|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-857 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1698.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALSRLPQVEGTEGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 81 VQPSADLVRVLNLCDKLAQKRGDNFISSELFVLAALDSRGSLADLLKSAGATSDKLTKAIDQMRGGDSVNDQGAEDQRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 161 LKKYTIDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLSL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 241 DMGALIAGAKYRGEFEERLKAVLSDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 401 IRMQIDSKPESLDRLERRIIQLKLEQQALKKESDDASIKRLDMLEAELSQKEREYSELEEEWKAEKASLSGTQHIKTELE 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 481 NAKLAMEQARRQGDLAQMSELQYGKIPELEKQLESATQSEGKTMRLLRNRVTDVEIADVLARWTGIPVDRMMEGERDKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 561 RMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 721 GSDLIQERFGALSYDAMKEMVMAVVSQSFRPEFINRIDELVVFHPLGEQHIASIARIQLTRLYQRLEERGYELHISEAAL 800
Cdd:PRK10865 721 GSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 891174144 801 QKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDVENDIIVAHQ 857
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAVQ 857
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-854 |
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: 1589.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALSRLPQVEGTEGDVQPSA 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 86 DLVRVLNLCDKLAQKRGDNFISSELFVLAALDSRGSLADLLKSAGATSDKLTKAIDQMRGGDSVNDQGAEDQRQALKKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 166 IDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLSLDMGAL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 246 IAGAKYRGEFEERLKAVLSDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 326 DAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 406 DSKPESLDRLERRIIQLKLEQQALKKESDDASIKRLDMLEAELSQKEREYSELEEEWKAEKASLSGTQHIKTELENAKLA 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 486 MEQARRQGDLAQMSELQYGKIPELEKQLESATQSEGKTM-RLLRNRVTDVEIADVLARWTGIPVDRMMEGERDKLLRMEQ 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQnRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 565 QLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVS 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 645 RLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDL 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 725 IQERFGALSYDAMKEMVMAVVSQSFRPEFINRIDELVVFHPLGEQHIASIARIQLTRLYQRLEERGYELHISEAALQKLA 804
Cdd:TIGR03346 721 IQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 891174144 805 ENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDVENDIIV 854
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-854 |
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: 1488.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALSRLPQVEGTEGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 81 VQPSADLVRVLNLCDKLAQKRGDNFISSELFVLAAL-DSRGSLADLLKSAGATSDKLTKAIDQMRGGDSVNDQGAEDQRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLrEGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 160 ALKKYTIDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLS 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 240 LDMGALIAGAKYRGEFEERLKAVLSDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 320 RQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 400 SIRMQIDSKPESLDRLERRIIQLKLEQQALKKESDDASIKRLDMLEAELSQKEREYSELEEEWKAEKASLSGTQHIKTEL 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 480 ENaklameqarrqgdlaqmselQYGKIPELEKQLESATQSEGKTMRLLRNRVTDVEIADVLARWTGIPVDRMMEGERDKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 560 LRMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 640 KHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 720 LGSDLIQERFG-ALSYDAMKEMVMAVVSQSFRPEFINRIDELVVFHPLGEQHIASIARIQLTRLYQRLEERGYELHISEA 798
Cdd:COG0542 701 IGSELILDLAEdEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 891174144 799 ALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDVENDIIV 854
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
17-851 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 863.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 17 AQSLA--LGHDnqFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALSRLPQVEGTEGDVQPSADlvRVLNLC 94
Cdd:CHL00095 16 SQEEArrLGHN--FVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPFTPRAK--RVLEMS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 95 DKLAQKRGDNFISSELFVLAAL-DSRGSLADLLKSAGATSDKLTKAIDQMRGGDSVNDQGAEDQRQ---ALKKYTIDLTE 170
Cdd:CHL00095 92 LEEARDLGHNYIGTEHLLLALLeEGEGVAARVLENLGVDLSKIRSLILNLIGEIIEAILGAEQSRSktpTLEEFGTNLTK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 171 RAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLSLDMGALIAGAK 250
Cdd:CHL00095 172 EAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 251 YRGEFEERLKAVLSDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALE 330
Cdd:CHL00095 252 YRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 331 RRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRM---QIDS 407
Cdd:CHL00095 331 RRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLinsRLPP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 408 KPESLDRLERRIIQLKleqqalkkesdDASIKRLDMLEAElsqkereyseleeewkaekaslsgtQHIKTELENAklame 487
Cdd:CHL00095 411 AARELDKELREILKDK-----------DEAIREQDFETAK-------------------------QLRDREMEVR----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 488 qarrqgdlAQMSELQYGKIPELEKQLEsatqsegktmrllRNRVTDVEIADVLARWTGIPVDRMMEGERDKLLRMEQQLH 567
Cdd:CHL00095 450 --------AQIAAIIQSKKTEEEKRLE-------------VPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLH 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 568 TRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLV 647
Cdd:CHL00095 509 KRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLI 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 648 GAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQE 727
Cdd:CHL00095 589 GSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIET 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 728 RFGAL------------SYDAMKEMVMAVVSQSFRPEFINRIDELVVFHPLGEQHIASIARIQLTRLYQRLEERGYELHI 795
Cdd:CHL00095 669 NSGGLgfelsenqlsekQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEV 748
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 891174144 796 SEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDVEND 851
Cdd:CHL00095 749 TERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDE 804
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-835 |
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: 776.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALSRLPQVEGTEGDVQPSa 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 86 dLVRVLNLCDKLAQKR-GDNFISSELFVLAALDSRGSLADLLKSAGATS----DKLTKAIDQMRGGDSVNDQGAED---- 156
Cdd:TIGR03345 80 -LVELLQEAWLLASLElGDGRIRSGHLLLALLTDPELRRLLGSISPELAkidrEALREALPALVEGSAEASAAAADaapa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 157 -------QRQALKKYTIDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVP 229
Cdd:TIGR03345 159 gaaagaaGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 230 EGLKGRRVLSLDMGALIAGAKYRGEFEERLKAVLSDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELH 309
Cdd:TIGR03345 239 PALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 310 CVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDK 389
Cdd:TIGR03345 319 TIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 390 AIDLIDEAASSIRMQIDSKPESLDRLERRIIQLKLEQQALKKES----DDASikRLDMLEAELSQKEREYSELEEEWKAE 465
Cdd:TIGR03345 399 AVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalgaDHDE--RLAELRAELAALEAELAALEARWQQE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 466 KASLSGTQHIKTELENAklamEQARRQGDLAQMSELQygkipELEKQLESATQSEgktmRLLRNRVTDVEIADVLARWTG 545
Cdd:TIGR03345 477 KELVEAILALRAELEAD----ADAPADDDDALRAQLA-----ELEAALASAQGEE----PLVFPEVDAQAVAEVVADWTG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 546 IPVDRMMEGERDKLLRMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDS 625
Cdd:TIGR03345 544 IPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGG 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 626 DDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGR 705
Cdd:TIGR03345 624 EQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGR 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 706 TVDFRNTVVIMTSNLGSDLIQERFG----ALSYDAMKEMVMAVVSQSFRPEFINRIdELVVFHPLGEQHIASIARIQLTR 781
Cdd:TIGR03345 704 EIDFKNTVILLTSNAGSDLIMALCAdpetAPDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDR 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 891174144 782 LYQRLEER-GYELHISEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILS 835
Cdd:TIGR03345 783 IARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-848 |
0e+00 |
|
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: 758.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLTQEGGsvRPLLTSASVDVSSLRNAIEQALS-RLPQ-VEGTEGDVQP 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEA--IEILEECGGDVELLRKRLEDYLEeNLPViPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 84 SADLVRVLNLCDKLAQKRGDNFISSELFVLAALDSRGSLAD-LLKSAGATSDKLTKAI-DQMRGGDSVNDQGA------E 155
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASyFLKSQGITRLDILNYIsHGISKDDGKDQLGEeagkeeE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 156 DQRQALKKYTIDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGR 235
Cdd:TIGR02639 159 KGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 236 RVLSLDMGALIAGAKYRGEFEERLKAVLSDLAKQEgNVILFIDELHTMVGAGK-ADGAMDAGNMLKPALARGELHCVGAT 314
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEP-NAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 315 TLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLI 394
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 395 DEAASSIRMQIDSKPesldrlerriiqlkleqqalkkesddasikrldmleaelsqkereyseleeewkaekaslsgtqh 474
Cdd:TIGR02639 398 DEAGAAFRLRPKAKK----------------------------------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 475 ikteleNAKlameqarrqgdlaqmselqygkipelekqlesatqsegktmrllrnrVTDVEIADVLARWTGIPVDRMMEG 554
Cdd:TIGR02639 413 ------KAN-----------------------------------------------VNVKDIENVVAKMAKIPVKTVSSD 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 555 ERDKLLRMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRIDM 634
Cdd:TIGR02639 440 DREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDM 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 635 SEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVV 714
Cdd:TIGR02639 517 SEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVIL 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 715 IMTSNLGSD--------LIQERFGALSYDAMKEMvmavvsqsFRPEFINRIDELVVFHPLGEQHIASIARIQLTRLYQRL 786
Cdd:TIGR02639 597 IMTSNAGASemskppigFGGENRESKSLKAIKKL--------FSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQL 668
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 891174144 787 EERGYELHISEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDV 848
Cdd:TIGR02639 669 NEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
6-851 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 580.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLtqEGGSVRPLLTSASVDVSSLRNA----IEQALSRLPQVEGTEgDV 81
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQEleafIEQTTPVLPASEEER-DT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 82 QPSADLVRVLNLCDKLAQKRGDNFISSELFVLAALDSRGSLAD-LLK-------------SAGATSDKLTKAIDQMRGGD 147
Cdd:PRK11034 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAyLLRkhevsrldvvnfiSHGTRKDEPSQSSDPGSQPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 148 SVNDQGAEDQrqaLKKYTIDLTERAELGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
Cdd:PRK11034 159 SEEQAGGEER---MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 228 VPEGLKGRRVLSLDMGALIAGAKYRGEFEERLKAVLSDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARG 306
Cdd:PRK11034 236 VPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 307 ELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQL 386
Cdd:PRK11034 315 KIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 387 PDKAIDLIDEAASSIRMqidskpesldrlerriiqlkleqqalkkesddasikrldmleaelsqkereyseleeewkaek 466
Cdd:PRK11034 395 PDKAIDVIDEAGARARL--------------------------------------------------------------- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 467 aslsgtqhiktelenaklaMEQARRQgdlaqmselqygkipelekqlesatqsegKTMrllrnRVTDVEiaDVLARWTGI 546
Cdd:PRK11034 412 -------------------MPVSKRK-----------------------------KTV-----NVADIE--SVVARIARI 436
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 547 PVDRMMEGERDKLLRMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMfdsD 626
Cdd:PRK11034 437 PEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---G 513
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 627 DAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRT 706
Cdd:PRK11034 514 IELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRK 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 707 VDFRNTVVIMTSNLGSDLIQERFGAL-----SYDAMKEmvmavVSQSFRPEFINRIDELVVFHPLGEQHIASIARIQLTR 781
Cdd:PRK11034 594 ADFRNVVLVMTTNAGVRETERKSIGLihqdnSTDAMEE-----IKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVE 668
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 782 LYQRLEERGYELHISEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQMDVEND 851
Cdd:PRK11034 669 LQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKE 738
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-763 |
1.60e-110 |
|
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: 335.69 E-value: 1.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 558 KLLRMEQQLHTRVIGQNEAVEAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 891174144 718 SNLgsdliqerfgalsydamkemvmavvsqsFRPEFINRIDELVVF 763
Cdd:cd19499 161 SNH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
596-759 |
3.67e-95 |
|
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: 295.26 E-value: 3.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 596 RPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVIL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 676 LDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQERFG---ALSYDAMKEMVMAVVSQSFRPE 752
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdSPDYELLKEEVMDLLKKGFIPE 160
|
....*..
gi 891174144 753 FINRIDE 759
Cdd:pfam07724 161 FLGRLPI 167
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
342-445 |
3.43e-46 |
|
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: 160.35 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 342 SVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPESLDRLERRIIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 891174144 422 LKLEQQALKKESDDASIKRLDMLE 445
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
766-844 |
7.66e-32 |
|
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: 118.66 E-value: 7.66e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 891174144 766 LGEQHIASIARIQLTRLYQRLEERGYELHISEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTI 844
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTV 79
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
766-854 |
6.35e-29 |
|
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: 110.61 E-value: 6.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 766 LGEQHIASIARIQLTRLYQRLEERGYELHISEAALQKLAENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKTIQ 845
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 891174144 846 MDVENDIIV 854
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
1.81e-22 |
|
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: 94.52 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 181 IGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINgevpeglKGRRVLSLDMGALIAGAKYRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 261 AVLSDLAKQEGNVILFIDELHTMVGAGKADG--AMDAGNMLKPalARGELHCVGATTLDEYRQyieKDAALERRFQKVFV 338
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNALlrVLETLNDLRI--DRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
...
gi 891174144 339 AEP 341
Cdd:cd00009 149 IPL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-725 |
2.96e-20 |
|
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: 87.97 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 571 IGQNEAVEAVSNAIRRsragladpnRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891174144 651 PGYVgyeeggyLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTdgqgrTVDFRNTVVIMTSNLGSDLI 725
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-725 |
3.33e-14 |
|
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: 70.87 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 602 LFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGY----LTEAVRRRPYSVILLD 677
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 891174144 678 EVEKAHPDVFNILLQVLDDGRLTDGQGRtvdFRNTVVIMTSNLGSDLI 725
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLG 130
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-337 |
5.69e-14 |
|
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: 69.54 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLSLDMGALIagAKYRGEFEERLKAVLsDLAKQEGNVILFIDELHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELF-EAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 891174144 284 VGAGKADG---AMDAGNMLKPAL-----ARGELHCVGATTldeyrqYIEK-DAALERRFQKVF 337
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
600-719 |
1.70e-11 |
|
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: 62.31 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 600 SFLFLGPTGVGKTELCKALANFMFDSDDAMVRidMSEFMEKhsvSRLVGA--PPGYVGYEEGGYLTEAVRRRpySVILLD 677
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 891174144 678 EVEKAHPDVFNILLQVLDDGRLTDGQGRT---VDFRNTVVIMTSN 719
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
63-382 |
2.51e-11 |
|
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: 66.47 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 63 AIEQALSRLPQVEGTEGDVQPSADLVRVLNLCDKLAQKRGDNFISSELFVLAALDSRGSLADLLKSAGATSDKLTKAIDQ 142
Cdd:COG0464 42 LLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 143 MRGGDSVNDQGAEDQRQALKKYTIDLTERAELGKLDPVIGRDE---EIRRTIQVLQRRTK-------NNP---VLIGEPG 209
Cdd:COG0464 122 LRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELRELVALPLKRPElreeyglPPPrglLLYGPPG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 210 VGKTAIVEGLAQRIingevpeglkGRRVLSLDMGALIagAKYRGEFEERLKAVLsDLAKQEGNVILFIDELHTMVGA--G 287
Cdd:COG0464 202 TGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKNLREVF-DKARGLAPCVLFIDEADALAGKrgE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 288 KADGAMDA--GNMLKpALA--RGELHCVGATtldeYRqyIEK-DAALERRFQ-KVFVAEPSVEDTIAILRGLKERYELHH 361
Cdd:COG0464 269 VGDGVGRRvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDE 341
|
330 340
....*....|....*....|...
gi 891174144 362 HVqitDPAIVAAAT--LSHRYIA 382
Cdd:COG0464 342 DV---DLEELAEATegLSGADIR 361
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
575-725 |
5.46e-11 |
|
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: 61.53 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 575 EAVEAVSNAIRRSRAGLadpNRPIGsFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKHSvsrlvgappgYV 654
Cdd:cd19481 7 EAVEAPRRGSRLRRYGL---GLPKG-ILLYGPPGTGKTLLAKALAG---ELGLPLIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 655 GYEEGGYLTEAVRRRPYSVILLDEVEKAHPD------------VFNILLQVLDDGRLTDgqgrtvdfrNTVVIMTSNLGS 722
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNRPD 140
|
...
gi 891174144 723 DLI 725
Cdd:cd19481 141 LLD 143
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
1.71e-10 |
|
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: 56.76 E-value: 1.71e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 891174144 17 AQSLALGHDNQFIEPLHLMSALLTQEGGSVRPLLTSASVDVSSLRNAIEQALS 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-719 |
6.69e-10 |
|
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: 57.60 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 602 LFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKHsvsrlVGAPPGYVgyeeGGYLTEAVRRRPySVILLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK---ELGAPFIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 891174144 682 AHP-----------DVFNILLQVLDdgrltdgqGRTVDFRNTVVIMTSN 719
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
2.31e-09 |
|
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: 53.68 E-value: 2.31e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 891174144 94 CDKLAQKRGDNFISSELFVLAAL-DSRGSLADLLKSAGATSDKLTKAIDQMRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLeEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-341 |
3.88e-07 |
|
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: 50.45 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 198 TKNNPVLIGEPGVGKTAIVEGLAQRI---------INGEVPEglkgRRVLSLDMGALIAGAKYRGEFEERLKAVLsDLAK 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGEDIL----EEVLDQLLLIIVGGKKASGSGELRLRLAL-ALAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891174144 269 QEGNVILFIDELHTMVGAG--KADGAMDAGNMLKPALARGELHCVGATTLDEyrqyIEKDAALERRFQKVFVAEP 341
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLL 146
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
574-781 |
2.62e-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: 50.68 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 574 NEAVEAVS-NAIRRSRAGLadpnRPIGSFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKhsvsrlvgappg 652
Cdd:COG0464 170 RELVALPLkRPELREEYGL----PPPRGLLLYGPPGTGKTLLARALAG---ELGLPLIEVDLSDLVSK------------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 653 YVGyEEGGYLTEAV---RRRPYSVILLDEVEKAHPD-----------VFNILLQVLDDGRltdgqgrtvdfRNTVVIMTS 718
Cdd:COG0464 231 YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAAT 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 891174144 719 NlgsdliqeRFGALsyDamkemvmavvsqsfrPEFINRIDELVVFHPLGEQHIASIARIQLTR 781
Cdd:COG0464 299 N--------RPDLL--D---------------PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
564-681 |
2.68e-06 |
|
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: 48.53 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 564 QQLHTRVIGQNEAVEAVS----NAIRRSR--AGLADPNRPiGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRIDMSEF 637
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAialrNRWRRMQlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 891174144 638 MEKhsvsrlvgappGYVGYEeggyLTEAVRRRPYSVILLDEVEK 681
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-283 |
2.48e-05 |
|
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: 45.35 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLSLDMGALIagAKYRGEFEERLKAVLsDLAKQEGNVILFIDELHTM 283
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIF-ERARRLAPCILFIDEIDAI 97
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
204-296 |
6.53e-05 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This 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: 410915 [Multi-domain] Cd Length: 161 Bit Score: 44.28 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 204 LIGEPGVGKTAIVEGLAqriingevpeGLKGRRVLSLDMGALIAGakYRGEFEERLKAVLsDLAKQEGNVILFIDELHTm 283
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA----------GVWQLPLLRLDMGRLFGG--LVGESESRLRQMI-QTAEAIAPCVLWIDEIEK- 101
|
90
....*....|...
gi 891174144 284 vGAGKADGAMDAG 296
Cdd:cd19507 102 -GFSNADSKGDSG 113
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
6.59e-05 |
|
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: 43.44 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 203 VLIGEPGVGKTAIVEGLAQRIINGEV----------PEGLKGRRVLSLDMGALIAGAKYRgEFEERLKAVLSDLAKQEGN 272
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891174144 273 VilfIDELHTmvgagkadgAMDAGNMLKPALaRGELHC------VGATTLDEYRQYIEKDAALERRF 333
Cdd:pfam07728 82 V---LNSLLS---------LLDERRLLLPDG-GELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
600-698 |
7.43e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.10 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 600 SFLFL-GPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK----HSVSRLVGAPPGYVGYEEG--GYLTEAVRRRP-Y 671
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLALAvA 85
|
90 100
....*....|....*....|....*..
gi 891174144 672 SVILLDEVEKAHPDVFNILLQVLDDGR 698
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
149-375 |
1.10e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.38 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 149 VNDQGAEDQRQALKKYTIDLTERAELgKLDPVIGRDEEIRRTIQVLQRRTKNN---------PV----LIGEPGVGKTAI 215
Cdd:COG1222 50 LNDANLTQKRLGTPRGTAVPAESPDV-TFDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKTLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 216 VEGLAQR----IINgevpegLKGRRVLSldmgaliagaKYRGEFEERLKAVLsDLAKQEGNVILFIDELHTMvgAGKADG 291
Cdd:COG1222 129 AKAVAGElgapFIR------VRGSELVS----------KYIGEGARNVREVF-ELAREKAPSIIFIDEIDAI--AARRTD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 292 AMDAG--NMLKPAL--------ARGELHCVGATtldeyrQYIEK-DAALER--RF-QKVFVAEPSVEDTIAILRGLKERY 357
Cdd:COG1222 190 DGTSGevQRTVNQLlaeldgfeSRGDVLIIAAT------NRPDLlDPALLRpgRFdRVIEVPLPDEEAREEILKIHLRDM 263
|
250
....*....|....*...
gi 891174144 358 ELHHHVqitDPAIVAAAT 375
Cdd:COG1222 264 PLADDV---DLDKLAKLT 278
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
570-729 |
3.08e-04 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 42.39 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 570 VIGQNEAVEAVSNAIRRsragLADPNRPIgsfLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMsefmekhsvsrlvGA 649
Cdd:pfam00158 1 IIGESPAMQEVLEQAKR----VAPTDAPV---LITGESGTGKELFARAIHQLSPRADGPFVAVNC-------------AA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 650 -PPGYV-----GYEEGGYlTEAVRRRP-------YSVILLDEVEKAHPDVFNILLQVLDDG---RLTDGQGRTVDFRntv 713
Cdd:pfam00158 61 iPEELLeselfGHEKGAF-TGADSDRKglfeladGGTLFLDEIGELPLELQAKLLRVLQEGefeRVGGTKPIKVDVR--- 136
|
170
....*....|....*...
gi 891174144 714 VI--MTSNLGSDLIQERF 729
Cdd:pfam00158 137 IIaaTNRDLEEAVAEGRF 154
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
3.74e-04 |
|
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: 42.11 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 179 PVIGRDEEIRRTIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQR----------------IINGEVPEGLKGRRVL- 238
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRAlerdggyflrgkcdenLPYSPLLEALTREGLLr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 891174144 239 -SLDMGALIAGAKYRGEFEERLKAV------------------LSDLAKQEGNVILFIDELH 281
Cdd:pfam13191 81 qLLDELESSLLEAWRAALLEALAPVpelpgdlaerlldlllrlLDLLARGERPLVLVLDDLQ 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
561-781 |
4.51e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 43.23 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 561 RMEQQLHTRVIGQNEAVEAVSNAIrrsragLAdpNRPIgsfLFLGPTGVGKTELCKALANfMFDSDdaMVRI----DMse 636
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIAL------LA--GGHL---LLEGVPGVGKTTLAKALAR-ALGLP--FIRIqftpDL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 637 fMEkhsvSRLVGAppgYVgYEEGgYLTEAVRRRPY--SVILLDEVEKAHPDVFNILLQVLDDGRLTDGqGRTVDFRNT-V 713
Cdd:COG0714 69 -LP----SDILGT---YI-YDQQ-TGEFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVTIP-GGTYKLPEPfL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 714 VIMTSNlgsDLIQE-----------RF------GALSYDAMKEMVMAV-------VSQSFRPEFINRIDELVVFHPLGEQ 769
Cdd:COG0714 138 VIATQN---PIEQEgtyplpeaqldRFllklyiGYPDAEEEREILRRHtgrhlaeVEPVLSPEELLALQELVRQVHVSEA 214
|
250
....*....|...
gi 891174144 770 HIASIARI-QLTR 781
Cdd:COG0714 215 VLDYIVDLvRATR 227
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
548-805 |
5.26e-04 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 43.41 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 548 VDRMMEGERdklLRMEQQLHTRVIGQNEAVEAVSNAIRRsragLADPNRPIgsfLFLGPTGVGKTELCKALANFMFDSDD 627
Cdd:COG2204 114 VERALERRR---LRRENAEDSGLIGRSPAMQEVRRLIEK----VAPSDATV---LITGESGTGKELVARAIHRLSPRADG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 628 AMVRIDMSEFMEKHSVSRLVGAppgyvgyeEGGYLTEAVRRRPYSV-------ILLDEVEKAHPDVFNILLQVLDDG--- 697
Cdd:COG2204 184 PFVAVNCAAIPEELLESELFGH--------EKGAFTGAVARRIGKFeladggtLFLDEIGEMPLALQAKLLRVLQERefe 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 698 RLTDGQGRTVDFRntvVIMTSNLgsDLIQErfgalsydamkemvmaVVSQSFRPEFINRIDELVVFHP-LGEQH--IASI 774
Cdd:COG2204 256 RVGGNKPIPVDVR---VIAATNR--DLEEL----------------VEEGRFREDLYYRLNVFPIELPpLRERRedIPLL 314
|
250 260 270
....*....|....*....|....*....|.
gi 891174144 775 ARIQLTRLYQRLeerGYELHISEAALQKLAE 805
Cdd:COG2204 315 ARHFLARFAAEL---GKPVKLSPEALEALLA 342
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
196-335 |
5.96e-04 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This 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: 410930 [Multi-domain] Cd Length: 170 Bit Score: 41.51 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 196 RRTKNNPVLIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLSLDMGALIagAKYRGEfEERLKAVLSDLAKQEGNVIL 275
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTLT--SKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 276 FIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYI----------EKDAALERRFQK 335
Cdd:cd19522 97 FIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
570-619 |
8.37e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 42.49 E-value: 8.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 891174144 570 VIGQNEAVEAVSNAIRRSRAGLAdpnrpigsFLFLGPTGVGKTELCKALA 619
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRLAHA--------YLFTGPRGVGKTTLARILA 53
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
508-680 |
8.43e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.30 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 508 ELEKQLESATQSEGKTMRLLRNRVTDVEIADVLARWTGIPVDRMMEGERDKLlRMEQqlhtrVIGQNEAVEAVSNAI--- 584
Cdd:COG1222 24 RLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDV-TFDD-----IGGLDEQIEEIREAVelp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 585 -----RRSRAGLadpnRPIGSFLFLGPTGVGKTELCKALANfmfDSDDAMVRIDMSEFMEKhsvsrlvgappgYVGyeEG 659
Cdd:COG1222 98 lknpeLFRKYGI----EPPKGVLLYGPPGTGKTLLAKAVAG---ELGAPFIRVRGSELVSK------------YIG--EG 156
|
170 180
....*....|....*....|....*.
gi 891174144 660 GYL-----TEAVRRRPySVILLDEVE 680
Cdd:COG1222 157 ARNvrevfELAREKAP-SIIFIDEID 181
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
177-383 |
8.84e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.79 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 177 LDPVIGrDEEIRRTIQVL---QRRTKN----------NPVLIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLSLDMG 243
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIikeLRRRENlrkfglwpprKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 244 ALIAgaKYRGEFEERLKAVLsDLAKQEGnVILFIDELHTMvgagkadgamdagnmlkpALARGELHCVGA---------T 314
Cdd:COG1223 70 SLIG--SYLGETARNLRKLF-DFARRAP-CVIFFDEFDAI------------------AKDRGDQNDVGEvkrvvnallQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 315 TLDEYRQYI----------EKDAALERRFQ-KVFVAEPSVEDTIAILRGLKERYELhhHVQITDPAIVAAAT-LSHRYIA 382
Cdd:COG1223 128 ELDGLPSGSvviaatnhpeLLDSALWRRFDeVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEgLSGADIE 205
|
.
gi 891174144 383 D 383
Cdd:COG1223 206 K 206
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
204-280 |
8.85e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This 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: 410911 [Multi-domain] Cd Length: 165 Bit Score: 40.74 E-value: 8.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891174144 204 LIGEPGVGKTAIVEGLAQRIingevpeglkGRRVLSLDmGALIAGaKYRGEFEERLKAVLSDlAKQEGNVILFIDEL 280
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSIS-GPSIVS-KYLGESEKNLREIFEE-ARSHAPSIIFIDEI 102
|
|
| PRK08116 |
PRK08116 |
hypothetical protein; Validated |
601-752 |
1.00e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236153 [Multi-domain] Cd Length: 268 Bit Score: 41.93 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 601 FLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMekhsvSRLVGAPPGYVGYEEGGYLTEAVRrrpYSVILLDE-- 678
Cdd:PRK08116 117 LLLWGSVGTGKTYLAACIANELIEKGVPVIFVNFPQLL-----NRIKSTYKSSGKEDENEIIRSLVN---ADLLILDDlg 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 679 VEK----AHPDVFNILlqvldDGRLTDGQGrtvdfrntvVIMTSNLGSDLIQERFGALSYDAMKEMVMAV--VSQSFRPE 752
Cdd:PRK08116 189 AERdtewAREKVYNII-----DSRYRKGLP---------TIVTTNLSLEELKNQYGKRIYDRILEMCTPVenEGKSYRKE 254
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
570-696 |
2.02e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.64 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 570 VIGQNEAVEAVSNAIR-------RSRAGLADPNRpigsFLFLGPTGVGKTELCKALAN---FMFdsddAMVRID--MSEF 637
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGelkLPL----LTVRLDslIGSY 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 891174144 638 MEKhSVSRLVGappgyvgyeeggyLTEAVRRRPySVILLDEVE---------KAHPD---VFNILLQVLDD 696
Cdd:COG1223 76 LGE-TARNLRK-------------LFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
570-684 |
5.14e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 40.29 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 570 VIGQNEAVEAVSNAIRRSRAGlaDPNRPIgsfLFLGPTGVGKTELCKALANFM-FDsddaMVRIDMSEFMEKHSVSRLVG 648
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALANDYgWE----VIELNASDQRTADVIERVAG 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 891174144 649 AppgyvgyeegGYLTEAVRRRPYSVILLDEVEKAHP 684
Cdd:PRK04195 87 E----------AATSGSLFGARRKLILLDEVDGIHG 112
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
204-285 |
6.28e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 38.56 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 204 LIGEPGVGKTAIVEGLAQRiingevpeglKGRRVLSLDMGALIagAKYRGEFEERLKAVLSdLAKQEGNVILFIDELHTM 283
Cdd:cd19520 40 LYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFS-LASKLQPSIIFIDEIDSF 106
|
..
gi 891174144 284 VG 285
Cdd:cd19520 107 LR 108
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
570-619 |
6.81e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 39.68 E-value: 6.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 570 VIGQNEAVEAVSNAI----RRSRagLADPNR----P--IgsfLFLGPTGVGKTELCKALA 619
Cdd:PRK05201 17 IIGQDDAKRAVAIALrnrwRRMQ--LPEELRdevtPknI---LMIGPTGVGKTEIARRLA 71
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
570-622 |
7.64e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain] Cd Length: 251 Bit Score: 39.12 E-value: 7.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 891174144 570 VIGQNEAVE----AVSNAIRRSRAGLADPNRPI----GSFLFLGPTGVGKTELCKALANFM 622
Cdd:cd19497 14 VIGQERAKKvlsvAVYNHYKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
180-377 |
9.80e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 39.30 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 180 VIGRDEEIRRTIQvlqrrTKNNPVLI--GEPGVGKTAivegLAqRIINGEVpeglkGRRVLSLDmgALIAGAKyrgefee 257
Cdd:PRK13342 20 LLGPGKPLRRMIE-----AGRLSSMIlwGPPGTGKTT----LA-RIIAGAT-----DAPFEALS--AVTSGVK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174144 258 RLKAVLSDlAKQE----GNVILFIDELHTMvgaGKADgaMDAgnmLKPALARGELHCVGATTldEyRQYIEKDAALERRF 333
Cdd:PRK13342 76 DLREVIEE-ARQRrsagRRTILFIDEIHRF---NKAQ--QDA---LLPHVEDGTITLIGATT--E-NPSFEVNPALLSRA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 891174144 334 QkVFVAEP-SVEDTIAIL-RGLKERYELhhHVQITDPAIVAAATLS 377
Cdd:PRK13342 144 Q-VFELKPlSEEDIEQLLkRALEDKERG--LVELDDEALDALARLA 186
|
|
| |
