|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
1-582 |
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: 910.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 1 MTKGKVTAIISNLISIEVDGPVSQNEICYVscGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPG 80
Cdd:COG1155 2 MTKGKIVKINGPLVTAEGMGGAKMYEVVYV--GEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 81 LLGKNFDGLQNDLDKLQ---GVFLERGKYNDlSEDKESTYDFTPIAKVGEEVQAGDWIGAVKEGW-IDHKIMVPFKFEGK 156
Cdd:COG1155 80 LLGNIFDGIQRPLDKIAeksGDFIPRGVDVP-ALDREKKWDFTPTVKVGDKVSAGDILGTVQETPlIEHKIMVPPGVSGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 157 gvVESVASAGTYHLQDTLAVIKSANGEKVNVTMIQTWPVKLTIKaYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGP 236
Cdd:COG1155 159 --VKEIAPEGEYTVEDTIAVLEDEDGEEHELTMYQKWPVRRPRP-YKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 237 FGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEFPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGMTI 316
Cdd:COG1155 236 FGTGKTVTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 317 AEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVYLNNGETGSITFIGTVSPAGG 396
Cdd:COG1155 316 AEYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 397 NLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIEypEFIEFSDINIEKGWADKVTKAKDIARRGQEANDQ 476
Cdd:COG1155 396 DFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLD--DLAEWYDENVDPDWSELRNEAMDLLQEEAELQEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 477 ISILGDDAVPLEYHQRLWKAELIDFVILQQDAFDKVDKNCPIERQKELLNQVMKVVEADYRFDDYSEVGTYFKR--LINA 554
Cdd:COG1155 474 VRLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKElpLREK 553
|
570 580 590
....*....|....*....|....*....|
gi 501925326 555 FKQMNYSVYQS--DDHKKYTAEMESIFAER 582
Cdd:COG1155 554 IARMKYSPENEllEKFDELEKEIDEEIEEL 583
|
|
| 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: 880.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 1 MTKGKVTAIISNLISIEVDGPVSQNEICYVscGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPG 80
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGARMYEVVRV--GEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 81 LLGKNFDGLQNDLDKLQ---GVFLERGKYNDlSEDKESTYDFTPIAKVGEEVQAGDWIGAVKEG-WIDHKIMVPFKFEGK 156
Cdd:PRK04192 80 LLGSIFDGIQRPLDELAeksGDFLERGVYVP-ALDREKKWEFTPTVKVGDKVEAGDILGTVQETpSIEHKIMVPPGVSGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 157 gvVESVASAGTYHLQDTLAVIKSANGEKVNVTMIQTWPVKLTIKaYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGP 236
Cdd:PRK04192 159 --VKEIVSEGDYTVDDTIAVLEDEDGEGVELTMMQKWPVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 237 FGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEFPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGMTI 316
Cdd:PRK04192 236 FGSGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 317 AEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVYLNNGETGSITFIGTVSPAGG 396
Cdd:PRK04192 316 AEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 397 NLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIEypEFIEFSDINIEKGWADKVTKAKDIARRGQEANDQ 476
Cdd:PRK04192 396 DFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLD--QVAPWWEENVDPDWRELRDEAMDLLQREAELQEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 477 ISILGDDAVPLEYHQRLWKAELIDFVILQQDAFDKVDKNCPIERQKELLNQVMKVVEADYRFDDYS---------EVGTY 547
Cdd:PRK04192 474 VRLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGvpvseilelEVRDR 553
|
570 580 590
....*....|....*....|....*....|....
gi 501925326 548 FKRLINAFKQMnYSVYQSDDHKKYTAEMESIFAE 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 ... |
72-438 |
1.73e-151 |
|
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: 437.01 E-value: 1.73e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 72 MLEIELGPGLLGKNFDGLQNDLDKLQ---GVFLERGKYNdlsedkestydftpiakvgeevqagdwigavkegwidhkim 148
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAetgSIFIPRGVNV----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 149 vpfkfegkgvvesvasagtyhlqdtlaviksangekvnvtmiQTWPVKlTIKAYKEKPRPFKLLETGVRTIDTFNPITEG 228
Cdd:cd01134 40 ------------------------------------------QRWPVR-QPRPVKEKLPPNVPLLTGQRVLDTLFPVAKG 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 229 GTGFIPGPFGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEFPELIDPRTGRSLMERTTIICNTSNMPVAAREA 308
Cdd:cd01134 77 GTAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 309 SVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVYLNN--GETGSIT 386
Cdd:cd01134 157 SIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGspGREGSVT 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 501925326 387 FIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKY 438
Cdd:cd01134 237 IVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
215-436 |
1.28e-85 |
|
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: 264.99 E-value: 1.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 215 GVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEFPElidprtgRSLMERTTI 294
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG-------SGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 295 ICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGF 374
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501925326 375 VylnNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYS 436
Cdd:pfam00006 154 V---KGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
242-533 |
4.17e-77 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 263.81 E-value: 4.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 242 TVLQHALATNANADLIIMTACGERANEVVEIFTEFPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYR 321
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 322 SMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVYL--NNGETGSITFIGTVSPAGGNLK 399
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgSDYRVGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 400 EPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIEYPEfiEFSDINIEKGWADKVTKAKDIARRGQEANDQISI 479
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVK--DWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501925326 480 LGDDAVPLEYHQRLWKAELIDFVILQQDAFDKVDKNCPIERQKELLNQVMKVVE 533
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYD 961
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
172-438 |
7.20e-70 |
|
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: 226.57 E-value: 7.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 172 DTLAVIKSANGEKVN----VTMIQTWPVKLTIKAYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHA 247
Cdd:cd19476 7 ELLGRILDGLGEPLDglppIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 248 LATN---ANADLIIMTACGERANEVVEIFTEFPELIDprtgrslMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMG 324
Cdd:cd19476 87 LARNqakAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 325 LKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVylnNGETGSITFIGTVSPAGGNLKEPVTE 404
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV---KDGGGSITAIPAVSTPGDDLTDPIPD 236
|
250 260 270
....*....|....*....|....*....|....
gi 501925326 405 STRKAARCFYALSQKRADSKRYPAVDPLDSYSKY 438
Cdd:cd19476 237 NTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
3-284 |
2.82e-43 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 166.35 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 3 KGKVTAIISNLISieVDGPVSQNEICYVSCGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPGLL 82
Cdd:PRK14698 4 KGRIIRVTGPLVI--ADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 83 GKNFDGLQNDLDKLQ---GVFLERG-KYNDLSEDKEstYDFTPIAKVGEEVQAGDWIGAVKE-GWIDHKIMVPFKFEGKg 157
Cdd:PRK14698 82 TSIYDGIQRPLEVIReksGDFIARGiSAPALPRDKK--WHFIPKVKVGDKVVGGDIIGEVPEtSIITHKIMVPPGIEGE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 158 VVEsVASAGTYHLQDTLAVIKSANGEKVNVTMIQTWPVKLTiKAYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPF 237
Cdd:PRK14698 159 IVE-IADEGEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVK-RPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 501925326 238 GAGKTVLQHALATNANADLIIMTACGE----RANEVVEIFTEFPELIDPRT 284
Cdd:PRK14698 237 GSGKCVDGDTLILTKEFGLIKIKDLYEildgKGKKTVEGNEEWTELEEPIT 287
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
86-210 |
4.80e-42 |
|
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: 147.16 E-value: 4.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 86 FDGLQNDLDKLQ---GVFLERGKYND-LSEDKEstYDFTPIAKVGEEVQAGDWIGAVKEGW-IDHKIMVPFKFEGKgvVE 160
Cdd:pfam16886 1 FDGIQRPLEKIAeksGSFIPRGVDVPaLDREKK--WEFTPTVKVGDKVSGGDILGTVQETSlIEHKIMVPPGVSGT--VT 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501925326 161 SVASAGTYHLQDTLAVIKSaNGEKVNVTMIQTWPVKltikaykeKPRPFK 210
Cdd:pfam16886 77 EIAPEGEYTVEDTIAEVED-EGKEKELTMMQKWPVR--------RPRPYK 117
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
212-437 |
9.24e-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: 146.17 E-value: 9.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATNANADLIIMTACGERANEVVEiFTEFpELidprtGRSLMER 291
Cdd:cd01136 51 LPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVRE-FIEK-DL-----GEEGLKR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 292 TTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYAR 371
Cdd:cd01136 124 SVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLER 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501925326 372 AGfvylnNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:cd01136 204 AG-----NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-436 |
1.76e-38 |
|
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: 146.71 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 4 GKVTAIISNLIsiEVDGP-VSQNEICYVSC-GNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPGL 81
Cdd:COG1157 21 GRVTRVVGLLI--EAVGPdASIGELCEIETaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 82 LGKNFDGLQNDLDklqgvflergkyndlsedkestydftpiakvgeevqagdwigavkegwidhkimvpfkfeGKGVVES 161
Cdd:COG1157 99 LGRVLDGLGRPLD------------------------------------------------------------GKGPLPG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 162 VASagtyhlqdtlaviksangekvnvtmiqtWPVkltikaYKEKPRPFK------LLETGVRTIDTFNPITEG------- 228
Cdd:COG1157 119 EER----------------------------RPL------DAPPPNPLEraritePLDTGVRAIDGLLTVGRGqrigifa 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 229 GTGfipgpfgAGKTVLQHALATNANADLIIMTACGERANEVVEiFTEfpelidprtgRSL----MERTTIICNTSNMPVA 304
Cdd:COG1157 165 GSG-------VGKSTLLGMIARNTEADVNVIALIGERGREVRE-FIE----------DDLgeegLARSVVVVATSDEPPL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 305 AREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPG-----PDAFPiDLPAIISsfyaRAGfvylnN 379
Cdd:COG1157 227 MRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPAtrgypPSVFA-LLPRLLE----RAG-----N 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501925326 380 GETGSITFIGTVSPAGGNLKEPVTESTRkaarcfyA-------LSQKRADSKRYPAVDPLDSYS 436
Cdd:COG1157 297 GGKGSITAFYTVLVEGDDMNDPIADAVR-------GildghivLSRKLAERGHYPAIDVLASIS 353
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-437 |
6.81e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.95 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 4 GKVTAIISNLISIEVDGpVSQNEICYVscGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPGLLG 83
Cdd:PRK06820 31 GPIVEIGPTLLRASLPG-VAQGELCRI--EPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 84 KNFDGLQNDLDklqgvflergkyndlsedkestydftpiakvGEEVQAGDWigavkegwidhkimvpfkfegkgvvesva 163
Cdd:PRK06820 108 RILDGLGAPID-------------------------------GGPPLTGQW----------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 164 sagtyhlqdtlaviKSANGEKvnvtmiqtwPVKLTIKAYKEkprpfkLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTV 243
Cdd:PRK06820 128 --------------RELDCPP---------PSPLTRQPIEQ------MLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 244 LQHALATNANADLIIMTACGERANEVveifTEFPELIDPRTGRSlmeRTTIICNTSNMPVAAREASVYVGMTIAEYYRSM 323
Cdd:PRK06820 179 LLGMLCADSAADVMVLALIGERGREV----REFLEQVLTPEARA---RTVVVVATSDRPALERLKGLSTATTIAEYFRDR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 324 GLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGfvylnNGETGSITFIGTVSPAGGNLKEPVT 403
Cdd:PRK06820 252 GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-----NSDRGSITAFYTVLVEGDDMNEPVA 326
|
410 420 430
....*....|....*....|....*....|....
gi 501925326 404 ESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK06820 327 DEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSR 360
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-437 |
5.98e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 128.33 E-value: 5.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 3 KGKVTAIISNLISIEVDGpVSQNEICYVSC--GNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPG 80
Cdd:PRK06936 24 RGRVTQVTGTILKAVVPG-VRIGELCYLRNpdNSLSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 81 LLGKNFDGLQNDLDklqgvflergkyndlsedkestydftpiakVGEEVQAGDWigavkegwidhkimvpfkfegkgvve 160
Cdd:PRK06936 103 LLGRVLDGLGQPFD------------------------------GGHPPEPAAW-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 161 svasagtyhlqdtlaviksangekvnvtmiqtWPVkltikaYKEKPRPF--KLLET----GVRTIDTFNPITEGGTGFIP 234
Cdd:PRK06936 127 --------------------------------YPV------YADAPAPMsrRLIETplslGVRVIDGLLTCGEGQRMGIF 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 235 GPFGAGKTVLQHALATNANADLIIMTACGERANEVveiftefPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGM 314
Cdd:PRK06936 169 AAAGGGKSTLLASLIRSAEVDVTVLALIGERGREV-------REFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVAT 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 315 TIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGfvylnNGETGSITFIGTVSPA 394
Cdd:PRK06936 242 SIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-----QSDKGSITALYTVLVE 316
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 501925326 395 GGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK06936 317 GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASR 359
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-437 |
9.69e-31 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 124.88 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 4 GKVTAIISNLISIE-VDgpVSQNEICYVSCGNAKLM--AEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPG 80
Cdd:PRK09099 26 GKVVEVIGTLLRVSgLD--VTLGELCELRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 81 LLGKNFDGLQNDLDklqgvflergkyndlsedkestydftpiakvgeevqagdwigavkegwidhkimvpfkfeGKGVVE 160
Cdd:PRK09099 104 LLGRVIDGLGEPID------------------------------------------------------------GGGPLD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 161 SvasagtyhlqDTLAVIKSANGEKVNVTMIqtwpvkltikaykEKPRPfklleTGVRTIDTFNPITEGGTGFIPGPFGAG 240
Cdd:PRK09099 124 C----------DELVPVIAAPPDPMSRRMV-------------EAPLP-----TGVRIVDGLMTLGEGQRMGIFAPAGVG 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 241 KTVLQHALATNANADLIIMTACGERANEVveifTEFPELIdprTGRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYY 320
Cdd:PRK09099 176 KSTLMGMFARGTQCDVNVIALIGERGREV----REFIELI---LGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 321 RSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFvylnnGETGSITFIGTVSPAGGNLKE 400
Cdd:PRK09099 249 RDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-----GETGSITALYTVLAEDESGSD 323
|
410 420 430
....*....|....*....|....*....|....*..
gi 501925326 401 PVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK09099 324 PIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSR 360
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-527 |
2.20e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 117.90 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 4 GKVTAIISnlISIEVDGPVSQ-NEICYV---SCGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGP 79
Cdd:PRK07721 20 GKVSRVIG--LMIESKGPESSiGDVCYIhtkGGGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 80 GLLGKNFDGLQNDLDklqgvflergkyndlsedkestydftpiakvGEEvqagdwigavkegwidhkimvpfkfegkgvv 159
Cdd:PRK07721 98 GLIGQVLDALGEPLD-------------------------------GSA------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 160 esvasagtyhLQDTLAviksangekvNVTMIQTWPVKLtikaykEKPRPFKLLETGVRTIDTFNPITEGG-TGFIPGPfG 238
Cdd:PRK07721 116 ----------LPKGLA----------PVSTDQDPPNPL------KRPPIREPMEVGVRAIDSLLTVGKGQrVGIFAGS-G 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 239 AGKTVLQHALATNANADLIIMTACGERANEVveiftefPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGMTIAE 318
Cdd:PRK07721 169 VGKSTLMGMIARNTSADLNVIALIGERGREV-------REFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 319 YYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGfvylnNGETGSITFIGTVSPAGGNL 398
Cdd:PRK07721 242 YFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG-----TNASGSITAFYTVLVDGDDM 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 399 KEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK---YIEYPEFIEFSDiniekgwadkvtKAKDIARRGQEAND 475
Cdd:PRK07721 317 NEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRvmnHIVSPEHKEAAN------------RFRELLSTYQNSED 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501925326 476 QISILG---------DDAVplEYHqrlwkAELIDFviLQQDAFDKVDKNCPIERQKELLNQ 527
Cdd:PRK07721 385 LINIGAykrgssreiDEAI--QFY-----PQIISF--LKQGTDEKATFEESIQALLSLFGK 436
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
212-437 |
1.08e-27 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 115.82 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATNANADLIIMTACGERANEVVEiFTEFPELIDPRtgrslmER 291
Cdd:PRK07594 139 LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGERGREVRE-FIDFTLSEETR------KR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 292 TTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYAR 371
Cdd:PRK07594 212 CVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLER 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501925326 372 AGFvylnnGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK07594 292 TGM-----GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
212-437 |
1.04e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 110.07 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGG-TGFIPGPfGAGKTVLQHALATNANADLIIMTACGERANEVveiftefPELIDPRTGRSLME 290
Cdd:PRK08927 142 LDLGVRALNTFLTCCRGQrMGIFAGS-GVGKSVLLSMLARNADADVSVIGLIGERGREV-------QEFLQDDLGPEGLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 291 RTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPG-----PDAFPiDLPAII 365
Cdd:PRK08927 214 RSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTtkgytPTVFA-ELPRLL 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501925326 366 SsfyaRAGFVYLNngeTGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK08927 293 E----RAGPGPIG---EGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
207-437 |
1.77e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 109.70 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 207 RPFKlleTGVRTIDTFNPITEGG-TGFIPGPfGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEfpelidprTG 285
Cdd:PRK06002 147 TGLR---TGVRVIDIFTPLCAGQrIGIFAGS-GVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED--------TL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 286 RSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFP----IDL 361
Cdd:PRK06002 215 ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPpsvfSEL 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 362 PAIISsfyaRAGfvylnNGE--TGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK06002 295 PRLLE----RAG-----PGAegGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
212-437 |
9.37e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 107.48 E-value: 9.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGG-TGFIPGPfGAGKTVLQHALATNANADLIIMTACGERANEVveifTEFPELIDPRTGRslmE 290
Cdd:PRK08972 146 LDVGVRAINAMLTVGKGQrMGLFAGS-GVGKSVLLGMMTRGTTADVIVVGLVGERGREV----KEFIEEILGEEGR---A 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 291 RTTIIC---NTSN-MPVAAREASVyvgmTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFP----IDLP 362
Cdd:PRK08972 218 RSVVVAapaDTSPlMRLKGCETAT----TIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPpsvfAKLP 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501925326 363 AIISsfyaRAGfvylNNGE-TGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK08972 294 ALVE----RAG----NGGPgQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISR 361
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
210-437 |
2.30e-24 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 105.85 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 210 KLLETGVRTIDTFnpITeGGTGFIPGPF---GAGKTVLQHALATNANADLIIMTACGERANEVveifTEFPELIDpRTGR 286
Cdd:PRK08149 133 EPLITGVRAIDGL--LT-CGVGQRMGIFasaGCGKTSLMNMLIEHSEADVFVIGLIGERGREV----TEFVESLR-ASSR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 287 SlmERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPID----LP 362
Cdd:PRK08149 205 R--EKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASvfdsLP 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501925326 363 AIISsfyaRAGfvylnNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK08149 283 RLLE----RPG-----ATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
127-440 |
2.50e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 102.75 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 127 EEVQAGDWIGAVKEgwidhKIMVPfkfegkgvvesvasAGTYHLQDTLavikSANGEKVN--VTMIQTWPVKLT---IKA 201
Cdd:PRK06793 74 EKVCYGDSVTLIAE-----DVVIP--------------RGNHLLGKVL----SANGEVLNeeAENIPLQKIKLDappIHA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 202 YkEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATNANADLIIMTACGERANEVveiftefPELID 281
Cdd:PRK06793 131 F-EREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV-------KDFIR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 282 PRTGRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELpgpdafPIDL 361
Cdd:PRK06793 203 KELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKEL------PIGG 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501925326 362 PAIISSFYARAGFVYLNNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIE 440
Cdd:PRK06793 277 KTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME 355
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
212-479 |
2.95e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 99.80 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIdtfNPITEGGTGFIPGPF---GAGKTVLQHALATNANADLIIMTACGERANEVveiftefPELIDPRTGRSL 288
Cdd:PRK05688 152 LDVGIRSI---NGLLTVGRGQRLGLFagtGVGKSVLLGMMTRFTEADIIVVGLIGERGREV-------KEFIEHILGEEG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 289 MERTTIICNTSN-MPVAAREASVYVgMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISS 367
Cdd:PRK05688 222 LKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 368 FYARAGfvylnNGET--GSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIeyPEFI 445
Cdd:PRK05688 301 LVERAG-----NAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM--PQVV 373
|
250 260 270
....*....|....*....|....*....|....*..
gi 501925326 446 EfsdiniekgwADKVTKA---KDIARRGQEANDQISI 479
Cdd:PRK05688 374 D----------PEHLRRAqrfKQLWSRYQQSRDLISV 400
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
192-505 |
6.21e-21 |
|
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: 95.94 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 192 TWPVKLTIKAYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATN---ANADLIIMTACGERANE 268
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiakEHGGYSVFAGVGERTRE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 269 VVEIFTEFPElidprtgRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSM-GLKVLLLADSTSRWAQALREMSNR 347
Cdd:TIGR01039 187 GNDLYHEMKE-------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSAL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 348 LEELPGPDAFPIDLPAIISSFYARagfvyLNNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYP 427
Cdd:TIGR01039 260 LGRMPSAVGYQPTLATEMGELQER-----ITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYP 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 428 AVDPLDSYSKYIEyPEFIEfsdiniEKGWaDKVTKAKDIARRGQEANDQISILGDDAVPLEYHQRLWKAELIDFVILQ 505
Cdd:TIGR01039 335 AVDPLDSTSRLLD-PSVVG------EEHY-DVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQ 404
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
212-437 |
5.83e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 92.65 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGG-TGFIPGPfGAGKTVLQHALATNANADLIIMTACGERANEVveiftefPELIDPRTGRSLME 290
Cdd:PRK07196 139 LDVGVNAINGLLTIGKGQrVGLMAGS-GVGKSVLLGMITRYTQADVVVVGLIGERGREV-------KEFIEHSLQAAGMA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 291 RTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYA 370
Cdd:PRK07196 211 KSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAE 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 371 RAGfvylnNGE-TGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK07196 291 SAG-----NSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
211-437 |
8.90e-20 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 92.15 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 211 LLETGVRTIdtfNPITEGGTGFIPGPF---GAGKTVLQHALATNANADLIIMTACGERANEVveifTEFPELIDPRTGRS 287
Cdd:PRK07960 158 VLDTGVRAI---NALLTVGRGQRMGLFagsGVGKSVLLGMMARYTQADVIVVGLIGERGREV----KDFIENILGAEGRA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 288 lmeRTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISS 367
Cdd:PRK07960 231 ---RSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPA 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501925326 368 FYARAGfvylnNGET--GSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSK 437
Cdd:PRK07960 308 LVERAG-----NGISggGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-406 |
3.81e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 90.09 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 5 KVTAIISNLISIEVDGpVSQNEICYVSCGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGSMLEIELGPGLLGK 84
Cdd:PRK02118 7 KITDITGNVITVEAEG-VGYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 85 NFDGLQNDLDKlqGVFLErgkyndlsedkestydftpiakvGEEVQAGdwigavkegwidhkimvpfkfegkgvvesvas 164
Cdd:PRK02118 86 RFNGSGKPIDG--GPELE-----------------------GEPIEIG-------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 165 agtyhlqdtlaviksanGEKVNvtmiqtwPVKLTIkaykekprPFKLLETGVRTIDTFNPITEGGTGFI---PG-PFGAg 240
Cdd:PRK02118 109 -----------------GPSVN-------PVKRIV--------PREMIRTGIPMIDVFNTLVESQKIPIfsvSGePYNA- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 241 ktvLQHALATNANADLIIMTACGeranevvEIFTEFPELIDPRTGRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYY 320
Cdd:PRK02118 156 ---LLARIALQAEADIIILGGMG-------LTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 321 RSMGLK-VL-LLADSTSrWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAgfVYLNNGetGSITFIGTVSPAGGNL 398
Cdd:PRK02118 226 ALEGKKkVLvLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG--GSITIIAVTTMPGDDV 300
|
....*...
gi 501925326 399 KEPVTEST 406
Cdd:PRK02118 301 THPVPDNT 308
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-388 |
2.23e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 87.96 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 5 KVTAIISNLISIEVDGPVSQNEICYVSCGNA-KLMAEVIKISGTSASAQVFESTRGVKLGDA-VEFTGSMLEIELGPGLL 82
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVEIELPNGeKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 83 GKNFDGLQNDLDKLQGVFLErgkyndlsedkestyDFTPIakvgeevqagdwigavkegwidhkimvpfkfegkgvvesv 162
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPE---------------KRLDI---------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 163 asagtyhlqdtlaviksaNGEKVNvtmiqtwPVkltikaYKEKPRPFklLETGVRTIDTFNPITEG-------GTGfIPG 235
Cdd:PRK04196 111 ------------------NGAPIN-------PV------AREYPEEF--IQTGISAIDGLNTLVRGqklpifsGSG-LPH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 236 PFGAGKTVLQHALATNANADLIIMTACG---ERANEVVEIFTefpelidpRTGrsLMERTTIICNTSNMPVAAREASVYV 312
Cdd:PRK04196 157 NELAAQIARQAKVLGEEENFAVVFAAMGitfEEANFFMEDFE--------ETG--ALERSVVFLNLADDPAIERILTPRM 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 313 GMTIAEY--YRsMGLKVL-LLADSTSrWAQALREMSNRLEELPGPDAFP----IDLpaiiSSFYARAGFVylnNGETGSI 385
Cdd:PRK04196 227 ALTAAEYlaFE-KGMHVLvILTDMTN-YCEALREISAAREEVPGRRGYPgymyTDL----ATIYERAGRI---KGKKGSI 297
|
...
gi 501925326 386 TFI 388
Cdd:PRK04196 298 TQI 300
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
203-437 |
3.56e-18 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 84.97 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 203 KEKPRPFklLETGVRTIDTFNPITEG-------GTGFipgPFG--AGKTVLQHALATNANADLIIMTACG---ERANEVV 270
Cdd:cd01135 46 RIYPEEM--IQTGISAIDVMNTLVRGqklpifsGSGL---PHNelAAQIARQAGVVGSEENFAIVFAAMGvtmEEARFFK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 271 EIFTEfpelidprTGrsLMERTTIICNTSNMPVAAREASVYVGMTIAEYYR-SMGLKVL-LLADSTSrWAQALREMSNRL 348
Cdd:cd01135 121 DDFEE--------TG--ALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVLvILTDMTN-YAEALREVSAAR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 349 EELPGPDAFPIDLPAIISSFYARAGFVylnNGETGSITFIGTVSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPA 428
Cdd:cd01135 190 EEVPGRRGYPGYMYTDLATIYERAGRV---EGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPP 266
|
....*....
gi 501925326 429 VDPLDSYSK 437
Cdd:cd01135 267 IDVLPSLSR 275
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
173-440 |
3.15e-16 |
|
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: 79.19 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 173 TLAVIKSANGEKVN----VTMIQTWPVKLTIKAYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHAL 248
Cdd:cd01133 8 TLGRIFNVLGEPIDergpIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 249 ATN---ANADLIIMTACGERANEVVEIFTEFPE--LIDPRTgrslMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSM 323
Cdd:cd01133 88 INNiakAHGGYSVFAGVGERTREGNDLYHEMKEsgVINLDG----LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 324 -GLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARagfvyLNNGETGSITFIGTVSPAGGNLKEPV 402
Cdd:cd01133 164 eGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER-----ITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 501925326 403 TESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIE 440
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
210-386 |
7.61e-16 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 79.95 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 210 KLLETGVRTIDTFNPITEGG-TGFIPGPfGAGKTVLQHALATNANADLIIMTACGERANEVVEIFTEFPELIDprtgrsl 288
Cdd:PRK05922 139 EIFPTGIKAIDAFLTLGKGQrIGVFSEP-GSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLA------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 289 MERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSF 368
Cdd:PRK05922 211 AQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEF 290
|
170
....*....|....*...
gi 501925326 369 YARAGfvylnNGETGSIT 386
Cdd:PRK05922 291 TERAG-----NNDKGSIT 303
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
212-386 |
7.63e-16 |
|
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: 77.98 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTvlqhALATNA-----NADLI-IMTACGERANEVVEIFTEFPElidprtg 285
Cdd:cd01132 53 LQTGIKAIDSLIPIGRGQRELIIGDRQTGKT----AIAIDTiinqkGKKVYcIYVAIGQKRSTVAQIVKTLEE------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 286 RSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAII 365
Cdd:cd01132 122 HGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH 201
|
170 180
....*....|....*....|.
gi 501925326 366 SSFYARAGFVYLNNGEtGSIT 386
Cdd:cd01132 202 SRLLERAAKLSDELGG-GSLT 221
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-71 |
1.58e-14 |
|
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: 68.49 E-value: 1.58e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501925326 3 KGKVTAIISNLISIEVDGPVSQNEICYVSCGN----AKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTGS 71
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnneTVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
212-386 |
1.95e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 72.69 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTvlqhALATNA-----NADLI-IMTACGERANEVVEIFTEFPElidprtg 285
Cdd:CHL00059 125 LQTGLIAIDSMIPIGRGQRELIIGDRQTGKT----AVATDTilnqkGQNVIcVYVAIGQKASSVAQVVTTLQE------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 286 RSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAII 365
Cdd:CHL00059 194 RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLH 273
|
170 180
....*....|....*....|...
gi 501925326 366 SSFYARAGfvYLNN--GEtGSIT 386
Cdd:CHL00059 274 SRLLERAA--KLSSqlGE-GSMT 293
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
212-386 |
3.46e-13 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 71.87 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTvlqhALATNA-----NADLI-IMTACGERANEVVEIftefpelIDPRTG 285
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKT----AIAIDAiinqkDSDVIcVYVAIGQKASAVARV-------IETLRE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 286 RSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAII 365
Cdd:PRK13343 215 HGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLH 294
|
170 180
....*....|....*....|.
gi 501925326 366 SSFYARAGFVYLNNGeTGSIT 386
Cdd:PRK13343 295 SRLLERAAKLSPELG-GGSLT 314
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
173-483 |
9.95e-12 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 67.37 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 173 TLAVIKSANGEKVN----VTMIQTWPVKLTIKAYKEKPRPFKLLETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHAL 248
Cdd:CHL00060 102 TLGRIFNVLGEPVDnlgpVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 249 ATN---ANADLIIMTACGERANEVVEIFTEFPE--LIDPRtgrSLME-RTTIICNTSNMPVAAREASVYVGMTIAEYYRS 322
Cdd:CHL00060 182 INNiakAHGGVSVFGGVGERTREGNDLYMEMKEsgVINEQ---NIAEsKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 323 MGLK-VLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARagfvyLNNGETGSITFIGTVSPAGGNLKEP 401
Cdd:CHL00060 259 VNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER-----ITSTKEGSITSIQAVYVPADDLTDP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 402 VTESTRKAARCFYALSQKRADSKRYPAVDPLDSYSKYIEyPEFI--EFSDIniekgwADKVtkaKDIARRGQEANDQISI 479
Cdd:CHL00060 334 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PRIVgeEHYET------AQRV---KQTLQRYKELQDIIAI 403
|
....
gi 501925326 480 LGDD 483
Cdd:CHL00060 404 LGLD 407
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
25-388 |
2.77e-11 |
|
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: 65.90 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 25 NEICYVSCGNAKL-MAEVIKISGTSASAQVFESTRGVklgDA----VEFTGSMLEIELGPGLLGKNFDGLQNDLDKLQGV 99
Cdd:TIGR01040 24 AEIVNLTLPDGTVrSGQVLEVSGNKAVVQVFEGTSGI---DAkkttCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 100 FLErgkyndlsedkestyDFTPIakvgeevqagdwigavkegwidhkimvpfkfegkgvvesvasagtyhlqdtlaviks 179
Cdd:TIGR01040 101 LAE---------------DYLDI--------------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 180 aNGEKVNvtmiqtwPvkltikayKEKPRPFKLLETGVRTIDTFNPITEGGTgfIPGPFGAG--------KTVLQHALATN 251
Cdd:TIGR01040 109 -NGQPIN-------P--------YARIYPEEMIQTGISAIDVMNSIARGQK--IPIFSAAGlphneiaaQICRQAGLVKL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 252 ANADL---------IIMTACGERAnEVVEIF-TEFPElidprtgRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYR 321
Cdd:TIGR01040 171 PTKDVhdghednfaIVFAAMGVNM-ETARFFkQDFEE-------NGSMERVCLFLNLANDPTIERIITPRLALTTAEYLA 242
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 322 -SMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAGFVylnNGETGSITFI 388
Cdd:TIGR01040 243 yQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---EGRNGSITQI 307
|
|
| 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 ... |
16-70 |
4.84e-10 |
|
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: 55.61 E-value: 4.84e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501925326 16 IEVDGPV---------SQNEICYVscGNAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTG 70
Cdd:cd18119 5 YRVSGPVvvaegmsgaAMYELVRV--GEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTG 66
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-70 |
1.09e-09 |
|
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: 54.86 E-value: 1.09e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501925326 6 VTAIISNLISIEVDGPVSQNEICYVSCG----NAKLMAEVIKISGTSASAQVFESTRGVKLGDAVEFTG 70
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElvefGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
206-391 |
4.90e-09 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 58.90 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 206 PRPFKLLeTGVRTIDTFNPITEGGTGFIPGPFGAGKTVLQHALATN----------ANADLIIMTACGERANEVVEIFte 275
Cdd:PTZ00185 168 PVNYNLL-TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqilsKNAVISIYVSIGQRCSNVARIH-- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 276 fpelidpRTGRSL--MERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPG 353
Cdd:PTZ00185 245 -------RLLRSYgaLRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPG 317
|
170 180 190
....*....|....*....|....*....|....*...
gi 501925326 354 PDAFPIDLPAIISSFYARAGFVYLNNGeTGSITFIGTV 391
Cdd:PTZ00185 318 REAYPGDVFYLHSRLLERAAMLSPGKG-GGSVTALPIV 354
|
|
| 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 ... |
456-530 |
6.78e-08 |
|
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: 50.85 E-value: 6.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501925326 456 WADKVTKAKDIARRGQEANDQISILGDDAVPLEyhQR--LWKAELIDFVILQQDAFDKVDKNCPIERQKELLNQVMK 530
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEE--DRltLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILT 75
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
212-386 |
2.37e-05 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 46.98 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 212 LETGVRTIDTFNPITEGGTGFIPGPFGAGKTvlqhALATNA-----NADLI-IMTACGERAN---EVVEIFTEfpelidp 282
Cdd:PRK09281 146 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKT----AIAIDTiinqkGKDVIcIYVAIGQKAStvaQVVRKLEE------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 283 rtgRSLMERTTIICNTSNMPVAAREASVYVGMTIAEYYRSMGLKVLLLADSTSRWAQALREMSNRLEELPGPDAFPIDLp 362
Cdd:PRK09281 215 ---HGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDV- 290
|
170 180 190
....*....|....*....|....*....|
gi 501925326 363 aiissFY------ARAGFVYLNNGeTGSIT 386
Cdd:PRK09281 291 -----FYlhsrllERAAKLSDELG-GGSLT 314
|
|
| 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 ... |
5-70 |
3.48e-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: 42.03 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 5 KVTAIISNLISIEVDGPVSQNEICYVSCGNA-KLMAEVIKISGTSASAQVFESTRGVKL-GDAVEFTG 70
Cdd:cd18118 4 TVSEINGPLVIVEGVKGVKYGEIVEITLPDGeVRRGQVLEVSGDKAVVQVFEGTSGLDLkGTKVRFTG 71
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
217-434 |
4.78e-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: 42.19 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 217 RTIDTFNPITEGGTGFIPGPFGAGKTVLQHALA---TNANADLIIMTA-CGERANEVVEiftefpelidprtgrslMERT 292
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIAnaiAKNHPEVELIVLlIDERPEEVTD-----------------MRRS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 293 T---IICNTSNMPvAAREASVyVGMTIAEYYR--SMGLKVLLLADSTSRWAQA---LREMSNRLEElPGPDAFPIDLPai 364
Cdd:cd01128 68 VkgeVVASTFDEP-PERHVQV-AEMVIEKAKRlvEHGKDVVILLDSITRLARAyntVVPSSGKTLS-GGVDANALHKP-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501925326 365 iSSFY--ARagfvylNNGETGSITFIGTVS-PAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVDPLDS 434
Cdd:cd01128 143 -KRFFgaAR------NIEEGGSLTIIATALvDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKS 208
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
193-373 |
5.83e-04 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 42.65 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 193 WPVKLTIKAYKEKPR---PFKL-------------LETGVRTIDTFNPITEGGTGFIPGPFGAGKTVLqhALAT---NAN 253
Cdd:PRK07165 92 YPEAQNPLSKKFLPNtssIFNLahglmtvktlneqLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI--ALNTiinQKN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 254 ADL-IIMTACGERANEVVEIFTEFPElidprtgRSLMERTTIICNTSNMPVAAREASvYVGMTIAEYYrSMGLKVLLLAD 332
Cdd:PRK07165 170 TNVkCIYVAIGQKRENLSRIYETLKE-------HDALKNTIIIDAPSTSPYEQYLAP-YVAMAHAENI-SYNDDVLIVFD 240
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501925326 333 STSRWAQALREMSNRLEELPGPDAFPIDLPAIISSFYARAG 373
Cdd:PRK07165 241 DLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAG 281
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
217-430 |
8.27e-04 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 41.98 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 217 RTIDTFNPITEGGTGFIPGPFGAGKTVL----QHALATN-ANADLIIMTAcGERANEVVEiftefpelidprtgrslMER 291
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLlqkiAQAITRNhPEVELIVLLI-DERPEEVTD-----------------MQR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501925326 292 TT---IICNTSNMPvAAREASVyVGMTIAEYYRSMGLK--VLLLADSTSRWAQALREM---SNRLEElPGPDAFPIDLPa 363
Cdd:TIGR00767 219 SVkgeVVASTFDEP-ASRHVQV-AEMVIEKAKRLVEHKkdVVILLDSITRLARAYNTVtpaSGKVLS-GGVDANALHRP- 294
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501925326 364 iiSSFYARAgfvyLNNGETGSITFIGT-VSPAGGNLKEPVTESTRKAARCFYALSQKRADSKRYPAVD 430
Cdd:TIGR00767 295 --KRFFGAA----RNIEEGGSLTIIATaLIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAID 356
|
|
| |
