVFAALPRLMERAG-----QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAAN 346
|
250
....*....|...
gi 769968640 425 RYPAINPIDSYSK 437
Cdd:PRK06936 347 HYPAIDVLRSASR 359
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
212-437 |
2.54e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 114.87 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 212 LETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVveifTEFPELVdphTGRKLMER 291
Cdd:PRK09099 147 LPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGREV----REFIELI---LGEDGMAR 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 292 TIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGR 371
Cdd:PRK09099 220 SVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769968640 372 AGHvilnnGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK09099 300 AGM-----GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSR 360
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
39-439 |
8.19e-27 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 113.51 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 39 MAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGPGLLQRNLDGLENDLDKMDgvflkrgeytfplDEEKLWh 118
Cdd:PRK07594 54 LAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE-------------LPDVCW- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 119 fkpiaKEGDKvragswlgevdenyqphkiMVPFSMkgeyrivriigegdyniyekiavvednegnvtelnmiqrwpVKVP 198
Cdd:PRK07594 120 -----KDYDA-------------------MPPPAM-----------------------------------------VRQP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 199 ITeysekpRPyklLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVveifTEFPE 278
Cdd:PRK07594 135 IT------QP---LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREV----REFID 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 279 LVDPHTGRKlmeRTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFP 358
Cdd:PRK07594 202 FTLSEETRK---RCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 359 MDLSVVISNFYGRAGHvilnnGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKY 438
Cdd:PRK07594 279 PGVFSALPRLLERTGM-----GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRV 353
|
.
gi 769968640 439 F 439
Cdd:PRK07594 354 F 354
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
184-439 |
1.14e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 112.78 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 184 VTELNMIQRWPVKVPITEYSEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACG 263
Cdd:PRK08149 107 PTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 264 ERANEVveifTEFPELVDpHTGRKlmERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALRE 343
Cdd:PRK08149 187 ERGREV----TEFVESLR-ASSRR--EKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 344 MSNRLEELPGPDAFPMDLSVVISNFYGRAGhvilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADK 423
Cdd:PRK08149 260 VALAAGELPARRGYPASVFDSLPRLLERPG-----ATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAK 334
|
250
....*....|....*.
gi 769968640 424 KRYPAINPIDSYSKYF 439
Cdd:PRK08149 335 GHYPAIDVLKSVSRVF 350
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
124-440 |
6.99e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 110.45 E-value: 6.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 124 KEGDKVRAGSWLGEVDEnyqphKIMVPfsmKGEYRIVRII-GEGDyniyekiaVVEDNEGNVTelnmIQRWPVKVPITEY 202
Cdd:PRK06793 71 EQTEKVCYGDSVTLIAE-----DVVIP---RGNHLLGKVLsANGE--------VLNEEAENIP----LQKIKLDAPPIHA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 203 SEKPRPYKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVveiftefPELVDP 282
Cdd:PRK06793 131 FEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV-------KDFIRK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 283 HTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELP-GPDAFPMDl 361
Cdd:PRK06793 204 ELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTLLME- 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 769968640 362 sVVISNFYGRAGHVilnngKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYFE 440
Cdd:PRK06793 283 -SYMKKLLERSGKT-----QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME 355
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
198-437 |
9.77e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 107.09 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 198 PITEYSEKP--RPyklLETGVRSIDTLNPIvegGTGFIPGAF---GTGKTVLQHSISKQAEADIVIIAACGERANEVVEi 272
Cdd:PRK08972 133 PINPLSRRPitEP---LDVGVRAINAMLTV---GKGQRMGLFagsGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKE- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 273 FTEfpELVDPHtGRKlmeRTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELP 352
Cdd:PRK08972 206 FIE--EILGEE-GRA---RSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 353 GPDAFPMDLSVVISNFYGRAGHvilNNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPI 432
Cdd:PRK08972 280 ATKGYPPSVFAKLPALVERAGN---GGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIE 356
|
....*
gi 769968640 433 DSYSK 437
Cdd:PRK08972 357 ASISR 361
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
212-437 |
2.26e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 106.24 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 212 LETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTVLQHSISKQAEADIVIIAACGERANEVVEiFTEFPeLVDPhtgrklME 290
Cdd:PRK06002 149 LRTGVRVIDIFTPLCAGQrIGIFAGS-GVGKSTLLAMLARADAFDTVVIALVGERGREVRE-FLEDT-LADN------LK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 291 RTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYG 370
Cdd:PRK06002 220 KAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLE 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 769968640 371 RAGhvilnNGKE--GSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK06002 300 RAG-----PGAEggGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
212-437 |
4.15e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 105.45 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 212 LETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTVLQHSISKQAEADIVIIAACGERANEVveiftefPELVDPHTGRKLME 290
Cdd:PRK08927 142 LDLGVRALNTFLTCCRGQrMGIFAGS-GVGKSVLLSMLARNADADVSVIGLIGERGREV-------QEFLQDDLGPEGLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 291 RTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYG 370
Cdd:PRK08927 214 RSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLE 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 769968640 371 RAGHVILNngkEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK08927 294 RAGPGPIG---EGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
213-437 |
8.65e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 104.38 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 213 ETGVRSIDTLnpiVEGGTGFIPGAF---GTGKTVLQHSISKQAEADIVIIAACGERANEVveiftefPELVDPHTGRKLm 289
Cdd:PRK08472 142 SVGVKSIDGL---LTCGKGQKLGIFagsGVGKSTLMGMIVKGCLAPIKVVALIGERGREI-------PEFIEKNLGGDL- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 290 ERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFY 369
Cdd:PRK08472 211 ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLM 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 769968640 370 GRAGHvilNNGKeGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:PRK08472 291 ERAGK---EEGK-GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR 354
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
198-437 |
3.82e-23 |
|
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: 99.60 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 198 PITEYSEKpRPYKLLETGVRSIDTLNPIVEGGTgfIPGAFGTG--------KTVLQHSISKQAEADIVIIAACG---ERA 266
Cdd:cd01135 40 PINPVARI-YPEEMIQTGISAIDVMNTLVRGQK--LPIFSGSGlphnelaaQIARQAGVVGSEENFAIVFAAMGvtmEEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 267 NEVVEIFTEfpelvdphTGrkLMERTIIVANTSNMPVAAREASVYTAMTIGEYYR-SMGLKVL-LMADSTSrWAQALREM 344
Cdd:cd01135 117 RFFKDDFEE--------TG--ALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVLvILTDMTN-YAEALREV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 345 SNRLEELPGPDAFPMDLSVVISNFYGRAGHVilnNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKK 424
Cdd:cd01135 186 SAAREEVPGRRGYPGYMYTDLATIYERAGRV---EGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKG 262
|
250
....*....|...
gi 769968640 425 RYPAINPIDSYSK 437
Cdd:cd01135 263 IYPPIDVLPSLSR 275
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
187-437 |
4.08e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 102.50 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 187 LNMIQRWPVKVPiteysekprpyklLETGVRSIDTLNPIvegGTGFIPGAF---GTGKTVLQHSISKQAEADIVIIAACG 263
Cdd:PRK05688 140 INPLNRHPISEP-------------LDVGIRSINGLLTV---GRGQRLGLFagtGVGKSVLLGMMTRFTEADIIVVGLIG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 264 ERANEVveiftefPELVDPHTGRKLMERTIIVANTSN-MPVAAREASVYTAmTIGEYYRSMGLKVLLMADSTSRWAQALR 342
Cdd:PRK05688 204 ERGREV-------KEFIEHILGEEGLKRSVVVASPADdAPLMRLRAAMYCT-RIAEYFRDKGKNVLLLMDSLTRFAQAQR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 343 EMSNRLEELPGPDAFPMDLSVVISNFYGRAGhvilnNGKE--GSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDR 420
Cdd:PRK05688 276 EIALAIGEPPATKGYPPSVFAKLPKLVERAG-----NAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRL 350
|
250
....*....|....*..
gi 769968640 421 ADKKRYPAINPIDSYSK 437
Cdd:PRK05688 351 AEEGHYPAIDIEASISR 367
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
145-483 |
5.57e-23 |
|
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: 102.10 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 145 HKIMVPFSMKGEYRIVRIIGEgdyNIyekiavveDNEGNVTELnmiQRWPVKVPITEYSEKPRPYKLLETGVRSIDTLNP 224
Cdd:TIGR01039 74 APISVPVGKETLGRIFNVLGE---PI--------DEKGPIPAK---ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 225 IVEGG-TGFIPGAfGTGKTVLQ----HSISKQAEAdIVIIAACGERANEVVEIFTEFPElvdphtgRKLMERTIIVANTS 299
Cdd:TIGR01039 140 YAKGGkIGLFGGA-GVGKTVLIqeliNNIAKEHGG-YSVFAGVGERTREGNDLYHEMKE-------SGVIDKTALVYGQM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 300 NMPVAAREASVYTAMTIGEYYRSM-GLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRaghviLN 378
Cdd:TIGR01039 211 NEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER-----IT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 379 NGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYFEyPEFqdyisseVSSDWVE 458
Cdd:TIGR01039 286 STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLD-PSV-------VGEEHYD 357
|
330 340
....*....|....*....|....*
gi 769968640 459 KVSEIKTRLLRGKEIAEQINILGDD 483
Cdd:TIGR01039 358 VARGVQQILQRYKELQDIIAILGMD 382
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
6-388 |
2.07e-22 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 100.29 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 6 TVKGIISNLVIVEVEGPVTQNEIAYI-DHEGTRLMAEVIKIVGKNASVQVFESTRGLKV-GSKVEFQGHMLEVVLGPGLL 83
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVEIeLPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLkDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 84 QRNLDGLendldkmdgvflkrGEytfPLDEeklwhfkpiakegdkvragswLGEvdenyqphkimvpfsmkgeyrivrII 163
Cdd:PRK04196 86 GRIFDGL--------------GR---PIDG---------------------GPE------------------------II 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 164 GEGDYNIyekiavvednegNVTELNMIQRwpvkvpiteysEKPRPYklLETGVRSIDTLNPIVEGGTgfIPGAFGTGktv 243
Cdd:PRK04196 104 PEKRLDI------------NGAPINPVAR-----------EYPEEF--IQTGISAIDGLNTLVRGQK--LPIFSGSG--- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 244 LQHS-----ISKQA------EADIVIIAACG---ERANEVVEIFTEfpelvdphTGrkLMERTIIVANTSNMPVAAREAS 309
Cdd:PRK04196 154 LPHNelaaqIARQAkvlgeeENFAVVFAAMGitfEEANFFMEDFEE--------TG--ALERSVVFLNLADDPAIERILT 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 310 VYTAMTIGEYYR-SMGLKVL-LMADSTSrWAQALREMSNRLEELPGPDAFP--M--DLSVVisnfYGRAGHVIlnnGKEG 383
Cdd:PRK04196 224 PRMALTAAEYLAfEKGMHVLvILTDMTN-YCEALREISAAREEVPGRRGYPgyMytDLATI----YERAGRIK---GKKG 295
|
....*
gi 769968640 384 SITFI 388
Cdd:PRK04196 296 SITQI 300
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
186-437 |
1.57e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 97.65 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 186 ELNMIQRWPVKVPiteysekprpyklLETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTVLQHSISKQAEADIVIIAACGE 264
Cdd:PRK07196 126 QIHPLQRRAVDTP-------------LDVGVNAINGLLTIGKGQrVGLMAGS-GVGKSVLLGMITRYTQADVVVVGLIGE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 265 RANEVveiftefPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREM 344
Cdd:PRK07196 192 RGREV-------KEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREI 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 345 SNRLEELPGPDAFPMDLSVVISNFYGRAGhvilNNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKK 424
Cdd:PRK07196 265 ALSLGEPPATKGYPPSAFSIIPRLAESAG----NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAG 340
|
250
....*....|...
gi 769968640 425 RYPAINPIDSYSK 437
Cdd:PRK07196 341 HYPAIDISQSISR 353
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
7-422 |
2.68e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 93.56 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 7 VKGIISNLVIVEVEGpVTQNEIAYIDHEGTRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGHMLEVVLGPGLLQRN 86
Cdd:PRK02118 8 ITDITGNVITVEAEG-VGYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 87 LDGlendldkmdgvflkrgeYTFPLDEEklwhfkpiakegdkvragswlGEVDENyqphkiMVPfsmkgeyrivriIGEG 166
Cdd:PRK02118 87 FNG-----------------SGKPIDGG---------------------PELEGE------PIE------------IGGP 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 167 DYNiyekiavvednegnvtelnmiqrwPVKVPIteysekprPYKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQH 246
Cdd:PRK02118 111 SVN------------------------PVKRIV--------PREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 247 SISKQAEADIVIIAACGeranevvEIFTEFPELVDPHTGRKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLK 326
Cdd:PRK02118 159 RIALQAEADIIILGGMG-------LTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKK 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 327 -VL-LMADSTSrWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAghVILNNGkeGSITFIGTVSPAGGNLKEPVTE 404
Cdd:PRK02118 232 kVLvLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG--GSITIIAVTTMPGDDVTHPVPD 306
|
410
....*....|....*...
gi 769968640 405 NTKKVARCFYALEQDRAD 422
Cdd:PRK02118 307 NTGYITEGQFYLRRGRID 324
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
158-386 |
8.62e-20 |
|
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: 89.54 E-value: 8.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 158 RIVRIIGEgdyNIYEKIAVVEDNEGNVTEL--NMIQRWPVKVPiteysekprpyklLETGVRSIDTLNPIVEGGTGFIPG 235
Cdd:cd01132 13 RVVDALGN---PIDGKGPIQTKERRRVESKapGIIPRQSVNEP-------------LQTGIKAIDSLIPIGRGQRELIIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 236 AFGTGKT-VLQHSISKQAEADIVII-AACGERANEVVEIFTEFPElvdphtgRKLMERTIIVANTSNMPVAAREASVYTA 313
Cdd:cd01132 77 DRQTGKTaIAIDTIINQKGKKVYCIyVAIGQKRSTVAQIVKTLEE-------HGAMEYTIVVAATASDPAPLQYLAPYAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 769968640 314 MTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHviLNNGK-EGSIT 386
Cdd:cd01132 150 CAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAK--LSDELgGGSLT 221
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
210-386 |
6.09e-19 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 89.58 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 210 KLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSISKQAEADIVIIAACGERANEVveiftefPELVDPHTGRKLM 289
Cdd:PRK05922 139 EIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREV-------REYIEQHKEGLAA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 290 ERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFY 369
Cdd:PRK05922 212 QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFT 291
|
170
....*....|....*..
gi 769968640 370 GRAGhvilNNGKeGSIT 386
Cdd:PRK05922 292 ERAG----NNDK-GSIT 303
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
187-437 |
5.39e-17 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 83.68 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 187 LNMIQRwpvkVPITEysekprpykLLETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTVLQHSISKQAEADIVIIAACGER 265
Cdd:PRK07960 147 FNPLQR----TPIEH---------VLDTGVRAINALLTVGRGQrMGLFAGS-GVGKSVLLGMMARYTQADVIVVGLIGER 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 266 ANEVveifTEFPELVDPHTGRKlmeRTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMS 345
Cdd:PRK07960 213 GREV----KDFIENILGAEGRA---RSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 346 NRLEELPGPDAFPMDLSVVISNFYGRAGHVIlNNGkeGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKR 425
Cdd:PRK07960 286 LAIGEPPATKGYPPSVFAKLPALVERAGNGI-SGG--GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGH 362
|
250
....*....|..
gi 769968640 426 YPAINPIDSYSK 437
Cdd:PRK07960 363 YPAIDIEASISR 374
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
179-437 |
7.56e-17 |
|
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: 81.11 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 179 DNEGnvtELNMIQRWPVKVPITEYSEKPRPYKLLETGVRSIDTLNPIVEGG-TGFIPGAfGTGKTV----LQHSISKqAE 253
Cdd:cd01133 21 DERG---PIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGkIGLFGGA-GVGKTVlimeLINNIAK-AH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 254 ADIVIIAACGERANEVVEIFTEFPElvdphTG---RKLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSM-GLKVLL 329
Cdd:cd01133 96 GGYSVFAGVGERTREGNDLYHEMKE-----SGvinLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 330 MADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRaghviLNNGKEGSITFIGTVSPAGGNLKEPVTENTKKV 409
Cdd:cd01133 171 FIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER-----ITSTKKGSITSVQAVYVPADDLTDPAPATTFAH 245
|
250 260
....*....|....*....|....*...
gi 769968640 410 ARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:cd01133 246 LDATTVLSRGIAELGIYPAVDPLDSTSR 273
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
209-386 |
2.46e-16 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 81.93 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 209 YKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKT-VLQHSISKQAEADIVII-AACGERANEVVEIFTEFPElvdphtgR 286
Cdd:CHL00059 122 YEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQNVICVyVAIGQKASSVAQVVTTLQE-------R 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 287 KLMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVIS 366
Cdd:CHL00059 195 GAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHS 274
|
170 180
....*....|....*....|.
gi 769968640 367 NFYGRAGHviLNNG-KEGSIT 386
Cdd:CHL00059 275 RLLERAAK--LSSQlGEGSMT 293
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
189-386 |
1.14e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 79.96 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 189 MIQRWPVKVPiteysekprpyklLETGVRSIDTLNPIVEGGTGFIPGAFGTGKTVLQ-HSISKQAEADIVII-AACGERA 266
Cdd:PRK13343 136 IIERDFVTEP-------------LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAiDAIINQKDSDVICVyVAIGQKA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 267 NEVVEIFtefpELVDPHTGrklMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSN 346
Cdd:PRK13343 203 SAVARVI----ETLREHGA---LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSL 275
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 769968640 347 RLEELPGPDAFPMDLSVVISNFYGRAGHVILNNGKeGSIT 386
Cdd:PRK13343 276 LLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGG-GSLT 314
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-72 |
1.77e-15 |
|
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: 71.19 E-value: 1.77e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 769968640 4 KGTVKGIISNLVIVEVEGPVTQNEIAYIDH----EGTRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQGH 72
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERgdgnNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-437 |
6.93e-15 |
|
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: 77.07 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 6 TVKGIISNLVIVE-VEGPvTQNEIAYID-HEGTRLMAEVIKIVGKNASVQVFESTRGLKV-GSKVEFQGHMLEVVLGPGL 82
Cdd:TIGR01040 4 TVSGVNGPLVILDnVKFP-RFAEIVNLTlPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAkKTTCEFTGDILRTPVSEDM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 83 LQRNLDGlendldkmDGvflkrgeytfpldeeklwhfKPIAKeGDKVRAGSWLgevDENYQPhkimvpfsmkgeyrivri 162
Cdd:TIGR01040 83 LGRVFNG--------SG--------------------KPIDK-GPPVLAEDYL---DINGQP------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 163 igegdYNIYEKIavvednegnvtelnmiqrwpvkvpiteysekpRPYKLLETGVRSIDTLNPIVEGGTGFIPGAFGTGKT 242
Cdd:TIGR01040 113 -----INPYARI--------------------------------YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHN 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 243 VLQHSISKQA--------------EADIVIIAACGERANEVVEIF-TEFPElvdphTGRklMERTIIVANTSNMPVAARE 307
Cdd:TIGR01040 156 EIAAQICRQAglvklptkdvhdghEDNFAIVFAAMGVNMETARFFkQDFEE-----NGS--MERVCLFLNLANDPTIERI 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 308 ASVYTAMTIGEYYR-SMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVilnNGKEGSIT 386
Cdd:TIGR01040 229 ITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---EGRNGSIT 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 769968640 387 FIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSK 437
Cdd:TIGR01040 306 QIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 356
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
211-483 |
1.83e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 72.77 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 211 LLETGVRSIDTLNPIVEGGT-GFIPGAfGTGKTV----LQHSISKqAEADIVIIAACGERANEVVEIFTEFPE--LVDPh 283
Cdd:CHL00060 144 IFETGIKVVDLLAPYRRGGKiGLFGGA-GVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKEsgVINE- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 284 tgRKLMERTI-IVANTSNMPVAAREASVYTAMTIGEYYRSMGLK-VLLMADSTSRWAQALREMSNRLEELPGPDAFPMDL 361
Cdd:CHL00060 221 --QNIAESKVaLVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 362 SVVISNFYGRaghviLNNGKEGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDSYSKYfey 441
Cdd:CHL00060 299 STEMGSLQER-----ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM--- 370
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 769968640 442 peFQDYISSEVSSDWVEKVSEIktrLLRGKEIAEQINILGDD 483
Cdd:CHL00060 371 --LQPRIVGEEHYETAQRVKQT---LQRYKELQDIIAILGLD 407
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
190-386 |
1.51e-11 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 67.01 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 190 IQRWPVKVPiteysekprpyklLETGVRSIDTLNPIvegGTG---FIPGAFGTGKT-VLQHSISKQAEADIVII-AACGE 264
Cdd:PRK09281 137 IDRKSVHEP-------------LQTGIKAIDAMIPI---GRGqreLIIGDRQTGKTaIAIDTIINQKGKDVICIyVAIGQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 265 RANEVVEIFtefpelvdphtgRKL-----MERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQ 339
Cdd:PRK09281 201 KASTVAQVV------------RKLeehgaMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAV 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 769968640 340 ALREMSNRLEELPGPDAFPMDLsvvisnFY------GRAGHVIlNNGKEGSIT 386
Cdd:PRK09281 269 AYRQLSLLLRRPPGREAYPGDV------FYlhsrllERAAKLS-DELGGGSLT 314
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
203-430 |
3.89e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 65.83 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 203 SEKPRPYKLLeTGVRSIDTLNPIVEGGTGFIPGAFGTGKTVL------------QHSISKQAEadIVIIAACGERANEVV 270
Cdd:PTZ00185 165 SRSPVNYNLL-TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIavstiinqvrinQQILSKNAV--ISIYVSIGQRCSNVA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 271 EIFtefpELVDPHTGrklMERTIIVANTSNMPVAAREASVYTAMTIGEYYRSMGLKVLLMADSTSRWAQALREMSNRLEE 350
Cdd:PTZ00185 242 RIH----RLLRSYGA---LRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 351 LPGPDAFPMDLSVVISNFYGRAGhvILNNGK-EGSITFIGTVSPAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAI 429
Cdd:PTZ00185 315 PPGREAYPGDVFYLHSRLLERAA--MLSPGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAV 392
|
.
gi 769968640 430 N 430
Cdd:PTZ00185 393 N 393
|
|
| 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 ... |
6-72 |
7.88e-10 |
|
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: 55.13 E-value: 7.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 6 TVKGIISNLVIVE-VEGpVTQNEIAYI-DHEGTRLMAEVIKIVGKNASVQVFESTRGLKV-GSKVEFQGH 72
Cdd:cd18118 4 TVSEINGPLVIVEgVKG-VKYGEIVEItLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLkGTKVRFTGE 72
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
7-71 |
1.58e-07 |
|
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: 48.70 E-value: 1.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 769968640 7 VKGIISNLVIVEVEGPVTQNEIAYID----HEGTRLMAEVIKIVGKNASVQVFESTRGLKVGSKVEFQG 71
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEvelvEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| 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 ... |
16-68 |
9.59e-07 |
|
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: 46.36 E-value: 9.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769968640 16 IVEVEGPV---------TQNEIAYIDHEGtrLMAEVIKIVGKNASVQVFESTRGLKVGSKVE 68
Cdd:cd18119 4 IYRVSGPVvvaegmsgaAMYELVRVGEEG--LIGEIIRLEGDKATIQVYEETSGLKVGEPVE 63
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
168-386 |
4.20e-05 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 46.50 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 168 YNIYEKIAVVEDNEGNVTELNMIQRWPVK---VPITEYSEKPRPYKL-------------LETGVRSIDTLNPIVEGGTG 231
Cdd:PRK07165 67 LNNTNKVKTSKEYFGKIIDIDGNIIYPEAqnpLSKKFLPNTSSIFNLahglmtvktlneqLYTGIIAIDLLIPIGKGQRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 232 FIPGAFGTGKTVLQ-HSISKQAEADIVII-AACGERANEVVEIFTEFPElvdphtgRKLMERTIIVANTSNMPVAAREAS 309
Cdd:PRK07165 147 LIIGDRQTGKTHIAlNTIINQKNTNVKCIyVAIGQKRENLSRIYETLKE-------HDALKNTIIIDAPSTSPYEQYLAP 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 769968640 310 vYTAMTIGEYYrSMGLKVLLMADSTSRWAQALREMSNRLEELPGPDAFPMDLSVVISNFYGRAGHVIlnNGKegSIT 386
Cdd:PRK07165 220 -YVAMAHAENI-SYNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFK--NRK--TIT 290
|
|
| 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 ... |
456-527 |
5.29e-05 |
|
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: 42.38 E-value: 5.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769968640 456 WVEKVSEIKTRLLRGKEIAEQINILGDDGVPVEYHITFWKSEFIDYIILQQDAFDDIDAVTSIERQ----KNILDL 527
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQykmlKLILTF 76
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
206-434 |
1.91e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 43.92 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 206 PRPYKLLETG-----VRSIDTLNPIVEGGTGFIPGAFGTGKTVLQHSIskqAEAdiviIAACGERANEVVEIFTEFPELV 280
Cdd:PRK12608 106 PRERLRLETGsddlsMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQI---AAA----VAANHPEVHLMVLLIDERPEEV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 281 -DphtgrklMERTI---IVANTSNMP----VAAREASVYTAMTIGEyyrsMGLKVLLMADSTSRWAQAL--------REM 344
Cdd:PRK12608 179 tD-------MRRSVkgeVYASTFDRPpdehIRVAELVLERAKRLVE----QGKDVVILLDSLTRLARAYnnevessgRTL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 345 SNrleelpGPDAFPMDlsvVISNFYGRAGHVilNNGkeGSITFIGT-VSPAGGNLKEPVTENTKKVARCFYALEQDRADK 423
Cdd:PRK12608 248 SG------GVDARALQ---RPKRLFGAARNI--EEG--GSLTIIATaLVDTGSRMDEVIFEEFKGTGNMEIVLDRELADK 314
|
250
....*....|.
gi 769968640 424 KRYPAINPIDS 434
Cdd:PRK12608 315 RVFPAIDIAKS 325
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
217-434 |
3.84e-04 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 42.58 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 217 RSIDTLNPIVEGGTGFIPGAFGTGKTVL----QHSISKQAEADIVIIAACGERANEVVEiftefpelvdphtgrklMERT 292
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLlqniANAIAKNHPEVELIVLLIDERPEEVTD-----------------MRRS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769968640 293 I---IVANTSNMPvAAREASVyTAMTIGEYYR--SMGLKVLLMADSTSRWAQA---LREMSNRLEElPGPDAFPMDlsvV 364
Cdd:cd01128 68 VkgeVVASTFDEP-PERHVQV-AEMVIEKAKRlvEHGKDVVILLDSITRLARAyntVVPSSGKTLS-GGVDANALH---K 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769968640 365 ISNFYGRAghvilNNGKEG-SITFIGTVS-PAGGNLKEPVTENTKKVARCFYALEQDRADKKRYPAINPIDS 434
Cdd:cd01128 142 PKRFFGAA-----RNIEEGgSLTIIATALvDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKS 208
|
|
| |
