|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
733-1063 |
0e+00 |
|
V-type (H+)-ATPase V1, A 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: 273411 [Multi-domain] Cd Length: 591 Bit Score: 663.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:TIGR01042 255 IVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADST 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:TIGR01042 335 SRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDV 972
Cdd:TIGR01042 415 FWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLVGKDALAETDKITLEV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 973 ATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGAN------WSKLADSTGDVKHAVSSSKFFEPSR 1046
Cdd:TIGR01042 495 AKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQddnkitWSIIKESLGDLLYRLSSMKFEDPSD 574
|
330
....*....|....*..
gi 256270281 1047 GEKEVHGEFEKLLSTMQ 1063
Cdd:TIGR01042 575 GEAKIKADYEKLNEDMQ 591
|
|
| Hom_end_hint |
pfam05203 |
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are ... |
284-736 |
0e+00 |
|
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life. The crystal structure of the homing nuclease PI-Sce revealed two domains: an endonucleolytic centre resembling the C-terminal domain of Drosophila melanogaster Hedgehog protein, and a second domain containing the protein-splicing active site. This Domain corresponds to the latter protein-splicing domain.
Pssm-ID: 368334 [Multi-domain] Cd Length: 444 Bit Score: 656.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 284 CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSsrevpeLLKFTCNATHE 363
Cdd:pfam05203 1 CFAKGTEVLMADGSIKSIEDIEVGDKVMGKDGTPREVVGLPRGRETMYEVTQKTQHRADESEG------LLSFTCNANHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 364 LVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYP-VSEGPERANelVESYRKASNKAYFEWTI 442
Cdd:pfam05203 75 LVLRTPQKIRVTEHVLRGKKYTSVTYFALEDTKTGDGRIIEIVKEVTKSFPhSSHGGERAA--AQEFAATIDKEPIEWTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 443 EARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIegPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERV 522
Cdd:pfam05203 153 EARDLDLLGAHVRKATFQLINPVLYESGHLAQYLEKQGFDKSL--APELAYLLGLWVGDGTSDAAEFSVDSQDTELMERI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 523 TEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGVRNNLNTENPLWDAIIGLGFLKDG--VKNIPSFLSTDNIGTRET 600
Cdd:pfam05203 231 VEYGKALGLTATTKDEQEPLRAKTVNLHSGNERDGGNRNRLNTNNLFWDAVVSLGFRKDGdgEKQIPSFLASEDIEVREQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 601 FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGtKHKISYAIYMSGGDVLLNVLSK 680
Cdd:pfam05203 311 FLAGLIDSDGYVKKDKGGSATIKTIYPSVMDGLVKLARSLGIKVSVTTESAKTDVGV-RHVSCYAITLSGGDALQSVLSK 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 256270281 681 CAGSKKFRPAPVAtFVRECQGFYFELQELKENDYYGITLSDDSDHQFLLANQVVVH 736
Cdd:pfam05203 390 CALSRKKAPVPEP-FAREPVPFYFTLEKLEEDDYYGITLPEDSDHQFLLSNLALVH 444
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
26-1068 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 577.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 26 GAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETI 105
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESQSiYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLISsHKILLPPRSRGTITW 185
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIIT-HKIMVPPGIEGEIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 186 IAPAGEYTLDEKILEVEF-DGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKT 264
Cdd:PRK14698 162 IADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 265 VisqslskysNSDAIIYVGCFAKgtnvlmadgsiecienIEVGNKVMGKDGRPREVIKlprGRETMYSVVQKSQHRAHKS 344
Cdd:PRK14698 242 V---------DGDTLILTKEFGL----------------IKIKDLYEILDGKGKKTVE---GNEEWTELEEPITLYGYKD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 345 DSSREVP--ELLKFTCNATHELVVRTPRSVR----------RLSRtiKGVEYFEVitfeMGQKKAPDGRIVeLVKEVsks 412
Cdd:PRK14698 294 GKIVEIKatHVYKGASAGMIEIKTRTGRKIKvtpihklftgRVTK--DGLEIEEV----MAKDIKKGDRIA-VAKKI--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 413 ypvsEGPERANELVESYRKASNKayfewtieardlsllgshvrkatyqtyapilyendhffdymqkskfhltIEGPKVL- 491
Cdd:PRK14698 364 ----DGGERVKLNIRVDQKRGKK-------------------------------------------------IKIPDVLd 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 492 ---AYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLnlcaeykdrkepqvaktVNLYSKVVRGNGVRNNLNTENP 568
Cdd:PRK14698 391 eelAEFLGYLIADGTLKPRTVAIYNNDESLLKRANELAMEL-----------------FGIEGKIVKERTVKALLIHSKA 453
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 569 LWDAIIGLGF---LKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGiKATIKTIHTSVRDGLVSLARSLGLVAS 645
Cdd:PRK14698 454 LVDFFKKLGIpgnKKARTWKVPKELLISEPEVVKAFIKAYIACDGYYDEEKG-EIEIVTASEEAAYGFSYLLAKLGIYAI 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 646 VNAEPakvdMNGtkhKISYAIYMSGGDVL--LNVLSKCAGSKKFRPAPV-------------ATFVREC---------QG 701
Cdd:PRK14698 533 IREKI----IGD---KEYYRVVISGEANLekLGIEREARGYTSIDIVPVdveeiyealgrpyAELKKAGieihnylsgEN 605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 702 FYFE----------LQELKEN--------------------DYYGITlsdDSDHQFLLAN-------------------- 731
Cdd:PRK14698 606 MSYEmfrkfakfvgLEEIAENhlqhilfdeiveinyisegqEVYDIT---TETHNFIGGNmptllhntvtqhqlakwsda 682
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 732 QVVVH-NCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIAD 810
Cdd:PRK14698 683 QVVIYiGCGERGNEMTDVLEEFPKLKDPKTG--KPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMAD 760
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 811 SSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT 890
Cdd:PRK14698 761 STSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 891 QVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNY-PEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKIT 969
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVdPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAI 920
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 970 LDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTgdVKHAVSSSKfFEPSRgek 1049
Cdd:PRK14698 921 LLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLP--VREEIGRMK-FEPDI--- 994
|
1130
....*....|....*....
gi 256270281 1050 evhGEFEKLLSTMQERFAE 1068
Cdd:PRK14698 995 ---EKIKALIDKTNEQFDE 1010
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
733-1068 |
4.17e-164 |
|
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: 496.16 E-value: 4.17e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:COG1155 256 VVYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVALMADST 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPdrTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:COG1155 334 SRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDFSEPVTQNTLRIVKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNY-PEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLD 971
Cdd:COG1155 412 FWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVdPDWSELRNEAMDLLQEEAELQEIVRLVGEDALPDEDRLTLE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 972 VATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADstGDVKHAVSSSKFFEpsrgEKEV 1051
Cdd:COG1155 492 VARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKE--LPLREKIARMKYSP----ENEL 565
|
330
....*....|....*..
gi 256270281 1052 HGEFEKLLSTMQERFAE 1068
Cdd:COG1155 566 LEKFDELEKEIDEEIEE 582
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
730-918 |
1.17e-132 |
|
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: 403.11 E-value: 1.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIA 809
Cdd:cd01134 102 SDVVIYVGCGERGNEMAEVLEEFPELKDPITG--ESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGI 889
Cdd:cd01134 180 DSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRI 259
|
170 180
....*....|....*....|....*....
gi 256270281 890 TQVFWGLDKKLAQRKHFPSINTSVSYSKY 918
Cdd:cd01134 260 VQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
26-284 |
2.62e-132 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 413.41 E-value: 2.62e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 26 GAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETI 105
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESqSIYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLIsSHKILLPPRSRGTITW 185
Cdd:PRK04192 85 FDGIQRPLDELAEKS-GDFLERGVYVPALDREKKWEFTP-TVKVGDKVEAGDILGTVQETPSI-EHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 186 IAPAGEYTLDEKILEVE-FDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKT 264
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260
....*....|....*....|
gi 256270281 265 VISQSLSKYSNSDAIIYVGC 284
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGC 261
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
729-916 |
5.63e-73 |
|
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: 240.72 E-value: 5.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 729 LANQ-----VVVHNCGERGNEMAEVLMEFPElytemsgtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGK 803
Cdd:pfam00006 34 IARQasadvVVYALIGERGREVREFIEELLG---------SGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 804 NVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKavalgSPDRTGSVSIVAAVSPAGGDFSDPVT 883
Cdd:pfam00006 105 DVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR-----VKGKGGSITALPTVLVPGDDITDPIP 179
|
170 180 190
....*....|....*....|....*....|...
gi 256270281 884 TATLGITQVFWGLDKKLAQRKHFPSINTSVSYS 916
Cdd:pfam00006 180 DNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
106-228 |
5.79e-70 |
|
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: 228.44 E-value: 5.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESQSiYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLISsHKILLPPRSRGTITW 185
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIE-HKIMVPPGVSGTVTE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 256270281 186 IAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKL 228
Cdd:pfam16886 78 IAPEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
92-293 |
1.31e-59 |
|
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: 206.27 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 92 PLSVELGPGLMETIYDGIQRPLKAIkEESQSIYIPRGIDTpaldrtikwqftpgkfqvgdhisggdiygsvfenslissh 171
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVI-AETGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 172 killpprsrgtitwiapageytldekilevefdgkksdftlyHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGG 251
Cdd:cd01134 40 ------------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 256270281 252 TTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKG---TNVLM 293
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGnemAEVLE 122
|
|
| Hop |
COG1372 |
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ... |
491-829 |
1.93e-14 |
|
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];
Pssm-ID: 440983 [Multi-domain] Cd Length: 866 Bit Score: 78.01 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 491 LAYLLGLWIGDG-LSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYskvVRGNGVRnnlntenpL 569
Cdd:COG1372 212 LAYLLGLLLGDGsLSKRGAGRFTNADEELLEDVAEAAEELFGRADEGPRVEARRATVYEVR---VSSKPLA--------E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 570 WDAIIGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVtDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAE 649
Cdd:COG1372 281 LLEELGLFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSV-SNRGGRIRLSTTSRRLAEQVQLLLLRLGIVSRIYER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 650 PAKvdmNGtKHKISYAIYMSGGDVLLN-------------------------------VLSKCAGSKKFRPAPVATFVRE 698
Cdd:COG1372 360 RRP---DG-KGRTAYRLRISGGDNLRRfaerigfgssrkqerlaellaalrrrkddlvRARELANGRRLSRERLRRLALE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 699 CQ--------GFYF----ELQELKENDYYGITLSDdsDHQFlLANQVVVHNCGERgnEMAEVLMEFPELYtemsgtkepi 766
Cdd:COG1372 436 DEalealadsDVYWdevvSIEPVGEEDVYDLTVPG--THNF-VANGIVVHNSGGA--LDDVGAAVLDEDL---------- 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256270281 767 mKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEM 829
Cdd:COG1372 501 -LGGEPEEGEAGGAAEDKDRAKTGATTLAAGDLLVERDVEAEPEEIEDVISGEGRILERAALL 562
|
|
| HintN |
smart00306 |
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ... |
283-388 |
7.67e-09 |
|
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.
Pssm-ID: 197642 [Multi-domain] Cd Length: 100 Bit Score: 54.20 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 283 GCFAKGTNVLMADGSIECIENIEVGNKVMGKDG-------RPREVIKLPRGRETMYSVVQKSQHrahksdssrevpellK 355
Cdd:smart00306 1 GCFPGDTLVLTEDGGIKKIEELEEGDKVLALDEgtlkyspVKVFLVREPKGEKKFYRIKTENGR---------------E 65
|
90 100 110
....*....|....*....|....*....|....
gi 256270281 356 FTCNATHELVVRTPRSVR-RLSRTIKGVEYFEVI 388
Cdd:smart00306 66 ITLTPDHLLLVRDGGKLVwVFASELKPGDYVLVP 99
|
|
| Hint |
cd00081 |
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ... |
284-373 |
4.78e-06 |
|
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.
Pssm-ID: 238035 [Multi-domain] Cd Length: 136 Bit Score: 47.26 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 284 CFAKGTNVLMADGSIECIENIEV--GNKVMGKD----GRPREVIKLPR--GRETMYSVVQKSQHrahksdssrevpellK 355
Cdd:cd00081 1 CFTGDTLVLLEDGGRKKIEELVEkkGDKVLALDetgkLVFSKVLKVLRrdYEKKFYKIKTESGR---------------E 65
|
90
....*....|....*...
gi 256270281 356 FTCNATHELVVRTPRSVR 373
Cdd:cd00081 66 ITLTPDHLLFVLEDGELK 83
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
24-113 |
3.40e-05 |
|
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: 47.79 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 24 EYGAIYSVSGPVVIAENMIGCAMYELVKVG-HDNLV--GEVIRIDGDKATIQVYEETAGLTVGDPVLR-TGKPLSVELGP 99
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTlPDGTVrsGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEfTGDILRTPVSE 80
|
90
....*....|....
gi 256270281 100 GLMETIYDGIQRPL 113
Cdd:TIGR01040 81 DMLGRVFNGSGKPI 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
733-1063 |
0e+00 |
|
V-type (H+)-ATPase V1, A 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: 273411 [Multi-domain] Cd Length: 591 Bit Score: 663.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:TIGR01042 255 IVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADST 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:TIGR01042 335 SRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDV 972
Cdd:TIGR01042 415 FWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLVGKDALAETDKITLEV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 973 ATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGAN------WSKLADSTGDVKHAVSSSKFFEPSR 1046
Cdd:TIGR01042 495 AKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQddnkitWSIIKESLGDLLYRLSSMKFEDPSD 574
|
330
....*....|....*..
gi 256270281 1047 GEKEVHGEFEKLLSTMQ 1063
Cdd:TIGR01042 575 GEAKIKADYEKLNEDMQ 591
|
|
| Hom_end_hint |
pfam05203 |
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are ... |
284-736 |
0e+00 |
|
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life. The crystal structure of the homing nuclease PI-Sce revealed two domains: an endonucleolytic centre resembling the C-terminal domain of Drosophila melanogaster Hedgehog protein, and a second domain containing the protein-splicing active site. This Domain corresponds to the latter protein-splicing domain.
Pssm-ID: 368334 [Multi-domain] Cd Length: 444 Bit Score: 656.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 284 CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSsrevpeLLKFTCNATHE 363
Cdd:pfam05203 1 CFAKGTEVLMADGSIKSIEDIEVGDKVMGKDGTPREVVGLPRGRETMYEVTQKTQHRADESEG------LLSFTCNANHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 364 LVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYP-VSEGPERANelVESYRKASNKAYFEWTI 442
Cdd:pfam05203 75 LVLRTPQKIRVTEHVLRGKKYTSVTYFALEDTKTGDGRIIEIVKEVTKSFPhSSHGGERAA--AQEFAATIDKEPIEWTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 443 EARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIegPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERV 522
Cdd:pfam05203 153 EARDLDLLGAHVRKATFQLINPVLYESGHLAQYLEKQGFDKSL--APELAYLLGLWVGDGTSDAAEFSVDSQDTELMERI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 523 TEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGVRNNLNTENPLWDAIIGLGFLKDG--VKNIPSFLSTDNIGTRET 600
Cdd:pfam05203 231 VEYGKALGLTATTKDEQEPLRAKTVNLHSGNERDGGNRNRLNTNNLFWDAVVSLGFRKDGdgEKQIPSFLASEDIEVREQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 601 FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGtKHKISYAIYMSGGDVLLNVLSK 680
Cdd:pfam05203 311 FLAGLIDSDGYVKKDKGGSATIKTIYPSVMDGLVKLARSLGIKVSVTTESAKTDVGV-RHVSCYAITLSGGDALQSVLSK 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 256270281 681 CAGSKKFRPAPVAtFVRECQGFYFELQELKENDYYGITLSDDSDHQFLLANQVVVH 736
Cdd:pfam05203 390 CALSRKKAPVPEP-FAREPVPFYFTLEKLEEDDYYGITLPEDSDHQFLLSNLALVH 444
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
26-1068 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 577.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 26 GAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETI 105
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESQSiYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLISsHKILLPPRSRGTITW 185
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIIT-HKIMVPPGIEGEIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 186 IAPAGEYTLDEKILEVEF-DGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKT 264
Cdd:PRK14698 162 IADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 265 VisqslskysNSDAIIYVGCFAKgtnvlmadgsiecienIEVGNKVMGKDGRPREVIKlprGRETMYSVVQKSQHRAHKS 344
Cdd:PRK14698 242 V---------DGDTLILTKEFGL----------------IKIKDLYEILDGKGKKTVE---GNEEWTELEEPITLYGYKD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 345 DSSREVP--ELLKFTCNATHELVVRTPRSVR----------RLSRtiKGVEYFEVitfeMGQKKAPDGRIVeLVKEVsks 412
Cdd:PRK14698 294 GKIVEIKatHVYKGASAGMIEIKTRTGRKIKvtpihklftgRVTK--DGLEIEEV----MAKDIKKGDRIA-VAKKI--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 413 ypvsEGPERANELVESYRKASNKayfewtieardlsllgshvrkatyqtyapilyendhffdymqkskfhltIEGPKVL- 491
Cdd:PRK14698 364 ----DGGERVKLNIRVDQKRGKK-------------------------------------------------IKIPDVLd 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 492 ---AYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLnlcaeykdrkepqvaktVNLYSKVVRGNGVRNNLNTENP 568
Cdd:PRK14698 391 eelAEFLGYLIADGTLKPRTVAIYNNDESLLKRANELAMEL-----------------FGIEGKIVKERTVKALLIHSKA 453
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 569 LWDAIIGLGF---LKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGiKATIKTIHTSVRDGLVSLARSLGLVAS 645
Cdd:PRK14698 454 LVDFFKKLGIpgnKKARTWKVPKELLISEPEVVKAFIKAYIACDGYYDEEKG-EIEIVTASEEAAYGFSYLLAKLGIYAI 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 646 VNAEPakvdMNGtkhKISYAIYMSGGDVL--LNVLSKCAGSKKFRPAPV-------------ATFVREC---------QG 701
Cdd:PRK14698 533 IREKI----IGD---KEYYRVVISGEANLekLGIEREARGYTSIDIVPVdveeiyealgrpyAELKKAGieihnylsgEN 605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 702 FYFE----------LQELKEN--------------------DYYGITlsdDSDHQFLLAN-------------------- 731
Cdd:PRK14698 606 MSYEmfrkfakfvgLEEIAENhlqhilfdeiveinyisegqEVYDIT---TETHNFIGGNmptllhntvtqhqlakwsda 682
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 732 QVVVH-NCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIAD 810
Cdd:PRK14698 683 QVVIYiGCGERGNEMTDVLEEFPKLKDPKTG--KPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMAD 760
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 811 SSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT 890
Cdd:PRK14698 761 STSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 891 QVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNY-PEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKIT 969
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVdPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAI 920
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 970 LDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTgdVKHAVSSSKfFEPSRgek 1049
Cdd:PRK14698 921 LLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLP--VREEIGRMK-FEPDI--- 994
|
1130
....*....|....*....
gi 256270281 1050 evhGEFEKLLSTMQERFAE 1068
Cdd:PRK14698 995 ---EKIKALIDKTNEQFDE 1010
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
733-1068 |
4.17e-164 |
|
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: 496.16 E-value: 4.17e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:COG1155 256 VVYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVALMADST 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPdrTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:COG1155 334 SRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDFSEPVTQNTLRIVKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNY-PEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLD 971
Cdd:COG1155 412 FWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVdPDWSELRNEAMDLLQEEAELQEIVRLVGEDALPDEDRLTLE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 972 VATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADstGDVKHAVSSSKFFEpsrgEKEV 1051
Cdd:COG1155 492 VARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKE--LPLREKIARMKYSP----ENEL 565
|
330
....*....|....*..
gi 256270281 1052 HGEFEKLLSTMQERFAE 1068
Cdd:COG1155 566 LEKFDELEKEIDEEIEE 582
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
733-1068 |
1.42e-157 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 479.28 E-value: 1.42e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELytEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:PRK04192 256 VIYVGCGERGNEMTEVLEEFPEL--IDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADST 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPdrTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:PRK04192 334 SRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDFSEPVTQNTLRIVKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSN-YPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLD 971
Cdd:PRK04192 412 FWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENvDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 972 VATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADstGDVKHAVSSSKFFEPSRGEKEV 1051
Cdd:PRK04192 492 VARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILE--LEVRDRIARLKYIPENEYLEKI 569
|
330
....*....|....*..
gi 256270281 1052 HGEFEKLLSTMQERFAE 1068
Cdd:PRK04192 570 DEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
732-1060 |
3.19e-142 |
|
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130115 [Multi-domain] Cd Length: 578 Bit Score: 439.16 E-value: 3.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 732 QVVVH-NCGERGNEMAEVLMEFPELytEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIAD 810
Cdd:TIGR01043 249 DIVVYiGCGERGNEMTDVLEEFPEL--KDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMAD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 811 SSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT 890
Cdd:TIGR01043 327 STSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFSEPVTQNTLRIV 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 891 QVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNY-PEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKIT 969
Cdd:TIGR01043 407 KVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVdPDWREMRDEAMDLLQKESELQEIVQLVGPDALPERQKLI 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 970 LDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADStgDVKHAVSSSKFFEPSRGE- 1048
Cdd:TIGR01043 487 LEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKL--EVKEEIGRMKYEPDNDILa 564
|
330
....*....|....
gi 256270281 1049 --KEVHGEFEKLLS 1060
Cdd:TIGR01043 565 kiDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
730-918 |
1.17e-132 |
|
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: 403.11 E-value: 1.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEVLMEFPELYTEMSGtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIA 809
Cdd:cd01134 102 SDVVIYVGCGERGNEMAEVLEEFPELKDPITG--ESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGI 889
Cdd:cd01134 180 DSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRI 259
|
170 180
....*....|....*....|....*....
gi 256270281 890 TQVFWGLDKKLAQRKHFPSINTSVSYSKY 918
Cdd:cd01134 260 VQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
26-284 |
2.62e-132 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 413.41 E-value: 2.62e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 26 GAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETI 105
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESqSIYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLIsSHKILLPPRSRGTITW 185
Cdd:PRK04192 85 FDGIQRPLDELAEKS-GDFLERGVYVPALDREKKWEFTP-TVKVGDKVEAGDILGTVQETPSI-EHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 186 IAPAGEYTLDEKILEVE-FDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKT 264
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260
....*....|....*....|
gi 256270281 265 VISQSLSKYSNSDAIIYVGC 284
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGC 261
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
729-916 |
5.63e-73 |
|
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: 240.72 E-value: 5.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 729 LANQ-----VVVHNCGERGNEMAEVLMEFPElytemsgtkEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGK 803
Cdd:pfam00006 34 IARQasadvVVYALIGERGREVREFIEELLG---------SGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 804 NVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKavalgSPDRTGSVSIVAAVSPAGGDFSDPVT 883
Cdd:pfam00006 105 DVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR-----VKGKGGSITALPTVLVPGDDITDPIP 179
|
170 180 190
....*....|....*....|....*....|...
gi 256270281 884 TATLGITQVFWGLDKKLAQRKHFPSINTSVSYS 916
Cdd:pfam00006 180 DNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
106-228 |
5.79e-70 |
|
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: 228.44 E-value: 5.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 106 YDGIQRPLKAIKEESQSiYIPRGIDTPALDRTIKWQFTPgKFQVGDHISGGDIYGSVFENSLISsHKILLPPRSRGTITW 185
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIE-HKIMVPPGVSGTVTE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 256270281 186 IAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKL 228
Cdd:pfam16886 78 IAPEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
733-918 |
5.91e-61 |
|
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: 209.23 E-value: 5.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLMEFPELytemsgtkePIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:cd19476 99 VVFAGIGERGREVNDLYEEFTKS---------GAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAValgspDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQV 892
Cdd:cd19476 170 SRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDG 244
|
170 180
....*....|....*....|....*.
gi 256270281 893 FWGLDKKLAQRKHFPSINTSVSYSKY 918
Cdd:cd19476 245 QIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
92-293 |
1.31e-59 |
|
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: 206.27 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 92 PLSVELGPGLMETIYDGIQRPLKAIkEESQSIYIPRGIDTpaldrtikwqftpgkfqvgdhisggdiygsvfenslissh 171
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVI-AETGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 172 killpprsrgtitwiapageytldekilevefdgkksdftlyHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGG 251
Cdd:cd01134 40 ------------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 256270281 252 TTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKG---TNVLM 293
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGnemAEVLE 122
|
|
| Hom_end |
pfam05204 |
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found ... |
585-690 |
6.67e-48 |
|
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life.
Pssm-ID: 368335 [Multi-domain] Cd Length: 110 Bit Score: 165.94 E-value: 6.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 585 NIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGTKHKISY 664
Cdd:pfam05204 1 NIPSFLSSEAIEVREAFLAGLIDSDGYVDKAKNITASVKTEDKSVMEGIVKLARSLGIKASVKTKEEPIDAKGVNLQFTY 80
|
90 100
....*....|....*....|....*.
gi 256270281 665 AIYMSGGDVLLNVLSKCAGSKKFRPA 690
Cdd:pfam05204 81 AITLSGGDALLSVLSKCALWNKRVEA 106
|
|
| 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 ... |
933-1027 |
1.08e-41 |
|
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: 147.92 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 933 FPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEA 1012
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90
....*....|....*
gi 256270281 1013 QKAVANGANWSKLAD 1027
Cdd:cd18111 81 LEALEKGVPLSKILE 95
|
|
| 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 ... |
25-91 |
1.79e-41 |
|
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: 145.75 E-value: 1.79e-41
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256270281 25 YGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGK 91
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
730-914 |
2.32e-28 |
|
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: 115.35 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEmaevLMEFPELytEMSGTKepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIA 809
Cdd:cd01136 93 ADVNVIALIGERGRE----VREFIEK--DLGEEG---LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLM 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAvalgspdRTGSVSIVAAVSPAGGDFSDPVTTATLGI 889
Cdd:cd01136 164 DSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNG-------EKGSITAFYTVLVEGDDFNDPIADEVRSI 236
|
170 180
....*....|....*....|....*..
gi 256270281 890 TQVFWGLDKKLAQRKHFPSIN--TSVS 914
Cdd:cd01136 237 LDGHIVLSRRLAERGHYPAIDvlASIS 263
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
739-956 |
9.60e-28 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 117.55 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEmaevLMEFPElytemSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK06936 197 GERGRE----VREFIE-----SDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAGkavalgsPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDK 898
Cdd:PRK06936 268 QREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-------QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSR 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256270281 899 KLAQRKHFPSINTSVSYSKytnVLNKFYDsnyPEFPVLRDRMKEILSNAEELEQVVQL 956
Cdd:PRK06936 341 KLAAANHYPAIDVLRSASR---VMNQIVS---KEHKTWAGRLRELLAKYEEVELLLQI 392
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
719-1007 |
1.41e-27 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 117.22 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 719 LSDDSDhqfllANQVVVHNCGERGNEMAEVLmefpelytEMSGTKEPiMKRTTLVANTSNMPVAAREASIYTGITLAEYF 798
Cdd:PRK06820 183 LCADSA-----ADVMVLALIGERGREVREFL--------EQVLTPEA-RARTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 799 RDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGkavalgsPDRTGSVSIVAAVSPAGGDF 878
Cdd:PRK06820 249 RDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------NSDRGSITAFYTVLVEGDDM 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 879 SDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKytnVLNKFYDsnyPEFPVLRDRMKEILSNAEELEQVVQlVG 958
Cdd:PRK06820 322 NEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSR---IMPQIVS---AGQLAMAQKLRRMLACYQEIELLVR-VG 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 256270281 959 KSAlSDSDKITlDVATLIKE---DFLQQNGystyDAFCPIWKTFDMMRAFIS 1007
Cdd:PRK06820 395 EYQ-AGEDLQA-DEALQRYPaicAFLQQDH----SETAHLETTLEHLAQVVG 440
|
|
| Hom_end |
pfam05204 |
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found ... |
478-579 |
2.19e-26 |
|
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life.
Pssm-ID: 368335 [Multi-domain] Cd Length: 110 Bit Score: 104.31 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 478 KSKFHLTIEGPKVL-AYLLGLWIGDGLSDRA---TFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNL---Y 550
Cdd:pfam05204 1 NIPSFLSSEAIEVReAFLAGLIDSDGYVDKAkniTASVKTEDKSVMEGIVKLARSLGIKASVKTKEEPIDAKGVNLqftY 80
|
90 100 110
....*....|....*....|....*....|
gi 256270281 551 SKVVRGNGVRNNLNTENPLWDAIIG-LGFL 579
Cdd:pfam05204 81 AITLSGGDALLSVLSKCALWNKRVEaLGFL 110
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
739-914 |
3.93e-25 |
|
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: 109.74 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEmaevLMEF------PELytemsgtkepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSS 812
Cdd:COG1157 192 GERGRE----VREFieddlgEEG-----------LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 813 SRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGkavalgsPDRTGSVSIVAAVSPAGGDFSDPVTTATLGItqv 892
Cdd:COG1157 257 TRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG-------NGGKGSITAFYTVLVEGDDMNDPIADAVRGI--- 326
|
170 180 190
....*....|....*....|....*....|
gi 256270281 893 fwgLD------KKLAQRKHFPSIN--TSVS 914
Cdd:COG1157 327 ---LDghivlsRKLAERGHYPAIDvlASIS 353
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
726-917 |
9.26e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 109.05 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 726 QFLLANQVVVHNCGERGNEMAEvlmeFPElytEMSGtkEPIMKRTTLVANTSN-MPVAAREASIYTgITLAEYFRDQGKN 804
Cdd:PRK05688 190 RFTEADIIVVGLIGERGREVKE----FIE---HILG--EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 805 VSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGspdrtGSVSIVAAVSPAGGDFSDPVTT 884
Cdd:PRK05688 260 VLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGG-----GSITAFYTVLSEGDDQQDPIAD 334
|
170 180 190
....*....|....*....|....*....|...
gi 256270281 885 ATLGITQVFWGLDKKLAQRKHFPSINTSVSYSK 917
Cdd:PRK05688 335 SARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
739-956 |
4.07e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 106.73 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEMAEVLMEfpELYTEMsgtkepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK07721 193 GERGREVREFIER--DLGPEG-------LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAGKavalgspDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDK 898
Cdd:PRK07721 264 QREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-------NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDR 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256270281 899 KLAQRKHFPSINTSVSYSKYTNVLNKfydsnyPEFPVLRDRMKEILSNAEELEQVVQL 956
Cdd:PRK07721 337 QLANKGQYPAINVLKSVSRVMNHIVS------PEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
739-1007 |
1.10e-23 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 105.46 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEMAEvlmeFPElYTEMSGTKEpimkRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK08149 186 GERGREVTE----FVE-SLRASSRRE----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAGKAvalgspdRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDK 898
Cdd:PRK08149 257 LRDVALAAGELPARRGYPASVFDSLPRLLERPGAT-------LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 899 KLAQRKHFPSINTSVSYSKytnVLNKFYDSNYPEfpvLRDRMKEILSNAEELEQVVQL----VGKSALSDsdkITLDVAT 974
Cdd:PRK08149 330 KLAAKGHYPAIDVLKSVSR---VFGQVTDPKHRQ---LAAAFRKLLTRLEELQLFIDLgeyrRGENADND---RAMDKRP 400
|
250 260 270
....*....|....*....|....*....|...
gi 256270281 975 LIkEDFLQQNgystYDAFCPIWKTFDMMRAFIS 1007
Cdd:PRK08149 401 AL-EAFLKQD----VAEKSSFSDTLERLNEFAA 428
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
730-917 |
4.64e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 103.63 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEvlmeFPElytEMSGTKEpiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIA 809
Cdd:PRK08972 188 ADVIVVGLVGERGREVKE----FIE---EILGEEG--RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKavalGSPDRtGSVSIVAAVSPAGGDFSDPVTTATLGI 889
Cdd:PRK08972 259 DSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN----GGPGQ-GSITAFYTVLTEGDDLQDPIADASRAI 333
|
170 180
....*....|....*....|....*...
gi 256270281 890 TQVFWGLDKKLAQRKHFPSINTSVSYSK 917
Cdd:PRK08972 334 LDGHIVLSRELADSGHYPAIDIEASISR 361
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
739-991 |
1.29e-22 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 102.15 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEmaevLMEFPELYTEMSGtkepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK09099 198 GERGRE----VREFIELILGEDG-----MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAGKAvalgspdRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDK 898
Cdd:PRK09099 269 QREIGLAAGEPPARRGFPPSVFAELPRLLERAGMG-------ETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 899 KLAQRKHFPSINTSVSYSKytnVLNKFYDSNYPEFPvlrDRMKEILSNAEELEQVVQL----VGKSALSDSDKITLDVAt 974
Cdd:PRK09099 342 EIAARNQYPAIDVLGSLSR---VMPQVVPREHVQAA---GRLRQLLAKHREVETLLQVgeyrAGSDPVADEAIAKIDAI- 414
|
250
....*....|....*....
gi 256270281 975 likEDFLQQ--NGYSTYDA 991
Cdd:PRK09099 415 ---RDFLSQrtDEYSDPDA 430
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
730-984 |
1.34e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 102.36 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEVLMEfpELYTEmsGtkepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIA 809
Cdd:PRK08927 184 ADVSVIGLIGERGREVQEFLQD--DLGPE--G-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGkavalgsPDRTGSVSIVA--AVSPAGGDFSDPVTTATL 887
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG-------PGPIGEGTITGlfTVLVDGDDHNEPVADAVR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 888 GITQVFWGLDKKLAQRKHFPSINT--SVSYSkytnvlnkFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDS 965
Cdd:PRK08927 328 GILDGHIVMERAIAERGRYPAINVlkSVSRT--------MPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDP 399
|
250 260
....*....|....*....|..
gi 256270281 966 DkitLDVATLIK---EDFLQQN 984
Cdd:PRK08927 400 E---VDEAIRLNpalEAFLRQG 418
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
733-917 |
3.22e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 101.23 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 733 VVVHNCGERGNEMAEVLmefpelytemSGTKEPIMKRTTLVANTSN-MPVAAREASIyTGITLAEYFRDQGKNVSMIADS 811
Cdd:PRK06002 194 VVIALVGERGREVREFL----------EDTLADNLKKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 812 SSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKavalgSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQ 891
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGP-----GAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
170 180
....*....|....*....|....*.
gi 256270281 892 VFWGLDKKLAQRKHFPSINTSVSYSK 917
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
734-984 |
1.89e-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: 99.02 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 734 VVHNCGER---GNEmaevlmefpeLYTEMSGTKepIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRD-QGKNVSMIA 809
Cdd:TIGR01039 176 VFAGVGERtreGND----------LYHEMKESG--VIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFI 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAgkavalgSPDRTGSVSIVAAVSPAGGDFSDP---VTTAT 886
Cdd:TIGR01039 244 DNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI-------TSTKTGSITSVQAVYVPADDLTDPapaTTFAH 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 887 LGITQVfwgLDKKLAQRKHFPSINTSVSYSKYTN---VLNKFYDsnypefpVLRDrMKEILSNAEELEQVVQLVGKSALS 963
Cdd:TIGR01039 317 LDATTV---LSRKIAELGIYPAVDPLDSTSRLLDpsvVGEEHYD-------VARG-VQQILQRYKELQDIIAILGMDELS 385
|
250 260
....*....|....*....|.
gi 256270281 964 DSDKITLDVATLIkEDFLQQN 984
Cdd:TIGR01039 386 EEDKLTVERARRI-QRFLSQP 405
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
730-993 |
2.24e-20 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 95.62 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEvlmeFPELYTEMSGtkepiMKRTTLVANTSNM-PVAAREASIYtGITLAEYFRDQGKNVSMI 808
Cdd:PRK07960 201 ADVIVVGLIGERGREVKD----FIENILGAEG-----RARSVVIAAPADVsPLLRMQGAAY-ATRIAEDFRDRGQHVLLI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 809 ADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGspdrtGSVSIVAAVSPAGGDFSDPVTTATLG 888
Cdd:PRK07960 271 MDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGG-----GSITAFYTVLTEGDDQQDPIADSARA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 889 ITQVFWGLDKKLAQRKHFPSINTSVSYSK-YTNVLNKFYDSNYPEFpvlrdrmKEILSNAEELEQVVQLVGKSALSDSdk 967
Cdd:PRK07960 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRaMTALIDEQHYARVRQF-------KQLLSSFQRNRDLVSVGAYAKGSDP-- 416
|
250 260 270
....*....|....*....|....*....|.
gi 256270281 968 iTLDVATLI---KEDFLQQNGY--STYDAFC 993
Cdd:PRK07960 417 -MLDKAIALwpqLEAFLQQGIFerADWEDSL 446
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
767-983 |
6.00e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 94.12 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLAS 845
Cdd:PRK04196 203 LERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLAT 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 846 FYERAGKAValgspDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSK------ 917
Cdd:PRK04196 283 IYERAGRIK-----GKKGSITQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLSRlmkdgi 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256270281 918 ---YT-----NVLNKFYDSnYpefpvlrdrmkeilSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQ 983
Cdd:PRK04196 356 gegKTredhkDVANQLYAA-Y--------------ARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
739-956 |
1.33e-19 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 93.09 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEMAEVLmefpelytEMSGTKEPiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK07594 190 GERGREVREFI--------DFTLSEET-RKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAGkavaLGSpdrTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDK 898
Cdd:PRK07594 261 AREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSR 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256270281 899 KLAQRKHFPSINTSVSYSKYTNVLNKfydsnyPEFPVLRDRMKEILSNAEELEQVVQL 956
Cdd:PRK07594 334 RLAERGHYPAIDVLATLSRVFPVVTS------HEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
767-917 |
1.72e-19 |
|
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: 89.97 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAReasIYT---GITLAEYFR-DQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAK 842
Cdd:cd01135 129 LERVVLFLNLANDPTIER---IITprmALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTD 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256270281 843 LASFYERAGKAvalgsPDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSK 917
Cdd:cd01135 206 LATIYERAGRV-----EGRKGSITQIPILTMPNDDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
767-1005 |
2.13e-18 |
|
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: 89.40 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQ-GKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLAS 845
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 846 FYERAGKAVAlgspdRTGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSK------ 917
Cdd:TIGR01040 290 IYERAGRVEG-----RNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLSRlmksai 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 918 --------YTNVLNKFYdSNYpefpvlrdrmkEILSNAEELEQVvqlVGKSALSDSDKITLDVATLIKEDFLQQNGYSTY 989
Cdd:TIGR01040 363 gegmtrkdHSDVSNQLY-ACY-----------AIGKDVQAMKAV---VGEEALSSEDLLYLEFLDKFEKNFIAQGPYENR 427
|
250
....*....|....*.
gi 256270281 990 DAFCPIWKTFDMMRAF 1005
Cdd:TIGR01040 428 TIFESLDIAWQLLRIF 443
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
730-917 |
2.58e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 88.79 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 730 ANQVVVHNCGERGNEMAEvlmefpelYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGiTLAEYFRDQGKNVSMIA 809
Cdd:PRK07196 181 ADVVVVGLIGERGREVKE--------FIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCH-AIATYYRDKGHDVLLLV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAvalgspDRTGSVSIVAAVSPAGGDFSDPVTTATLGI 889
Cdd:PRK07196 252 DSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNS------SGNGTMTAIYTVLAEGDDQQDPIVDCARAV 325
|
170 180
....*....|....*....|....*...
gi 256270281 890 TQVFWGLDKKLAQRKHFPSINTSVSYSK 917
Cdd:PRK07196 326 LDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
734-984 |
1.89e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 80.11 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 734 VVHNCGERGNEMaevlmefPELYTEMSGTKepiMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSS 813
Cdd:PRK08472 187 VVALIGERGREI-------PEFIEKNLGGD---LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 814 RWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAvalgspDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVF 893
Cdd:PRK08472 257 RFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKE------EGKGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 894 WGLDKKLAQRKHFPSINTSVSYSKYTNvlnkfyDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDkitLDVA 973
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMN------DIISPEHKLAARKFKRLYSLLKENEVLIRIGAYQKGNDKE---LDEA 401
|
250
....*....|....
gi 256270281 974 TLIK---EDFLQQN 984
Cdd:PRK08472 402 ISKKefmEQFLKQN 415
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
28-90 |
2.98e-15 |
|
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: 71.42 E-value: 2.98e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256270281 28 IYSVSGPVVIAENMIG--CAMYELVKVGHDN----LVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTG 90
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGrlPGLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
734-956 |
4.43e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 78.87 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 734 VVHNCGERGNEMAEVLMEfpELytemsgtKEPIMKRTTLVANTSNMP--VAAREASIYTGItlAEYFRDQGKNVSMIADS 811
Cdd:PRK06793 186 VISLVGERGREVKDFIRK--EL-------GEEGMRKSVVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 812 SSRWAEALREISGRLGEMPADqGFPAYLGAKLASFYERAGKAvalgspdRTGSVSIVAAVSPAGGDFSDPVTTATLGITQ 891
Cdd:PRK06793 255 VTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKT-------QKGSITGIYTVLVDGDDLNGPVPDLARGILD 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256270281 892 VFWGLDKKLAQRKHFPSINTSVSYSKytnVLNKFYDSNYPEfpvLRDRMKEILSNAEELEQVVQL 956
Cdd:PRK06793 327 GHIVLKRELATLSHYPAISVLDSVSR---IMEEIVSPNHWQ---LANEMRKILSIYKENELYFKL 385
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
739-983 |
7.06e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 78.54 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GER---GNEmaevlmefpeLYTEM--SG---TKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGK-NVSMIA 809
Cdd:CHL00060 199 GERtreGND----------LYMEMkeSGvinEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 810 DSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAgkavalgSPDRTGSV-SIVAAVSPAgGDFSDPV---TTA 885
Cdd:CHL00060 269 DNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSItSIQAVYVPA-DDLTDPApatTFA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 886 TLGITQVfwgLDKKLAQRKHFPSINTSVSYSKYTN---VLNKFYDSNypefpvlrDRMKEILSNAEELEQVVQLVGKSAL 962
Cdd:CHL00060 341 HLDATTV---LSRGLAAKGIYPAVDPLDSTSTMLQpriVGEEHYETA--------QRVKQTLQRYKELQDIIAILGLDEL 409
|
250 260
....*....|....*....|.
gi 256270281 963 SDSDKITLDVATLIkEDFLQQ 983
Cdd:CHL00060 410 SEEDRLTVARARKI-ERFLSQ 429
|
|
| Hop |
COG1372 |
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ... |
491-829 |
1.93e-14 |
|
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];
Pssm-ID: 440983 [Multi-domain] Cd Length: 866 Bit Score: 78.01 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 491 LAYLLGLWIGDG-LSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYskvVRGNGVRnnlntenpL 569
Cdd:COG1372 212 LAYLLGLLLGDGsLSKRGAGRFTNADEELLEDVAEAAEELFGRADEGPRVEARRATVYEVR---VSSKPLA--------E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 570 WDAIIGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVtDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAE 649
Cdd:COG1372 281 LLEELGLFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSV-SNRGGRIRLSTTSRRLAEQVQLLLLRLGIVSRIYER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 650 PAKvdmNGtKHKISYAIYMSGGDVLLN-------------------------------VLSKCAGSKKFRPAPVATFVRE 698
Cdd:COG1372 360 RRP---DG-KGRTAYRLRISGGDNLRRfaerigfgssrkqerlaellaalrrrkddlvRARELANGRRLSRERLRRLALE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 699 CQ--------GFYF----ELQELKENDYYGITLSDdsDHQFlLANQVVVHNCGERgnEMAEVLMEFPELYtemsgtkepi 766
Cdd:COG1372 436 DEalealadsDVYWdevvSIEPVGEEDVYDLTVPG--THNF-VANGIVVHNSGGA--LDDVGAAVLDEDL---------- 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256270281 767 mKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEM 829
Cdd:COG1372 501 -LGGEPEEGEAGGAAEDKDRAKTGATTLAAGDLLVERDVEAEPEEIEDVISGEGRILERAALL 562
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
739-917 |
4.73e-14 |
|
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: 73.79 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GER---GNEmaevlmefpeLYTEM--SG-TKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQ-GKNVSMIADS 811
Cdd:cd01133 105 GERtreGND----------LYHEMkeSGvINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDN 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 812 SSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAgkavalgSPDRTGSVSIVAAVSPAGGDFSDP--VTT-ATLG 888
Cdd:cd01133 175 IFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERI-------TSTKKGSITSVQAVYVPADDLTDPapATTfAHLD 247
|
170 180
....*....|....*....|....*....
gi 256270281 889 ITQVfwgLDKKLAQRKHFPSINTSVSYSK 917
Cdd:cd01133 248 ATTV---LSRGIAELGIYPAVDPLDSTSR 273
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
237-284 |
9.38e-14 |
|
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: 71.23 E-value: 9.38e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 256270281 237 GQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGC 284
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALI 48
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
739-851 |
1.12e-13 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 74.56 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GERGNEMAEVLMEFPElytemsGTKEpimKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEA 818
Cdd:PRK05922 192 GERGREVREYIEQHKE------GLAA---QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAA 262
|
90 100 110
....*....|....*....|....*....|...
gi 256270281 819 LREISGRLGEMPADQGFPAYLGAKLASFYERAG 851
Cdd:PRK05922 263 LQEVALARGETLSAHHYAASVFHHVSEFTERAG 295
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
213-291 |
3.86e-13 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 70.95 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 213 YHTWPVRVPRP-VTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNS---DAIIYVGCFAKG 288
Cdd:cd19476 29 KQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGERG 108
|
...
gi 256270281 289 TNV 291
Cdd:cd19476 109 REV 111
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
767-917 |
3.35e-12 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 67.97 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPA---YLGAKL 843
Cdd:cd01132 125 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256270281 844 asfYERAGKavaLGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSK 917
Cdd:cd01132 205 ---LERAAK---LSDELGGGSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAINVGLSVSR 272
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
739-984 |
3.87e-12 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 69.73 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 739 GER---GNEmaevlmefpeLYTEMSGTKepIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRD-QGKNVSMIADSSSR 814
Cdd:COG0055 184 GERtreGND----------LYREMKESG--VLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 815 WAEALREISGRLGEMPADQGFPAYLGAKLASFYERAgkavalgSPDRTGSVSIVAAV-SPAgGDFSDP--VTTAT-LGIT 890
Cdd:COG0055 252 FTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERI-------TSTKKGSITSVQAVyVPA-DDLTDPapATTFAhLDAT 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 891 QVfwgLDKKLAQRKHFPSINTSVSYSKYTN---VLNKFYDsnypefpVLRdRMKEILSNAEELEQVVQLVGKSALSDSDK 967
Cdd:COG0055 324 TV---LSRKIAELGIYPAVDPLDSTSRILDpliVGEEHYR-------VAR-EVQRILQRYKELQDIIAILGMDELSEEDK 392
|
250
....*....|....*..
gi 256270281 968 ITLDVATLIkEDFLQQN 984
Cdd:COG0055 393 LTVARARKI-QRFLSQP 408
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
25-91 |
5.02e-12 |
|
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: 62.33 E-value: 5.02e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256270281 25 YGAIYSVSGPVVIAENMIGCAMYELVKVGHDN------LVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGK 91
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
24-113 |
3.07e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 66.77 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 24 EYGAIYSVSGPVVIAENMIGCAMYELVKVGHDN---LVGEVIRIDGDKATIQVYEETAGLTVGDPVLR-TGKPLSVELGP 99
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNgekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSE 82
|
90
....*....|....
gi 256270281 100 GLMETIYDGIQRPL 113
Cdd:PRK04196 83 DMLGRIFDGLGRPI 96
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
767-951 |
1.01e-10 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 65.32 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPA---YLGAKL 843
Cdd:PRK13343 218 LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 844 asfYERAGK-AVALGspdrTGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSKytn 920
Cdd:PRK13343 298 ---LERAAKlSPELG----GGSLTALPIIETLAGELSAYIPTNLISITdgQIY--LDSDLFAAGQRPAVDVGLSVSR--- 365
|
170 180 190
....*....|....*....|....*....|....
gi 256270281 921 VLNKfydsnyPEFPVLRD---RMKEILSNAEELE 951
Cdd:PRK13343 366 VGGK------AQHPAIRKesgRLRLDYAQFLELE 393
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
767-917 |
1.79e-10 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 64.60 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPA---YLGAKL 843
Cdd:CHL00059 197 MEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256270281 844 asfYERAGK-AVALGSpdrtGSVSIVAAVSPAGGDFSDPVTTATLGIT--QVFwgLDKKLAQRKHFPSINTSVSYSK 917
Cdd:CHL00059 277 ---LERAAKlSSQLGE----GSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINVGISVSR 344
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
767-917 |
5.60e-09 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 60.05 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPA---YLGAKL 843
Cdd:PTZ00185 253 LRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL 332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256270281 844 asfYERAgkavALGSPDR-TGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSK 917
Cdd:PTZ00185 333 ---LERA----AMLSPGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| HintN |
smart00306 |
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ... |
283-388 |
7.67e-09 |
|
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.
Pssm-ID: 197642 [Multi-domain] Cd Length: 100 Bit Score: 54.20 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 283 GCFAKGTNVLMADGSIECIENIEVGNKVMGKDG-------RPREVIKLPRGRETMYSVVQKSQHrahksdssrevpellK 355
Cdd:smart00306 1 GCFPGDTLVLTEDGGIKKIEELEEGDKVLALDEgtlkyspVKVFLVREPKGEKKFYRIKTENGR---------------E 65
|
90 100 110
....*....|....*....|....*....|....
gi 256270281 356 FTCNATHELVVRTPRSVR-RLSRTIKGVEYFEVI 388
Cdd:smart00306 66 ITLTPDHLLLVRDGGKLVwVFASELKPGDYVLVP 99
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
767-891 |
1.17e-08 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 58.51 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLAS 845
Cdd:PRK02118 194 LDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLAS 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 256270281 846 FYEragKAVALgsPDrTGSVSIVAAVSPAGGDFSDPVTTATLGITQ 891
Cdd:PRK02118 274 RYE---KAVDF--ED-GGSITIIAVTTMPGDDVTHPVPDNTGYITE 313
|
|
| 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 ... |
24-91 |
2.16e-08 |
|
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: 52.05 E-value: 2.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256270281 24 EYGAIYSVSGPVVIAENMIGCAMYELVKVGHDN---LVGEVIRIDGDKATIQVYEETAGLTVGDPVLR-TGK 91
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDgevRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRfTGE 72
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
25-112 |
6.12e-08 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 56.20 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 25 YGAIYSVSGPV--VIAEnmiGCAMYEL--VKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPG 100
Cdd:PRK02118 5 YTKITDITGNVitVEAE---GVGYGELatVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSES 81
|
90
....*....|..
gi 256270281 101 LMETIYDGIQRP 112
Cdd:PRK02118 82 LLGRRFNGSGKP 93
|
|
| Hint |
cd00081 |
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ... |
284-373 |
4.78e-06 |
|
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.
Pssm-ID: 238035 [Multi-domain] Cd Length: 136 Bit Score: 47.26 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 284 CFAKGTNVLMADGSIECIENIEV--GNKVMGKD----GRPREVIKLPR--GRETMYSVVQKSQHrahksdssrevpellK 355
Cdd:cd00081 1 CFTGDTLVLLEDGGRKKIEELVEkkGDKVLALDetgkLVFSKVLKVLRrdYEKKFYKIKTESGR---------------E 65
|
90
....*....|....*...
gi 256270281 356 FTCNATHELVVRTPRSVR 373
Cdd:cd00081 66 ITLTPDHLLFVLEDGELK 83
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
937-987 |
5.49e-06 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 45.13 E-value: 5.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 256270281 937 RDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIkEDFLQQNGYS 987
Cdd:cd01429 5 ARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRL-EEFLQQGQFE 54
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
767-823 |
7.47e-06 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 49.68 E-value: 7.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 256270281 767 MKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREIS 823
Cdd:PRK09281 218 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLS 274
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
24-113 |
3.40e-05 |
|
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: 47.79 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 24 EYGAIYSVSGPVVIAENMIGCAMYELVKVG-HDNLV--GEVIRIDGDKATIQVYEETAGLTVGDPVLR-TGKPLSVELGP 99
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTlPDGTVrsGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEfTGDILRTPVSE 80
|
90
....*....|....
gi 256270281 100 GLMETIYDGIQRPL 113
Cdd:TIGR01040 81 DMLGRVFNGSGKPI 94
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
25-113 |
7.56e-05 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 46.48 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 25 YGAIYSVSGPVVIAEnMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMET 104
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
....*....
gi 256270281 105 IYDGIQRPL 113
Cdd:PRK07594 101 VIDGFGRPL 109
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-113 |
2.03e-04 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 45.29 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 2 AGAIENARKEIKRISLEDHAEsEYGAIYSVSGPVVIAENMIGCAMYELVKVGhDNLVGEVIRIDGDKATIQVYEETAGLT 81
Cdd:PRK13343 6 DEWLARIRQRIARYEPQPDAR-EIGRVESVGDGIAFVSGLPDAALDELLRFE-GGSRGFAFNLEEELVGAVLLDDTADIL 83
|
90 100 110
....*....|....*....|....*....|..
gi 256270281 82 VGDPVLRTGKPLSVELGPGLMETIYDGIQRPL 113
Cdd:PRK13343 84 AGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPL 115
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
221-282 |
2.12e-04 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 44.99 E-value: 2.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256270281 221 PRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLskYSNSDAIIYV 282
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNML--IEHSEADVFV 181
|
|
| Intein_splicing |
pfam14890 |
Intein splicing domain; Inteins are segments of protein which excise themselves from a ... |
511-737 |
3.07e-04 |
|
Intein splicing domain; Inteins are segments of protein which excise themselves from a precursor protein and mediate the rejoining of the remainder of the precursor (the extein). Most inteins consist of a splicing domain which is split into two segments by a homing endonuclease domain. This domain represents the splicing domain.
Pssm-ID: 434290 [Multi-domain] Cd Length: 378 Bit Score: 44.37 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 511 VDSRDTSLMERVTEYAEKLnlcaeYKDRKEPQVAKTVNLYSKV--VRGNGVRNNLNTENPLWDAIIGLGFLKDGVKNIPS 588
Cdd:pfam14890 142 KYTREIPLKELIEWIEEEL-----FGDVINPRIKPERKFWYQVglVAGDGLTHDKKNPIAKWLESLEIFGLLSYNKFIPE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 589 FLSTDNIGTRETFLAGLIDSDGYVTdEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKvDMNGtkhkisYAIYM 668
Cdd:pfam14890 217 FVFSLPKGAIASFIRGYFDTDGCIS-KRNPGIYLSSTSERLAEDVQLLLLSLGINARLSKINGK-GRNV------YHVLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256270281 669 SGGDVLLNVLSKCAGSKKFRPAPVATFV-------RECQGFYFELQELKENDYY-----GITLSDD---------SDHQF 727
Cdd:pfam14890 289 TGKSSLEKFKEKIGAYLQIKKEKLEEILnkykqsnAESSEVKDFLEWLINSDVYwdkvkSIEVLDEeeyvydltvEGYHN 368
|
250
....*....|
gi 256270281 728 LLANQVVVHN 737
Cdd:pfam14890 369 FVANGIIVHN 378
|
|
| HintC |
smart00305 |
Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. ... |
699-741 |
2.82e-03 |
|
Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. Domain has been split to accommodate large insertions of endonucleases.
Pssm-ID: 197641 Cd Length: 46 Bit Score: 36.77 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 256270281 699 CQGFYF----ELQELKENDYYGITLSDDsdHQFLlANQVVVHNCGER 741
Cdd:smart00305 1 EGDFRFvrvkSIEETEYTGVYDPTVTEN--HNFI-ANGILVHNCAEI 44
|
|
| |
