|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
13-855 |
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: 1168.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 13 LDAASKRDLEMAAERCVVRGGNKILVEDLLLGLLERPESLLARALQDAEIDAGELAQALQP---RGEHSESRNPVFSAEL 89
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARaldKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 90 VQWLQDALLVANLELGASQIDQAALILALLRNP-MRYAGSRYQTLLSKLNAERLR---DFALSQQPQAAGGKAAAPG--- 162
Cdd:TIGR03345 81 VELLQEAWLLASLELGDGRIRSGHLLLALLTDPeLRRLLGSISPELAKIDREALRealPALVEGSAEASAAAADAAPaga 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 163 ------ESNLARFTHNFTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQV 236
Cdd:TIGR03345 161 aagaagTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 237 LKGVELLCLDLGLLQAGASVKGEFERRLQGVIDEVKASPKPIILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTI 316
Cdd:TIGR03345 241 LRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 317 AATTWSEYKKYFEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAV 396
Cdd:TIGR03345 321 AATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 397 DVLDTACARVRISLAAAPEALERLRGEIAEGERQGEAMRRDLDAGLNIDhEALDALETRLVAARAELEQVETRWSIQRDL 476
Cdd:TIGR03345 401 SLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALGADHD-ERLAELRAELAALEAELAALEARWQQEKEL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 477 AERLLEQRKLCAAARlAGDEEETDAPRASLEELEAELRalqaelaAAQASERLVSFEVCPRLVAEVISHWTGVPLSQLAR 556
Cdd:TIGR03345 480 VEAILALRAELEADA-DAPADDDDALRAQLAELEAALA-------SAQGEEPLVFPEVDAQAVAEVVADWTGIPVGRMVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 557 EHNTKVITFADDLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVIN 636
Cdd:TIGR03345 552 DEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITIN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 637 MSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTL 716
Cdd:TIGR03345 632 MSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 717 ILMTSNLASERIASLCAGGER-PAAEDLELAIRPQLTQHFKPALLGRMRVVPYYPMDGDLLRQLVGLKLARFGERLARR- 794
Cdd:TIGR03345 712 ILLTSNAGSDLIMALCADPETaPDPEALLEALRPELLKVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLDRIARRLKENh 791
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222379302 795 QLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQHLQPLVVDRLLDAMAAGEQLQRVHATL 855
Cdd:TIGR03345 792 GAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPIERIHLDV 852
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
17-858 |
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: 960.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 17 SKRDLEMAAERCVVRGGNKILVEDLLLGLLERPESLLARALQDAEIDAGELAQALQ---PRGEHSE--SRNPVFSAELVQ 91
Cdd:COG0542 10 AQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEealGRLPKVSgsSGQPYLSPRLKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 92 WLQDALLVANlELGASQIDQAALILALLRNPMRYAGSryqtLLSK--LNAERLRDfALSQQPQAAGGKAAAPGES--NLA 167
Cdd:COG0542 90 VLELAELEAR-KLGDEYISTEHLLLALLREGEGVAAR----ILKKlgITLEALRE-ALEELRGGSRVTSQNPESKtpALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 168 RFTHNFTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVELLCLDL 247
Cdd:COG0542 164 KYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 248 GLLQAGASVKGEFERRLQGVIDEVKASPKPIILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTIAATTWSEYKKY 327
Cdd:COG0542 244 GALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEYRKY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 328 FEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVR 407
Cdd:COG0542 324 IEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAARVR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 408 ISLAAAPEALERLRGEIAEGERQGEAMRRDLDAGlniDHEALDALETRLVAARAELEQVETRWSIQRDLAERLLEQRklc 487
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEALKKEQDEA---SFERLAELRDELAELEEELEALKARWEAEKELIEEIQELK--- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 488 aaARLAGDEEETDAPRASLEELEAELRALqaelaaaqasERLVSFEVCPRLVAEVISHWTGVPLSQLAREHNTKVITFAD 567
Cdd:COG0542 478 --EELEQRYGKIPELEKELAELEEELAEL----------APLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 568 DLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVS 647
Cdd:COG0542 546 ELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVS 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 648 RLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMTSNLASER 727
Cdd:COG0542 626 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSEL 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 728 IASLCagGERPAAEDLELAIRPQLTQHFKPALLGRM-RVVPYYPMDGDLLRQLVGLKLARFGERLARRQLAFSHCDGLVE 806
Cdd:COG0542 706 ILDLA--EDEPDYEEMKEAVMEELKKHFRPEFLNRIdEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKD 783
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1222379302 807 HLAERCTHGDSGARLIDHLIDQHLQPLVVDRLLDAMAAGEqlQRVHATLDAD 858
Cdd:COG0542 784 FLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEG--DTITVDVDDG 833
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
50-858 |
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: 651.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 50 ESLLARALQDAEIDAGELAQAL------QPRGEHSESrNPVFSAELVQWLQDALLVANlELGASQIDQAALILALLRNP- 122
Cdd:TIGR03346 38 GGLARPLLQKAGVNVGALRQALekelerLPKVSGPGG-QVYLSPDLNRLLNLAEKLAQ-KRGDEFISSEHLLLALLDDKg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 123 -----MRYAGSRYQTLLSKLNAERLRDFALSQQPQAAGGKaaapgesnLARFTHNFTQQARDGKLDPVLCRDGAIRQMVD 197
Cdd:TIGR03346 116 tlgklLKEAGATADALEAAINAVRGGQKVTDANAEDQYEA--------LEKYARDLTERAREGKLDPVIGRDEEIRRTIQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 198 ILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVELLCLDLGLLQAGASVKGEFERRLQGVIDEVKASPKP 277
Cdd:TIGR03346 188 VLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 278 IILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTIAATTWSEYKKYFEKDPALARRFQPVQLHEPTVDEAVTILRG 357
Cdd:TIGR03346 268 IILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 358 LAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPEALERLRGEIAEGERQGEAMRRD 437
Cdd:TIGR03346 348 LKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 438 LDAGlniDHEALDALETRLVAARAELEQVETRWSIQRDLAERLLEQRKLCAAARLAGD--EEETDAPRAS------LEEL 509
Cdd:TIGR03346 428 KDEA---SKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLELEqaEREGDLAKAAelqygkLPEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 510 EAELraLQAELAAAQASERLVSFEVCPRLVAEVISHWTGVPLSQLAREHNTKVITFADDLRQRVRGQEQAIQALDRAMRA 589
Cdd:TIGR03346 505 EKQL--QAAEQKLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRR 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 590 TAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAV 669
Cdd:TIGR03346 583 SRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAV 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 670 RQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMTSNLASERIASLCAGGERpaaEDLELAIRP 749
Cdd:TIGR03346 663 RRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAGGDDY---EEMREAVME 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 750 QLTQHFKPALLGRM-RVVPYYPMDGDLLRQLVGLKLARFGERLARRQLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQ 828
Cdd:TIGR03346 740 VLRAHFRPEFLNRIdEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQR 819
|
810 820 830
....*....|....*....|....*....|
gi 1222379302 829 HLQplvvDRLLDAMAAGEQLQRVHATLDAD 858
Cdd:TIGR03346 820 EIE----NPLAKKILAGEVAPGDTIRVDVE 845
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
104-840 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 556.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 104 LGASQIDQAALILALLRnpmrYAGSRYQTLLSKLNAE--RLRDFALSQQPQAAGGKAAAPGES----NLARFTHNFTQQA 177
Cdd:CHL00095 98 LGHNYIGTEHLLLALLE----EGEGVAARVLENLGVDlsKIRSLILNLIGEIIEAILGAEQSRsktpTLEEFGTNLTKEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 178 RDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVELLCLDLGLLQAGASVK 257
Cdd:CHL00095 174 IDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTKYR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 258 GEFERRLQGVIDEVKASpKPIILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTIAATTWSEYKKYFEKDPALARR 337
Cdd:CHL00095 254 GEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALERR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 338 FQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPEAL 417
Cdd:CHL00095 333 FQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLINSRLPPAA 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 418 ERLrgeiaegerqgeamrrdldaglniDHEALDALETRLVAARAEleqvetRWSIQRDLAERLLEQRKLCAAARLAGDEE 497
Cdd:CHL00095 413 REL------------------------DKELREILKDKDEAIREQ------DFETAKQLRDREMEVRAQIAAIIQSKKTE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 498 ETDAPrasleeleaelralqaelaaaqasERLVsfeVCPRLVAEVISHWTGVPLSQLAREHNTKVITFADDLRQRVRGQE 577
Cdd:CHL00095 463 EEKRL------------------------EVPV---VTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQD 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 578 QAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVSRLIGAPPGYV 657
Cdd:CHL00095 516 EAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYV 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 658 GYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMTSNLASERI--ASLCAGG 735
Cdd:CHL00095 596 GYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIetNSGGLGF 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 736 ERPAAEDLELA-------IRPQLTQHFKPALLGRM-RVVPYYPMDGDLLRQLVGLKLARFGERLARRQLAFSHCDGLVEH 807
Cdd:CHL00095 676 ELSENQLSEKQykrlsnlVNEELKQFFRPEFLNRLdEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTL 755
|
730 740 750
....*....|....*....|....*....|...
gi 1222379302 808 LAERCTHGDSGARLIDHLIDQHLQPLVVDRLLD 840
Cdd:CHL00095 756 LIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLS 788
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
166-846 |
1.80e-176 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 531.34 E-value: 1.80e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 166 LARFTHNFTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVELLCL 245
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 246 DLGLLQAGASVKGEFERRLQGVIDEVKASPKPIILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTIAATTWSEYK 325
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 326 KYFEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACAR 405
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 406 VRISLAAAPEALERLRGEIAEGERQGEAMRRDLDAGlniDHEALDALETRLVAARAELEQVETRWS--------IQRDLA 477
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEA---SKKRLDMLNEELSDKERQYSELEEEWKaekaslsgTQTIKA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 478 ErlLEQRKLC-AAARLAGD-EEETDAPRASLEELEAELralQAELAAAQASERLVSFEVCPRLVAEVISHWTGVPLSQLA 555
Cdd:PRK10865 478 E--LEQAKIAiEQARRVGDlARMSELQYGKIPELEKQL---AAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRML 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 556 REHNTKVITFADDLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVI 635
Cdd:PRK10865 553 ESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRI 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 636 NMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNT 715
Cdd:PRK10865 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNT 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 716 LILMTSNLASERIASLCAGGERPAAEDLELAIrpqLTQHFKPALLGRM-RVVPYYPMDGDLLRQLVGLKLARFGERLARR 794
Cdd:PRK10865 713 VVIMTSNLGSDLIQERFGELDYAHMKELVLGV---VSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQRLYKRLEER 789
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1222379302 795 QLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQHLQ-PLVVDRLLDAMAAGE 846
Cdd:PRK10865 790 GYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIEnPLAQQILSGELVPGK 842
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
76-839 |
4.42e-175 |
|
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: 523.43 E-value: 4.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 76 EHSESRNPVFSAELVQWLQDALLVANlELGASQIDQAALILALLRNPMRYAGsrY---QTLLSKLNAERLRDFALSQQPQ 152
Cdd:TIGR02639 69 PEDIDEEPEQTVGVQRVIQRALLHVK-SAGKKEIDIGDLLVALFDEEDSHAS--YflkSQGITRLDILNYISHGISKDDG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 153 AAGGKAAAPGE-----SNLARFTHNFTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALR 227
Cdd:TIGR02639 146 KDQLGEEAGKEeekgqDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 228 IATGEVPQVLKGVELLCLDLGLLQAGASVKGEFERRLQGVIDEVKASPKPIiLFIDEAHTLIGAG-GQAGSGDAANLLKP 306
Cdd:TIGR02639 226 IAEGKVPERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAI-LFIDEIHTIVGAGaTSGGSMDASNLLKP 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 307 ALARGELRTIAATTWSEYKKYFEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYL 386
Cdd:TIGR02639 305 ALSSGKIRCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 387 AGRQLPDKAVDVLDTACARVRISLAAAPEALERLRGeiaegerqgeamrrdldaglnidhealdaletrlvaaraeleqv 466
Cdd:TIGR02639 385 NDRFLPDKAIDVIDEAGAAFRLRPKAKKKANVNVKD-------------------------------------------- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 467 etrwsiqrdlaerlleqrklcaaarlagdeeetdaprasleeleaelralqaelaaaqaserlvsfevcprlVAEVISHW 546
Cdd:TIGR02639 421 ------------------------------------------------------------------------IENVVAKM 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 547 TGVPLSQLAREHNTKVITFADDLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLy 626
Cdd:TIGR02639 429 AKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 627 gG---ERFltviNMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVAN 703
Cdd:TIGR02639 508 -GvhlLRF----DMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLT 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 704 DGEGREINFRNTLILMTSNL-ASERIASLCA-GGERpaaedLELAIRPQLTQHFKPALLGRM-RVVPYYPMDGDLLRQLV 780
Cdd:TIGR02639 583 DNNGRKADFRNVILIMTSNAgASEMSKPPIGfGGEN-----RESKSLKAIKKLFSPEFRNRLdAIIHFNDLSEEMAEKIV 657
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222379302 781 GLKLARFGERLARRQLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQHLQPLVVDRLL 839
Cdd:TIGR02639 658 KKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
163-839 |
2.27e-118 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 376.87 E-value: 2.27e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 163 ESNLARFTHNFTQQARDGKLDPVLCRDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVEL 242
Cdd:PRK11034 166 EERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTI 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 243 LCLDLGLLQAGASVKGEFERRLQGVIDEVKASpKPIILFIDEAHTLIGAGGQAGSG-DAANLLKPALARGELRTIAATTW 321
Cdd:PRK11034 246 YSLDIGSLLAGTKYRGDFEKRFKALLKQLEQD-TNSILFIDEIHTIIGAGAASGGQvDAANLIKPLLSSGKIRVIGSTTY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 322 SEYKKYFEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDT 401
Cdd:PRK11034 325 QEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 402 ACARVRISLAAapealerlrgeiaegerqgeamRRDLDAGLnidhealdaletrlvaarAELEQVetrwsiqrdlaerll 481
Cdd:PRK11034 405 AGARARLMPVS----------------------KRKKTVNV------------------ADIESV--------------- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 482 eqrklcaAARLAGDEEETdaprasleeleaelralqaelaaAQASERLVsfevcprlvaevishwtgvplsqlarehntk 561
Cdd:PRK11034 430 -------VARIARIPEKS-----------------------VSQSDRDT------------------------------- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 562 VITFADDLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLyGGErfLTVINMSEFQ 641
Cdd:PRK11034 449 LKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE--LLRFDMSEYM 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 642 EKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMTS 721
Cdd:PRK11034 526 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTT 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 722 NLASERIASLCAG-GERPAAEDLELAIRPQLTQHFKPALLGrmrVVPYYPMDGDLLRQLVGLKLARFGERLARRQLAFSH 800
Cdd:PRK11034 606 NAGVRETERKSIGlIHQDNSTDAMEEIKKIFTPEFRNRLDN---IIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEV 682
|
650 660 670
....*....|....*....|....*....|....*....
gi 1222379302 801 CDGLVEHLAERCTHGDSGARLIDHLIDQHLQPLVVDRLL 839
Cdd:PRK11034 683 SQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 721
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
561-769 |
5.57e-83 |
|
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: 263.65 E-value: 5.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 561 KVITFADDLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPVGVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEF 640
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 641 QEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMT 720
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1222379302 721 SNlaseriaslcaggerpaaedlelairpqltqHFKPALLGRMRVVPYY 769
Cdd:cd19499 161 SN-------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
600-766 |
2.19e-78 |
|
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: 250.96 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 600 PVGVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVSRLIGAPPGYVGYGEGGMLTEAVRQKPYSVILL 679
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 680 DEVEKADPDVMNVFYQIFDKGVANDGEGREINFRNTLILMTSNLASERIASLCAGGERPAAEDLELAIRPQLTQHFKPAL 759
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEF 161
|
....*..
gi 1222379302 760 LGRMRVV 766
Cdd:pfam07724 162 LGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
347-439 |
1.05e-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: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 347 TVDEAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLPDKAVDVLDTACARVRISLAAAPEALERLRGEIAE 426
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90
....*....|...
gi 1222379302 427 GERQGEAMRRDLD 439
Cdd:pfam17871 81 LEIEKEALEREQD 93
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
575-728 |
1.02e-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: 72.18 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 575 GQEQAIQALDRAMRataaglNRPDAPVgvfLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVSRLIgapp 654
Cdd:cd00009 2 GQEEAIEALREALE------LPPPKNL---LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF---- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222379302 655 gyvGYGEGGMLTEAVRQKPYSVILLDEVEKADPDVMNVFYQIFdkgvaNDGEGREINFRNTLILMTSNLASERI 728
Cdd:cd00009 69 ---GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVL-----ETLNDLRIDRENVRVIGATNRPLLGD 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-731 |
2.38e-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: 62.39 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 602 GVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEKHTVSRLIGAPPGYVGYGEGGM----LTEAVRQKPYSVI 677
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1222379302 678 LLDEVEKADPDVMNVFYQIFDKGVANDGEGREinfRNTLILMTSNLASERIASL 731
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKDLGPAL 133
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
188-339 |
4.30e-11 |
|
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: 61.78 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 188 RDGAIRQMVDILARRRKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQV-LKGVELLcldlgllqAGASVKGEFERRLQG 266
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLyLNASDLL--------EGLVVAELFGHFLVR 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222379302 267 VIDEVKASPKPIILFIDEAHTLIGAGGQAGSGDAANLLKPALARGELRTIAATTwseYKKYFEKDPALARRFQ 339
Cdd:cd00009 75 LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVIGATN---RPLLGDLDRALYDRLD 144
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
604-731 |
2.59e-09 |
|
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: 56.15 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 604 FLLVGPSGVGKTETALALADLLYGGERFltVINMSEFQekhTVSRLIGA--PPGYVGYGEGGMLTEAVRQKpySVILLDE 681
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRPVF--YVQLTRDT---TEEDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1222379302 682 VEKADPDVMNVFYQIFDKGVANDGEGREI---NFRNTLILMTSNLASERIASL 731
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELvkaAPDGFRLIATMNPLDRGLNEL 127
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
776-856 |
2.05e-08 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 52.45 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 776 LRQLVGLKLARFGERLARRQLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQHLQPLVVDRLLDAMAAGEQLQRVHATL 855
Cdd:smart01086 6 LVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVVVDVDD 85
|
.
gi 1222379302 856 D 856
Cdd:smart01086 86 G 86
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
208-339 |
6.75e-08 |
|
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: 51.83 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 208 IVVGEAGVGKTAIVEGLA-------LRIATGEVpqVLKGVellcldlgllqagasvkGEFERRLQGVIDEVKaSPKPIIL 280
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAkelgapfIEISGSEL--VSKYV-----------------GESEKRLRELFEAAK-KLAPCVI 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222379302 281 FIDEAHTLIGAGGQAGSG---DAANLLKPALARGELRT-----IAATTwseykkYFEK-DPALARRFQ 339
Cdd:pfam00004 62 FIDEIDALAGSRGSGGDSesrRVVNQLLTELDGFTSSNskvivIAATN------RPDKlDPALLGRFD 123
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
605-722 |
3.04e-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: 50.28 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 605 LLVGPSGVGKTETALALADLLygGERFLTvINMSEFQEKhtvsrligappgYVGYGEG---GMLTEAVRQKPySVILLDE 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL--GAPFIE-ISGSELVSK------------YVGESEKrlrELFEAAKKLAP-CVIFIDE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1222379302 682 VEK-----------ADPDVMNVFYQIFDkgvandgeGREINFRNTLILMTSN 722
Cdd:pfam00004 66 IDAlagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
776-840 |
1.03e-06 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.
Pssm-ID: 463090 [Multi-domain] Cd Length: 81 Bit Score: 47.02 E-value: 1.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222379302 776 LRQLVGLKLARFGERLARRQLAFSHCDGLVEHLAERCTHGDSGARLIDHLIDQHLQPLVVDRLLD 840
Cdd:pfam10431 6 LRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILS 70
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
577-685 |
1.31e-06 |
|
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: 49.20 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 577 EQAIQALDRAMRATAAGLNrpdAPVGVfLLVGPSGVGKTETALALADLLyGGErfLTVINMSEFQEKhtvsrligappgY 656
Cdd:cd19481 6 REAVEAPRRGSRLRRYGLG---LPKGI-LLYGPPGTGKTLLAKALAGEL-GLP--LIVVKLSSLLSK------------Y 66
|
90 100 110
....*....|....*....|....*....|.
gi 1222379302 657 VGYGEGGM--LTEAVRQKPYSVILLDEVEKA 685
Cdd:cd19481 67 VGESEKNLrkIFERARRLAPCILFIDEIDAI 97
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
203-338 |
1.54e-06 |
|
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: 48.52 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 203 RKNNPIVVGEAGVGKTAIVEGLALRIATGEVPQVLKGVELLCLDLGLLQAGASVK-----GEFERRLQGVIDEVKAsPKP 277
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGgkkasGSGELRLRLALALARK-LKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222379302 278 IILFIDEAHTLIGAGGQAG--SGDAANLLKPALARGELRTIAATTWSEykkyFEKDPALARRF 338
Cdd:smart00382 80 DVLILDEITSLLDAEQEALllLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
408-684 |
3.44e-05 |
|
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: 47.21 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 408 ISLAAAPEALERLRGEIAEGERQGEAMRRDLDAGLNIDHEALDALETRLVAARAELEQVETRWSIQRDLAERLLEQRKLC 487
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 488 AAARLAGDEEETDAPRASLEELEAELRALQAELAAAQASERLVSFEVCPRLVAEVISHWTGVPLSQLAREHntKVITFAD 567
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLEL--REAILDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 568 -----DLRQRVRgqEQAIQALDRAMRATAAGLNRPdapvGVFLLVGPSGVGKTETALALADLLygGERFLTVinmsefqe 642
Cdd:COG0464 159 lggleEVKEELR--ELVALPLKRPELREEYGLPPP----RGLLLYGPPGTGKTLLARALAGEL--GLPLIEV-------- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1222379302 643 khTVSRLIGappGYVGYGEGG---MLTEAvRQKPYSVILLDEVEK 684
Cdd:COG0464 223 --DLSDLVS---KYVGETEKNlreVFDKA-RGLAPCVLFIDEADA 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-514 |
3.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 350 EAVTILRGLAPVYEKSHGIYLRDDAVVAAAELSARYLAGRQLpdkavDVLDTACARVRISLAAAPEALERLRGEIAEGER 429
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL-----ELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 430 QGEAMRRDLDaglNIDHEALDALETRLVAARAELEQVETRWSIQRDLAERL----------LEQRKLCAAARLAGDEEET 499
Cdd:COG4913 324 ELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeeFAALRAEAAALLEALEEEL 400
|
170
....*....|....*
gi 1222379302 500 DAPRASLEELEAELR 514
Cdd:COG4913 401 EALEEALAEAEAALR 415
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
603-732 |
3.78e-04 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 42.00 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 603 VFLLVGPSGVGKTETALALADLL--YGGErfLTVINMSEFQEKHTVSRLIGAPPGYVG-YGE----------GGM----- 664
Cdd:cd03230 28 IYGLLGPNGAGKTTLIKIILGLLkpDSGE--IKVLGKDIKKEPEEVKRRIGYLPEEPSlYENltvrenlklsGGMkqrla 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222379302 665 LTEAVRQKPySVILLDEVEKA-DPDVMNVFYQIFdkgvandgegREINFRNTLILMTSNLASErIASLC 732
Cdd:cd03230 106 LAQALLHDP-ELLILDEPTSGlDPESRREFWELL----------RELKKEGKTILLSSHILEE-AERLC 162
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
450-622 |
7.58e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 42.55 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 450 DA--LETRLVAARAELEQVETRWSIQRDLAERLLEQRKLCAAARLAGDEEETDAPRASLEELEAELRALQAELAAAQASE 527
Cdd:COG1419 25 DAviLSTRKVKKGGFLKKVEVTAAVDEDEAEKAPAAAAAPAAASAAAEEEELEELRRELAELKELLEEQLSGLAGESARL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 528 RLVSFEVCPRLVAEvishwtGVPlSQLAREhntkvitfaddLRQRVRGQEQAIQALDRAMRATAAGLNRPDAPV----GV 603
Cdd:COG1419 105 PPELAELLERLLEA------GVS-PELARE-----------LLEKLPEDLSAEEAWRALLEALARRLPVAEDPLldegGV 166
|
170 180
....*....|....*....|
gi 1222379302 604 FLLVGPSGVGKTeTALA-LA 622
Cdd:COG1419 167 IALVGPTGVGKT-TTIAkLA 185
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
258-387 |
1.03e-03 |
|
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: 42.59 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 258 GEFERRLQGVIDEVKASpKPIILFIDEAHTLIGAGGQAGSGDA----ANLLKpALA--RGELRTIAATTwseykkYFEK- 330
Cdd:COG0464 233 GETEKNLREVFDKARGL-APCVLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAATN------RPDLl 304
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222379302 331 DPALARRFQ-PVQLHEPTVDEAVTILRGLAPVYEKSHGIYLrDDAVVAAAELSARYLA 387
Cdd:COG0464 305 DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDL-EELAEATEGLSGADIR 361
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
328-514 |
1.65e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 328 FEKDPALARRFQPVQLHEPTVDEAVTILRGLAPVYEKS----HGIYLRDDAVVAAAELSARYLAGRQLPDKAV-----DV 398
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryyvLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlegEG 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 399 LDTACARVRISLAAAPEALERLRGEIAEGERQGEAMRRDLDAGLNIDHEALDALETRLVAARAELEQVETRwSIQRDLAE 478
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL-EEQLEAER 734
|
170 180 190
....*....|....*....|....*....|....*.
gi 1222379302 479 RLLEQRKLCAAARLAGDEEETDAPRASLEELEAELR 514
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
602-698 |
1.71e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 602 GVFLLVGPSGVGKTETALALADLLYGGERFLTVINMSEFQEK----HTVSRLIGAPPgyVGYGEGGMLTEAVRQ-----K 672
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPL--SGRLSKEELLAALQQlllalA 83
|
90 100
....*....|....*....|....*.
gi 1222379302 673 PYSVILLDEVEKADPDVMNVFYQIFD 698
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
573-686 |
1.93e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 41.83 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 573 VRGQEQAIQALDRAMRATAAGlnRPDAPVgvfLLVGPSGVGKTETALALAdllygGERFLTVI--NMSEFQEKHTVSRLI 650
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALA-----NDYGWEVIelNASDQRTADVIERVA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1222379302 651 GAppgyvgygegGMLTEAVRQKPYSVILLDEV----EKAD 686
Cdd:PRK04195 86 GE----------AATSGSLFGARRKLILLDEVdgihGNED 115
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
564-640 |
4.15e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 40.36 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 564 TFADDLRQRVRGQEQAIQALDRAMrataaglnrpDAPVGVFLLV-GPSGVGKTETALALADLLYG--GERFLTVINMSEF 640
Cdd:PRK12402 8 KYRPALLEDILGQDEVVERLSRAV----------DSPNLPHLLVqGPPGSGKTAAVRALARELYGdpWENNFTEFNVADF 77
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
564-622 |
5.59e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 39.79 E-value: 5.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 564 TFADdlrqrVRGQEQAIQALDRAMRAtaaglNR-PDApvgvFLLVGPSGVGKTETALALA 622
Cdd:COG2812 8 TFDD-----VVGQEHVVRTLKNALAS-----GRlAHA----YLFTGPRGVGKTTLARILA 53
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
575-802 |
5.70e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 39.48 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 575 GQEQAIQALDRAMRATAAGLNR----PDAPVGVfLLVGPSGVGKTETALALADLLygGERFLTViNMSEfqekhtvsrLI 650
Cdd:COG1223 6 GQEEAKKKLKLIIKELRRRENLrkfgLWPPRKI-LFYGPPGTGKTMLAEALAGEL--KLPLLTV-RLDS---------LI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 651 GAppgYVGYGEG--GMLTEAVRQKPySVILLDEvekadpdvmnvFYQIF-DKGVAND-GEGREInfRNTLILMTSNLASE 726
Cdd:COG1223 73 GS---YLGETARnlRKLFDFARRAP-CVIFFDE-----------FDAIAkDRGDQNDvGEVKRV--VNALLQELDGLPSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 727 RIasLCAGGERPAAEDlelairpqltqhfkPALLGRMRVVPYYPM-DGDLLRQLVGLKLARFG-------ERLARRQLAF 798
Cdd:COG1223 136 SV--VIAATNHPELLD--------------SALWRRFDEVIEFPLpDKEERKEILELNLKKFPlpfeldlKKLAKKLEGL 199
|
....
gi 1222379302 799 SHCD 802
Cdd:COG1223 200 SGAD 203
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
406-514 |
7.63e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222379302 406 VRISLAAAPEALERLRGEIAEGERQGEAMR---RDLDAGLNIDHEALDALETRLVAARAELEQVETRWS---IQRDLAER 479
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapVDLGNAED 412
|
90 100 110
....*....|....*....|....*....|....*
gi 1222379302 480 LLEQRklcaaarlagdEEETDAPRASLEELEAELR 514
Cdd:PRK02224 413 FLEEL-----------REERDELREREAELEATLR 436
|
|
| |
