|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
10-832 |
0e+00 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 1054.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 10 LNPICFRALEQAAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIQRAQAQFKTGCTRMPVFSVHL 89
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 90 IELLEGAILQAT--FQRiPLVRSALLLLTLLTRERLRSQLAQGMPLLLQLPAAELESQWQNWCRNSVEEAADPDKGES-- 165
Cdd:TIGR03345 81 VELLQEAWLLASleLGD-GRIRSGHLLLALLTDPELRRLLGSISPELAKIDREALREALPALVEGSAEASAAAADAAPag 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 166 ---PKREGGVLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAEASVPP 242
Cdd:TIGR03345 160 aaaGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 243 PLRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSPQPIILFIDEAHTLIGAGGAEGGNDAANLLKPALARGELRT 322
Cdd:TIGR03345 240 ALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 323 IAATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQLPDKA 402
Cdd:TIGR03345 320 IAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 403 ISVLDTACARVALAQHDVPPQLEEIRQQQAAIEEESERLNRELLVGVDHHDRLCELEAQAEKLHQQAREVEGRWQDERQR 482
Cdd:TIGR03345 400 VSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALGADHDERLAELRAELAALEAELAALEARWQQEKEL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 483 VGELQAARQRML-DLSARLDDDEELEQELVEcaaligkLETAAAQLRDEVPLVPDCVDPATVASVISGWTGIPIGQMQTD 561
Cdd:TIGR03345 480 VEAILALRAELEaDADAPADDDDALRAQLAE-------LEAALASAQGEEPLVFPEVDAQAVAEVVADWTGIPVGRMVRD 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 562 EAHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITINL 641
Cdd:TIGR03345 553 EIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 642 SEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGTGLIVDFKNTVM 721
Cdd:TIGR03345 633 SEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVI 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 722 LATSNVGAELILDT---PAAELNSERFNKALREELLCHFRPAFLARMTTVAYRALDEEILKGIVLAKLEKLSQRYFVATG 798
Cdd:TIGR03345 713 LLTSNAGSDLIMALcadPETAPDPEALLEALRPELLKVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLDRIARRLKENHG 792
|
810 820 830
....*....|....*....|....*....|....*.
gi 2197300106 799 EKLNMEDGLVERVMEKCKGV--GARDVENLVVGEVM 832
Cdd:TIGR03345 793 AELVYSEALVEHIVARCTEVesGARNIDAILNQTLL 828
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
9-832 |
0e+00 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 955.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 9 RLNPICFRALEQAAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIQRAQAQFK--TGCTRMPVFS 86
Cdd:COG0542 5 KFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPkvSGSSGQPYLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 87 VHLIELLEGAILQATFQRIPLVRSAL--LLLTLLTRERLRSQLAQgmpllLQLPAAELESQWQNWCRNSveeaadPDKGE 164
Cdd:COG0542 85 PRLKRVLELAELEARKLGDEYISTEHllLALLREGEGVAARILKK-----LGITLEALREALEELRGGS------RVTSQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 165 SPKREGGVLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAEASVPPPL 244
Cdd:COG0542 154 NPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 245 RDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSPQPIILFIDEAHTLIGAGGAEGGNDAANLLKPALARGELRTIA 324
Cdd:COG0542 234 KDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 325 ATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQLPDKAIS 404
Cdd:COG0542 314 ATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 405 VLDTACARVALAQHDVPPQLEEIRQQQAAIEEESERLNRELLVGvdHHDRLCELEAQAEKLHQQAREVEGRWQDERQRVG 484
Cdd:COG0542 394 LIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEA--SFERLAELRDELAELEEELEALKARWEAEKELIE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 485 ELQAARqrmldlsarldddEELEQELVECAALIGKLETAAAQLRDEVPLVPDCVDPATVASVISGWTGIPIGQMQTDEAH 564
Cdd:COG0542 472 EIQELK-------------EELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGERE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 565 ALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITINLSEY 644
Cdd:COG0542 539 KLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEY 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 645 QEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGTGLIVDFKNTVMLAT 724
Cdd:COG0542 619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 725 SNVGAELILDTPAAELNSERFNKALREELLCHFRPAFLARMT-TVAYRALDEEILKGIVLAKLEKLSQRyFVATGEKLNM 803
Cdd:COG0542 699 SNIGSELILDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDeIIVFHPLSKEELRKIVDLQLKRLRKR-LAERGITLEL 777
|
810 820 830
....*....|....*....|....*....|.
gi 2197300106 804 EDGLVERVMEKCKGV--GARDVENLVVGEVM 832
Cdd:COG0542 778 TDAAKDFLAEKGYDPeyGARPLKRAIQRELE 808
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
17-792 |
0e+00 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 650.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 17 ALEQAAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIQRAQAqfktgctRMPVFSVHLIELLEGA 96
Cdd:TIGR03346 8 ALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELE-------RLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 97 ILQATFQRiplvrsalllltlltrerlRSQLAQGMP--------LLLQL-----PAAELESQwQNWCRNSVEEAADPDKG 163
Cdd:TIGR03346 81 DLNRLLNL-------------------AEKLAQKRGdefissehLLLALlddkgTLGKLLKE-AGATADALEAAINAVRG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 164 ------ESPKREGGVLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAE 237
Cdd:TIGR03346 141 gqkvtdANAEDQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 238 ASVPPPLRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSPQPIILFIDEAHTLIGAGGAEGGNDAANLLKPALAR 317
Cdd:TIGR03346 221 GDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALAR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 318 GELRTIAATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQ 397
Cdd:TIGR03346 301 GELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 398 LPDKAISVLDTACARVALAQHDVPPQLEEIRQQQAAIEEESERLNREllVGVDHHDRLCELEAQAEKLHQQAREVEGRWQ 477
Cdd:TIGR03346 381 LPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKE--KDEASKKRLEDLEKELADLEEEYAELEEQWK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 478 DERQRVGELQAARQRMLDLSARLDDDE---------ELEQELVecAALIGKLETAAAQLRDEVP-LVPDCVDPATVASVI 547
Cdd:TIGR03346 459 AEKASIQGIQQIKEEIEQVRLELEQAEregdlakaaELQYGKL--PELEKQLQAAEQKLGEEQNrLLREEVTAEEIAEVV 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 548 SGWTGIPIGQMQTDEAHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALAD 627
Cdd:TIGR03346 537 SRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 628 ALYGGERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVME 707
Cdd:TIGR03346 617 FLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLT 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 708 DGTGLIVDFKNTVMLATSNVGAELILDTPAAElNSERFNKALREELLCHFRPAFLARM-TTVAYRALDEEILKGIVLAKL 786
Cdd:TIGR03346 697 DGQGRTVDFRNTVIIMTSNLGSDFIQELAGGD-DYEEMREAVMEVLRAHFRPEFLNRIdEIVVFHPLGREQIARIVEIQL 775
|
....*.
gi 2197300106 787 EKLSQR 792
Cdd:TIGR03346 776 GRLRKR 781
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
2-777 |
3.05e-173 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 521.15 E-value: 3.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 2 DLKALVKRLN-------PICFRA---LEQAAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIqra 71
Cdd:CHL00095 62 EVEKIIGRGTgfvaveiPFTPRAkrvLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLI--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 72 qaqfktgctrmpvfsvhlIELLEgailqatfqriplvrsalllltlltrerlrsqlaqgmplllqlpaaelesqwqnwcr 151
Cdd:CHL00095 139 ------------------LNLIG--------------------------------------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 152 NSVEEAADPDKGESPKReggVLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGL 231
Cdd:CHL00095 144 EIIEAILGAEQSRSKTP---TLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 232 ALRIAEASVPPPLRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSpQPIILFIDEAHTLIGAGGAEGGNDAANLL 311
Cdd:CHL00095 221 AQRIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANIL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 312 KPALARGELRTIAATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQR 391
Cdd:CHL00095 300 KPALARGELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 392 YISGRQLPDKAISVLDTACARVALAQHDVPPQLEEIRQQQAAIEEESERLNREllvgvdhHDrlceLEAQAEKLhqqARE 471
Cdd:CHL00095 380 YIADRFLPDKAIDLLDEAGSRVRLINSRLPPAARELDKELREILKDKDEAIRE-------QD----FETAKQLR---DRE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 472 VEGRWQderqrvgelqaarqrmldlsarldddeeleqelveCAALIGKLETAaaqlrDEVPLVPDCVDPATVASVISGWT 551
Cdd:CHL00095 446 MEVRAQ-----------------------------------IAAIIQSKKTE-----EEKRLEVPVVTEEDIAEIVSAWT 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 552 GIPIGQMQTDEAHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALYG 631
Cdd:CHL00095 486 GIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFG 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 632 GERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGTG 711
Cdd:CHL00095 566 SEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKG 645
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197300106 712 LIVDFKNTVMLATSNVGAELIL-----------DTPAAELNSERFNKALREELLCHFRPAFLARmttvayraLDEEI 777
Cdd:CHL00095 646 RTIDFKNTLIIMTSNLGSKVIEtnsgglgfelsENQLSEKQYKRLSNLVNEELKQFFRPEFLNR--------LDEII 714
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
8-827 |
3.26e-171 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 512.65 E-value: 3.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 8 KRLNPICFRALEQAAERSraqgHWFVEPEHMLLALLDDEhcDLAYCLSNAAISTDTLREEIQR----AQAQFKTGCTRMP 83
Cdd:TIGR02639 3 EELERILSDALEEAKERR----HEFVTLEHLLLALLDDN--EAIEILEECGGDVELLRKRLEDyleeNLPVIPEDIDEEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 84 VFSVHLIELLEGAILQATFQRIPLVRSALLLLTLLTRERLRSQLAQGMPLLLQLPAAELESQwQNWCRNSVEEAADPDKG 163
Cdd:TIGR02639 77 EQTVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISH-GISKDDGKDQLGEEAGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 164 ESPKREGGvLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAEASVPPP 243
Cdd:TIGR02639 156 EEEKGQDA-LEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 244 LRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSPQPIiLFIDEAHTLIGAGGAEGGN-DAANLLKPALARGELRT 322
Cdd:TIGR02639 235 LKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAI-LFIDEIHTIVGAGATSGGSmDASNLLKPALSSGKIRC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 323 IAATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQLPDKA 402
Cdd:TIGR02639 314 IGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 403 ISVLDTACARValaqhdvppqleeirqqqaaieeeseRLNRellvgvdhhdrlceleaqaeklhqqarevegrwqderqr 482
Cdd:TIGR02639 394 IDVIDEAGAAF--------------------------RLRP--------------------------------------- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 483 vgelqaarqrmldlsarldddeeleqelvecaaliGKLETAAAQLRDevplvpdcvdpatVASVISGWTGIPIGQMQTDE 562
Cdd:TIGR02639 409 -----------------------------------KAKKKANVNVKD-------------IENVVAKMAKIPVKTVSSDD 440
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 563 AHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALyggERNLITINLS 642
Cdd:TIGR02639 441 REQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDMS 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 643 EYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGTGLIVDFKNTVML 722
Cdd:TIGR02639 518 EYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILI 597
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 723 ATSNVGAELILDTP---AAELNSERFNKALREellcHFRPAFLARMT-TVAYRALDEEILKGIVLAKLEKLSQRyFVATG 798
Cdd:TIGR02639 598 MTSNAGASEMSKPPigfGGENRESKSLKAIKK----LFSPEFRNRLDaIIHFNDLSEEMAEKIVKKFLDELQDQ-LNEKN 672
|
810 820 830
....*....|....*....|....*....|.
gi 2197300106 799 EKLNMEDGLVERVMEKC--KGVGARDVENLV 827
Cdd:TIGR02639 673 IELELTDDAKKYLAEKGydEEFGARPLARVI 703
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
17-792 |
1.18e-165 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 502.84 E-value: 1.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 17 ALEQAAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIQRAQAQFK----TGCTRMPvfSVHLIEL 92
Cdd:PRK10865 13 ALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPqvegTGGDVQP--SQDLVRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 93 LEGAILQATFQRIPLVRSALLLLTLLTRERLRSQLaqgmplllqLPAAELESQwqnwcrnSVEEAADPDKGESPKREGGV 172
Cdd:PRK10865 91 LNLCDKLAQKRGDNFISSELFVLAALESRGTLADI---------LKAAGATTA-------NITQAIEQMRGGESVNDQGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 173 LDQ------YTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAEASVPPPLRD 246
Cdd:PRK10865 155 EDQrqalkkYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 247 VALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSPQPIILFIDEAHTLIGAGGAEGGNDAANLLKPALARGELRTIAAT 326
Cdd:PRK10865 235 RRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 327 TWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQLPDKAISVL 406
Cdd:PRK10865 315 TLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 407 DTACARVALAQHDVPPQLE-------EIRQQQAAIEEESERLNREllvgvdhhdRLCELEAQAEKLHQQAREVEGRWQDE 479
Cdd:PRK10865 395 DEAASSIRMQIDSKPEELDrldrriiQLKLEQQALMKESDEASKK---------RLDMLNEELSDKERQYSELEEEWKAE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 480 RQRV-------GELQAAR------QRMLDLsARLDDDE-----ELEQELVECAALIGKletaaaqlrdEVPLVPDCVDPA 541
Cdd:PRK10865 466 KASLsgtqtikAELEQAKiaieqaRRVGDL-ARMSELQygkipELEKQLAAATQLEGK----------TMRLLRNKVTDA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 542 TVASVISGWTGIPIGQMQTDEAHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTET 621
Cdd:PRK10865 535 EIAEVLARWTGIPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTEL 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 622 AYALADALYGGERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVF 701
Cdd:PRK10865 615 CKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVL 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 702 DKGVMEDGTGLIVDFKNTVMLATSNVGAELILDTpAAELNSERFNKALREELLCHFRPAFLARM-TTVAYRALDEEILKG 780
Cdd:PRK10865 695 DDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQER-FGELDYAHMKELVLGVVSHNFRPEFINRIdEVVVFHPLGEQHIAS 773
|
810
....*....|..
gi 2197300106 781 IVLAKLEKLSQR 792
Cdd:PRK10865 774 IAQIQLQRLYKR 785
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
152-782 |
2.23e-117 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 373.79 E-value: 2.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 152 NSVEEAADPDKGESPKREGGvLDQYTHDLTRDAREGRIDPIIGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGL 231
Cdd:PRK11034 149 QSSDPGSQPNSEEQAGGEER-MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 232 ALRIAEASVPPPLRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKSpQPIILFIDEAHTLIGAGGAEGGN-DAANL 310
Cdd:PRK11034 228 AWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQD-TNSILFIDEIHTIIGAGAASGGQvDAANL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 311 LKPALARGELRTIAATTWQEYKKYFEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQ 390
Cdd:PRK11034 307 IKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 391 RYISGRQLPDKAISVLDTAcarvalaqhdvppqleeirqqqaaieeeserlnrellvgvdhhdrlceleaqaeklhqqar 470
Cdd:PRK11034 387 KYINDRHLPDKAIDVIDEA------------------------------------------------------------- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 471 evegrwqderqrvgelqAARQRMLDLSARldddeeleqelvecaaligkletaaaqlrdevplvPDCVDPATVASVISGW 550
Cdd:PRK11034 406 -----------------GARARLMPVSKR-----------------------------------KKTVNVADIESVVARI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 551 TGIPIGQMQTDEAHALRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALy 630
Cdd:PRK11034 434 ARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL- 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 631 ggERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGT 710
Cdd:PRK11034 513 --GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNN 590
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2197300106 711 GLIVDFKNTVMLATSNVGAELILDTPAAELNSERFNKALrEELLCHFRPAFLARMTTVA-YRALDEEILKGIV 782
Cdd:PRK11034 591 GRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAM-EEIKKIFTPEFRNRLDNIIwFDHLSTDVIHQVV 662
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
566-768 |
5.95e-81 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 257.88 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 566 LRTLVARMSERVMGQQAALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITINLSEYQ 645
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 646 EAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNVFDKGVMEDGTGLIVDFKNTVMLATS 725
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2197300106 726 NvgaelildtpaaelnserfnkalreellcHFRPAFLARMTTV 768
Cdd:cd19499 162 N-----------------------------HFRPEFLNRIDEI 175
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
603-765 |
1.23e-67 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 221.69 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 603 KPVGVFLLVGPTGVGKTETAYALADALYGGERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGALTEAVRRRPYSVVL 682
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 683 LDEIEKAHPDVLEAFYNVFDKGVMEDGTGLIVDFKNTVMLATSNVGAELILDTP--AAELNSERFNKALREELLCHFRPA 760
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASrlGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*
gi 2197300106 761 FLARM 765
Cdd:pfam07724 161 FLGRL 165
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
354-444 |
1.02e-35 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 130.68 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 354 DENSSVIMLRAVADKLEAHHGVQILDTAIREAVRLSQRYISGRQLPDKAISVLDTACARVALAQHDVPPQLEEIRQQQAA 433
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90
....*....|.
gi 2197300106 434 IEEESERLNRE 444
Cdd:pfam17871 81 LEIEKEALERE 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
579-746 |
1.46e-14 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 71.79 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 579 GQQAALETIAQRLRAyrsgltDPQKPVgvfLLVGPTGVGKTETAYALADALYGGERNLITINLSEYQEAHTVSqlkgapp 658
Cdd:cd00009 2 GQEEAIEALREALEL------PPPKNL---LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 659 GYVGYGSGGALTEAVRRRPYSVVLLDEIEKAHPDVLEAFYNvfdkgVMEDGTGLIVDFKNTVMLATSNVGAELILDTPAA 738
Cdd:cd00009 66 ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLR-----VLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140
|
....*...
gi 2197300106 739 ELNSERFN 746
Cdd:cd00009 141 DRLDIRIV 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
193-348 |
1.32e-13 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 69.10 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 193 IGRDAEIRQCIDILLRRRQNNPILVGAPGVGKTAVAEGLALRIAEASVPpplrdvaLLALDLGLLQAGAGVKGEFEQRLK 272
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197300106 273 GVIDAVKKSPQPIILFIDEAHTLiGAGGAEGGNDAANLLKPALA-RGELRTIAATTwqeYKKYFEKDPALDRRFQRI 348
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATN---RPLLGDLDRALYDRLDIR 146
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
608-726 |
1.98e-13 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 68.09 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 608 FLLVGPTGVGKTETAYALADALYGgeRNLITINLSEYQeahTVSQLKGA--PPGYVGYGSGGALTEAVRRRpySVVLLDE 685
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSN--RPVFYVQLTRDT---TEEDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2197300106 686 IEKAHPDVLEAFYNVFDKGVM--EDGTGLIVDFKNTVML-ATSN 726
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLllPDGGELVKAAPDGFRLiATMN 118
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
215-349 |
2.21e-11 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 61.84 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 215 ILVGAPGVGKTAVAEGLAlriAEASVP------PPLRDVALlaldlgllqagagvkGEFEQRLKGVIDAVKKSpQPIILF 288
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVA---KELGAPfieisgSELVSKYV---------------GESEKRLRELFEAAKKL-APCVIF 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 289 IDEAHTLIGAGGAEG---GNDAANLLKPALARGELRT-----IAATTwqeykkYFEK-DPALDRRFQRIQ 349
Cdd:pfam00004 63 IDEIDALAGSRGSGGdseSRRVVNQLLTELDGFTSSNskvivIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
606-727 |
4.17e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 606 GVFLLVGPTGVGKTETAYALADALYGGERNLITINLSEYQEAHTVSQLKGAPPGYVGYGSGGA----LTEAVRRRPYSVV 681
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2197300106 682 LLDEIEKAHPDVLEAfyNVFDKGVMEDGTGLIVDFKNTVMLATSNV 727
Cdd:smart00382 83 ILDEITSLLDAEQEA--LLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-355 |
4.59e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 210 RQNNPILVGAPGVGKTAVAEGLALRIAEASVP-----PPLRDVALLALDLGLLQAGAGVKGEFEQRLKGVIDAVKKsPQP 284
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK-LKP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2197300106 285 IILFIDEAHTLIGAGGAEGGNDAA--NLLKPALARGELRTIAATTWQEykkyFEKDPALDRRFQRIQIEEPDE 355
Cdd:smart00382 80 DVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLLIL 148
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
582-689 |
5.69e-08 |
|
proteases similar to RecA; 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: 410889 [Multi-domain] Cd Length: 158 Bit Score: 53.06 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 582 AALETIAQRLRAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALAdalygGE--RNLITINLSEYQEAhtvsqlkgappg 659
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALA-----GElgLPLIVVKLSSLLSK------------ 65
|
90 100 110
....*....|....*....|....*....|..
gi 2197300106 660 YVGYGSG--GALTEAVRRRPYSVVLLDEIEKA 689
Cdd:cd19481 66 YVGESEKnlRKIFERARRLAPCILFIDEIDAI 97
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
190-404 |
1.12e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 53.73 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 190 DPIIGRDAEIRQCIDIL--LRRRQN----------NPILVGAPGVGKTAVAEGLAlriAEASVPpplrdvallaldlGLL 257
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIkeLRRRENlrkfglwpprKILFYGPPGTGKTMLAEALA---GELKLP-------------LLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 258 QAGAGVKGEF----EQRLKGVIDAVKKspQPIILFIDEAHTLigagGAEGGNDAanllkpalARGELR------------ 321
Cdd:COG1223 66 VRLDSLIGSYlgetARNLRKLFDFARR--APCVIFFDEFDAI----AKDRGDQN--------DVGEVKrvvnallqeldg 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 322 ------TIAATtwqeykkYFEK--DPALDRRFQ-RIQIEEPDENSSVIML---------------RAVADKLEAHHG--- 374
Cdd:COG1223 132 lpsgsvVIAAT-------NHPEllDSALWRRFDeVIEFPLPDKEERKEILelnlkkfplpfeldlKKLAKKLEGLSGadi 204
|
250 260 270
....*....|....*....|....*....|
gi 2197300106 375 VQILDTAIREAVRLSQRYISGRQLpDKAIS 404
Cdd:COG1223 205 EKVLKTALKKAILEDREKVTKEDL-EEALK 233
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
609-726 |
1.73e-07 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 50.67 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 609 LLVGPTGVGKTETAYALADALYggeRNLITINLSEyqeahTVSQLKGAPPGYVgygsGGALTEAVRRRPySVVLLDEIEK 688
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG---APFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2197300106 689 AHP-----------DVLEAFYNVFDkgvmedgtGLIVDFKNTVMLATSN 726
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
21-71 |
1.55e-06 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 45.59 E-value: 1.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2197300106 21 AAERSRAQGHWFVEPEHMLLALLDDEHCDLAYCLSNAAISTDTLREEIQRA 71
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKL 51
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
57-398 |
6.39e-06 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 49.52 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 57 AAISTDTLREEIQRAQAQFKTGCTRMPVFSVHLIELLEGAILQATFQRIPLVRSALLLLTLLTRERLRSQLAQGMPLLLQ 136
Cdd:COG0464 29 LLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 137 LPAAELESQWQNWCRNSVEEAADPDKGESPKREGGVldqytHDLTRDAREGRIDPIIGRDAEIRQCIDIL--------LR 208
Cdd:COG0464 109 LLLLDLERALLELLRESAEALALAAPLVTYEDIGGL-----EEELLELREAILDDLGGLEEVKEELRELValplkrpeLR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 209 RRQNNP-----ILVGAPGVGKTAVAEGLA-------LRIAEASVppplrdvallaldlgllqAGAGVkGEFEQRLKGVID 276
Cdd:COG0464 184 EEYGLPpprglLLYGPPGTGKTLLARALAgelglplIEVDLSDL------------------VSKYV-GETEKNLREVFD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 277 AVKKSpQPIILFIDEAHTLIGAGGAEGGNDA----ANLLKpALA--RGELRTIAATTwqeykkYFEK-DPALDRRFQR-I 348
Cdd:COG0464 245 KARGL-APCVLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAATN------RPDLlDPALLRRFDEiI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197300106 349 QIEEPDENSSVIMLRAVADKLEAHHGV------------------QILDTAIREAVRLSQRYISGRQL 398
Cdd:COG0464 317 FFPLPDAEERLEIFRIHLRKRPLDEDVdleelaeateglsgadirNVVRRAALQALRLGREPVTTEDL 384
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
602-639 |
9.48e-06 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 46.32 E-value: 9.48e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2197300106 602 QKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITI 639
Cdd:cd01129 8 KRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITI 45
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
577-691 |
1.89e-05 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 47.99 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 577 VMGQQAALETIAQRLRAYRSGltDPQKPVgvfLLVGPTGVGKTETAYALA-DalYGGErnLITINLSEYQEAHTVSQlkg 655
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALAnD--YGWE--VIELNASDQRTADVIER--- 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 2197300106 656 appgYVGYGS-GGALTEAVRRrpysVVLLDEIEKAHP 691
Cdd:PRK04195 84 ----VAGEAAtSGSLFGARRK----LILLDEVDGIHG 112
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
606-705 |
2.33e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 44.64 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 606 GVFLLVGPTGVGKTETAYALADALYGGERNLITINLSEYQEA----HTVSQLKGAPPgyVGYGSGGALTEAV-----RRR 676
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPL--SGRLSKEELLAALqqlllALA 83
|
90 100 110
....*....|....*....|....*....|..
gi 2197300106 677 PYSVVLLDEIEKAHPDVLE---AFYNVFDKGV 705
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEelrDLLNLSSKLL 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-530 |
3.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 411 ARVALAQHDVPPQLEEIRQQQAAIEEESERLNRELLVGVDHHDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAAR 490
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2197300106 491 -QRMLDLSARLDDDEELEQELVECAALIGKLETAAAQLRDE 530
Cdd:COG1196 375 aEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
561-639 |
3.99e-05 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 46.78 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 561 DEAHAlRTLVARMSERV---MGQQAALETIAQRLRAYRSGLTDPQKpvgVFLLVGPTGVGKTETAYALA--DALYGGERN 635
Cdd:COG1419 121 SPELA-RELLEKLPEDLsaeEAWRALLEALARRLPVAEDPLLDEGG---VIALVGPTGVGKTTTIAKLAarFVLRGKKKV 196
|
....*
gi 2197300106 636 -LITI 639
Cdd:COG1419 197 aLITT 201
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
423-592 |
1.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLNRELlvgvDHHDRLCELEAQAEKLHQQAREVEgRWQDERQRV----GELQAARQRMLDLSA 498
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERR----EALQRLAEYSWDEIDVASAEREIA-ELEAELERLdassDDLAALEEQLEELEA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 499 RLDddeELEQELVECAALIGKLETAAAQLRDEVPLVPDCVDPAtvASVISGWTGIPIGQM--QTDEAHALRTLVARMSER 576
Cdd:COG4913 700 ELE---ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERfaAALGDAVERELRENLEER 774
|
170
....*....|....*.
gi 2197300106 577 VMGQQAALETIAQRLR 592
Cdd:COG4913 775 IDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
423-597 |
1.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLN--RELLVGVDH----------HDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAAR 490
Cdd:COG4913 253 LLEPIRELAERYAAARERLAelEYLRAALRLwfaqrrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 491 -----QRMLDLSARLdddEELEQELVECAALIGKLETAAAQLRDEVPLvpdcvDPATVASVISGWTGIPigQMQTDEAHA 565
Cdd:COG4913 333 rgnggDRLEQLEREI---ERLERELEERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALL--EALEEELEA 402
|
170 180 190
....*....|....*....|....*....|..
gi 2197300106 566 LRTLVARMSERVMGQQAALETIAQRLRAYRSG 597
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
402-528 |
1.47e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 402 AISVLDTA---CARVALAQHDVPPQLEEIRQQQAAIEEESERLNRELLVGVDHHDR-------LCEL--EAQAEKLHQQA 469
Cdd:PRK04863 419 AVQALERAkqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlVRKIagEVSRSEAWDVA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 470 REVEGRWQDERQRVGELQAAR----------------QRMLD-----LSARLDDDEELEQELVECAALIGKLETAAAQLR 528
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRmrlseleqrlrqqqraERLLAefckrLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-600 |
1.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 335 FEKDPALDRRFQRIQIEEPDENSSVIMLRAVADKLEAhhgvqiLDTAIREAVRLSQRYisgRQLPDKAISVLDTACARVA 414
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEE------LEEELEQLRKELEEL---SRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 415 LAQHDVPPQLEEIRQQQAAIEEESERLNREllvgvdhHDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAA----R 490
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEA-------EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 491 QRMLDLSARLdddEELEQELVECAALIGKLETAAAQLRDEVplvpdcvdpATVASVISGwTGIPIGQMQTDEAHALRtLV 570
Cdd:TIGR02168 817 EEAANLRERL---ESLERRIAATERRLEDLEEQIEELSEDI---------ESLAAEIEE-LEELIEELESELEALLN-ER 882
|
250 260 270
....*....|....*....|....*....|
gi 2197300106 571 ARMSERVMGQQAALETIAQRLRAYRSGLTD 600
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
425-527 |
1.67e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 425 EEIRQQQAAIEEESERLNREllvgvdhHDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLDLSARLDDDE 504
Cdd:PRK02224 523 ELIAERRETIEEKRERAEEL-------RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
90 100
....*....|....*....|...
gi 2197300106 505 ELEQELVECAALIGKLETAAAQL 527
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREAL 618
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
215-348 |
2.58e-04 |
|
proteases similar to RecA; 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: 410889 [Multi-domain] Cd Length: 158 Bit Score: 42.27 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 215 ILVGAPGVGKTAVAEGLAlriAEASVPP---PLRDVALLAldlgllqagagvKGEFEQRLKGVIDAVKKSpQPIILFIDE 291
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA---GELGLPLivvKLSSLLSKY------------VGESEKNLRKIFERARRL-APCILFIDE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197300106 292 AHTLIGAGGAEGGNDAANLLKPAL--------ARGELRTIAATTWQEykkyfEKDPALDR--RFQRI 348
Cdd:cd19481 94 IDAIGRKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD-----LLDPALLRpgRFDEV 155
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
433-688 |
3.06e-04 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 44.13 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 433 AIEEESERLNRELLVGVDHHDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLDLSARLDDDEELEQELVE 512
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 513 CAALIGKLETAAAQLRDEVPLVPDCVDPATVASVISGWTGIPIGQMQTDEAHALRTLVARMSErVMGQQAALETIAQRLR 592
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDD-LGGLEEVKEELRELVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 593 AYRSGLTDPQK----PVGVFLLVGPTGVGKTETAYALADALyggERNLITINLSEyqeahTVSQlkgappgYVGyGSGGA 668
Cdd:COG0464 175 LPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD-----LVSK-------YVG-ETEKN 238
|
250 260
....*....|....*....|...
gi 2197300106 669 LTEAV---RRRPYSVVLLDEIEK 688
Cdd:COG0464 239 LREVFdkaRGLAPCVLFIDEADA 261
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
607-688 |
3.64e-04 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 42.16 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 607 VFLLVGPTGVGKTETAYALADALyggERNLITINLSeyqEAHTVSQLKGAPPGYVGYGSG---GALTEAVRRRPysVVLL 683
Cdd:cd19500 39 ILCLVGPPGVGKTSLGKSIARAL---GRKFVRISLG---GVRDEAEIRGHRRTYVGAMPGriiQALKKAGTNNP--VFLL 110
|
....*
gi 2197300106 684 DEIEK 688
Cdd:cd19500 111 DEIDK 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-530 |
6.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLNRELLvgvdhhdrlcELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRmlDLSARLDD 502
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEEL 335
|
90 100
....*....|....*....|....*...
gi 2197300106 503 DEELEQELVECAALIGKLETAAAQLRDE 530
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEA 363
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
567-688 |
8.82e-04 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 41.21 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 567 RTLVARMSERVMGQQAALET--IAQRLRAYRSGLTDPQK----PVGVfLLVGPTGVGKTETAYALAdALYGGErnLITIN 640
Cdd:cd19498 3 REIVSELDKYIIGQDEAKRAvaIALRNRWRRMQLPEELRdevtPKNI-LMIGPTGVGKTEIARRLA-KLAGAP--FIKVE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2197300106 641 LSEYQEAhtvsqlkgappGYVGYGsggaLTEAVRRRPYSVVLLDEIEK 688
Cdd:cd19498 79 ATKFTEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
602-639 |
1.05e-03 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 42.49 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2197300106 602 QKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITI 639
Cdd:COG2804 310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITV 347
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
588-687 |
1.07e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.79 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 588 AQRLRAYrsGLTDPQKpvgvFLLVGPTGVGKTETAYALADALyggERNLITINLSEYqeahtVSQlkgappgYVGYGSG- 666
Cdd:COG1223 24 RENLRKF--GLWPPRK----ILFYGPPGTGKTMLAEALAGEL---KLPLLTVRLDSL-----IGS-------YLGETARn 82
|
90 100
....*....|....*....|..
gi 2197300106 667 -GALTEAVRRRPySVVLLDEIE 687
Cdd:COG1223 83 lRKLFDFARRAP-CVIFFDEFD 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
423-529 |
1.66e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLNRELLVGVDHHDrLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLD---LSAR 499
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgeLAEL 474
|
90 100 110
....*....|....*....|....*....|
gi 2197300106 500 LDDDEELEQELVECAALIGKLETAAAQLRD 529
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
154-355 |
1.73e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 41.53 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 154 VEEAADPDKGESPKREGGVLDQYTHDltrdAREGRIDPIIGRDAEIRQCIDILLRRRQNNPI-------------LVGAP 220
Cdd:COG1222 46 PALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQIEEIREAVELPLKNPELfrkygieppkgvlLYGPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 221 GVGKTAVAEGLAlriAEASVppPLRDVallaldlgllqAGAGV--K--GEFEQRLKGVIDAVKKSpQPIILFIDEAHTLI 296
Cdd:COG1222 122 GTGKTLLAKAVA---GELGA--PFIRV-----------RGSELvsKyiGEGARNVREVFELAREK-APSIIFIDEIDAIA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197300106 297 GAGGAEGGNDAANLLKPAL--------ARGELRTIAATTwqeykkYFEK-DPALDR--RFQR-IQIEEPDE 355
Cdd:COG1222 185 ARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATN------RPDLlDPALLRpgRFDRvIEVPLPDE 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-530 |
2.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLNRELlvgvdhHDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLDLSARLDD 502
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAEL------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110
....*....|....*....|....*....|..
gi 2197300106 503 ----DEELEQELVECAALIGKLETAAAQLRDE 530
Cdd:COG1196 412 llerLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
599-697 |
2.61e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.04 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 599 TDPQKPVGVFLlVGPTGVGKTETAYALADALyGGERNLITINLSEYQEAH-TVSQLKGAPP----GYVGYGSG----GAL 669
Cdd:pfam06414 6 TSQERPKAILL-GGQPGAGKTELARALLDEL-GRQGNVVRIDPDDFRELHpHYRELQAADPktasEYTQPDASrwveKLL 83
|
90 100
....*....|....*....|....*...
gi 2197300106 670 TEAVRRRpYSVVLldEIEKAHPDVLEAF 697
Cdd:pfam06414 84 QHAIENG-YNIIL--EGTLRSPDVAKKI 108
|
|
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
602-639 |
2.83e-03 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 40.51 E-value: 2.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2197300106 602 QKPVGVFLLVGPTGVGKTETAYALADALyGGERNLITI 639
Cdd:NF041000 125 QRRSGLILFSGPTGSGKTTTMYSLARKL-ALNKQVITI 161
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
602-686 |
3.73e-03 |
|
Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.
Pssm-ID: 425681 [Multi-domain] Cd Length: 269 Bit Score: 39.96 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 602 QKPVGVFLLVGPTGVGKTETAYALADALYGGERNLITINLS-EYQEAHT-VSQLKGAppgyVGYGSGGALTEAVRRRPyS 679
Cdd:pfam00437 127 RQPRGNILVTGPTGSGKTTTLYAALGELNTRDENIVTVEDPvEIQLEGInQVQLNAR----AGVTFADLLRAILRQDP-D 201
|
....*..
gi 2197300106 680 VVLLDEI 686
Cdd:pfam00437 202 RIMVGEI 208
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
191-293 |
5.21e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 191 PIIGRDAEIRQCIDILLRRRQNNP---ILVGAPGVGKTAVAEGLALRI-------------------------------- 235
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALerdggyflrgkcdenlpyspllealtregllr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2197300106 236 -----AEASVPPPLRDVALLALDLGLLQAGAGVKgEFEQRLKGVIDAVKKSPQPIILFIDEAH 293
Cdd:pfam13191 81 qlldeLESSLLEAWRAALLEALAPVPELPGDLAE-RLLDLLLRLLDLLARGERPLVLVLDDLQ 142
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
566-639 |
6.18e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 39.63 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 566 LRTLVARMSERVMGQQA---ALETIAQRLrAYRSGLTDPQKPVGVFLLVGPTGVGKTETAYALAD--ALYGGERN--LIT 638
Cdd:TIGR03499 153 ARELLEKLPEDADAEDAwrwLREALEGML-PVKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAArfALEHGKKKvaLIT 231
|
.
gi 2197300106 639 I 639
Cdd:TIGR03499 232 T 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
423-531 |
6.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 423 QLEEIRQQQAAIEEESERLNRELlvgVDHHDRLCELEAQAEkLHQQAREVEGRWQDERQRVGELQAARQRMLDLSARLDD 502
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERL---EALEAELDALQERRE-ALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100
....*....|....*....|....*....
gi 2197300106 503 DEELEQELVECAALIGKLETAAAQLRDEV 531
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEI 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-531 |
7.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 422 PQLEEIRQQQAAIEEESERLNRELLVGVDHHDRLC----ELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLD-L 496
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEaL 430
|
90 100 110
....*....|....*....|....*....|....*
gi 2197300106 497 SARLDDDEELEQELVECAALIGKLETAAAQLRDEV 531
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-530 |
9.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 362 LRAVADKLEAHHGVQildTAIREAVRLSQRYISGRQLPDKAISVLDTACARVALAQHdvppQLEEIRQQQAAIEEESerl 441
Cdd:COG4913 615 LEAELAELEEELAEA---EERLEALEAELDALQERREALQRLAEYSWDEIDVASAER----EIAELEAELERLDASS--- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300106 442 nrellvgvdhhDRLCELEAQAEKLHQQAREVEGRWQDERQRVGELQAARQRMLDLSARLDDDEElEQELVECAALIGKLE 521
Cdd:COG4913 685 -----------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE-AAEDLARLELRALLE 752
|
....*....
gi 2197300106 522 TAAAQLRDE 530
Cdd:COG4913 753 ERFAAALGD 761
|
|
| |
