|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
4-675 |
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: 954.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 4 SALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARIV 83
Cdd:COG0542 160 PALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 84 ELDMGAIMAGTIWRGQLEERLKDVMTEVKGSEGKVIVFIDEIHMLV---RSDHQGTAAEILKPALGRGGFRCIGATTLKE 160
Cdd:COG0542 240 SLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVgagGAEGAMDAANLLKPALARGELRCIGATTLDE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 161 YKRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEAS 240
Cdd:COG0542 320 YRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 241 ACMRVQLDTQSEELDELQNEKSKLEAEAKKELNDVNNQLQPLLSKYQKQKSEMEKLTKLKQKKQEilVEIQAAQKRQDLI 320
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWE--AEKELIEEIQELK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 321 RAADLRRQKLDDVELKIGDVERRIRKHGFIEKDTVGPEEIADEVSRWTGVPVSRLTGEEKEWVMGLAGRLKKRVVGQNEA 400
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDEA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 401 VDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIGSPPGYVGY 480
Cdd:COG0542 558 VEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYVGY 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 481 HEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNLGAGHL--FSEKYCPMQ 558
Cdd:COG0542 638 EEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELIldLAEDEPDYE 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 559 VARERVIQKVKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKSALDFVLDQSFDPVYGAR 638
Cdd:COG0542 718 EMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGAR 797
|
650 660 670
....*....|....*....|....*....|....*..
gi 1775893503 639 PIRRWLEKKVVTNISKMLMKEEIGEEYTVYVDANDDG 675
Cdd:COG0542 798 PLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
5-675 |
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: 871.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 5 ALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARIVE 84
Cdd:TIGR03346 155 ALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 85 LDMGAIMAGTIWRGQLEERLKDVMTEVKGSEGKVIVFIDEIHMLV---RSDHQGTAAEILKPALGRGGFRCIGATTLKEY 161
Cdd:TIGR03346 235 LDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVgagKAEGAMDAGNMLKPALARGELHCIGATTLDEY 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 162 KRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEASA 241
Cdd:TIGR03346 315 RKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 242 CMRVQLDTQSEELDELQNEKSKLEAEAK------------------KELNDVNNQLQPLLSKYQKQKSEMEKLTKLKQKK 303
Cdd:TIGR03346 395 RIRMEIDSKPEELDELDRRIIQLEIEREalkkekdeaskkrledleKELADLEEEYAELEEQWKAEKASIQGIQQIKEEI 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 304 QEILVEIQAAQKRQDLIRAADLRRQKLDDVELKIGDVERRIRKHGF-IEKDTVGPEEIADEVSRWTGVPVSRLTGEEKEW 382
Cdd:TIGR03346 475 EQVRLELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQNrLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREK 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 383 VMGLAGRLKKRVVGQNEAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYM 462
Cdd:TIGR03346 555 LLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYM 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 463 EKHSVSRLIGSPPGYVGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTS 542
Cdd:TIGR03346 635 EKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTS 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 543 NLGAGHLFS-EKYCPMQVARERVIQKVKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKS 621
Cdd:TIGR03346 715 NLGSDFIQElAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDA 794
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1775893503 622 ALDFVLDQSFDPVYGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVYVDANDDG 675
Cdd:TIGR03346 795 ALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
3-674 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 696.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 3 KSALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARI 82
Cdd:PRK10865 158 RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 83 VELDMGAIMAGTIWRGQLEERLKDVMTEVKGSEGKVIVFIDEIHMLV---RSDHQGTAAEILKPALGRGGFRCIGATTLK 159
Cdd:PRK10865 238 LALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVgagKADGAMDAGNMLKPALARGELHCVGATTLD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 160 EYKRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEA 239
Cdd:PRK10865 318 EYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 240 SACMRVQLDTQSEELDELQNE--KSKLEAEAKK----------------ELNDVNNQLQPLLSKYQKQKSEMEKLTKLKQ 301
Cdd:PRK10865 398 ASSIRMQIDSKPEELDRLDRRiiQLKLEQQALMkesdeaskkrldmlneELSDKERQYSELEEEWKAEKASLSGTQTIKA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 302 KKQEILVEIQAAQKRQDLIRAADLRRQKLDDVELKIGDVERRIRKHGFIEKDTVGPEEIADEVSRWTGVPVSRLTGEEKE 381
Cdd:PRK10865 478 ELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESERE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 382 WVMGLAGRLKKRVVGQNEAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEY 461
Cdd:PRK10865 558 KLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEF 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 462 MEKHSVSRLIGSPPGYVGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMT 541
Cdd:PRK10865 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 542 SNLGAgHLFSEKYCPMQVA--RERVIQKVKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSMMKDVARRLSEKGIAMAVT 619
Cdd:PRK10865 718 SNLGS-DLIQERFGELDYAhmKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHIS 796
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1775893503 620 KSALDFVLDQSFDPVYGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVYVDANDD 674
Cdd:PRK10865 797 DEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-676 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 672.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 1 MAKSALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGA 80
Cdd:CHL00095 157 SKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 81 RIVELDMGAIMAGTIWRGQLEERLKDVMTEVKgSEGKVIVFIDEIHMLV---RSDHQGTAAEILKPALGRGGFRCIGATT 157
Cdd:CHL00095 237 LVITLDIGLLLAGTKYRGEFEERLKRIFDEIQ-ENNNIILVIDEVHTLIgagAAEGAIDAANILKPALARGELQCIGATT 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 158 LKEYKRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVD 237
Cdd:CHL00095 316 LDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLD 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 238 EASAcmRVQLdtqseeldelqnekskleaeakkelndVNNQLQPLLSKYQKQksemekltklkqkKQEILVEIQAAQKRQ 317
Cdd:CHL00095 396 EAGS--RVRL---------------------------INSRLPPAARELDKE-------------LREILKDKDEAIREQ 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 318 DLIRAADLR-RQKLDDVELKIGDVERRIRKHGFIEKDTVGPEEIADEVSRWTGVPVSRLTGEEKEWVMGLAGRLKKRVVG 396
Cdd:CHL00095 434 DFETAKQLRdREMEVRAQIAAIIQSKKTEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 397 QNEAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIGSPPG 476
Cdd:CHL00095 514 QDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPG 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 477 YVGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNLGAGH-------- 548
Cdd:CHL00095 594 YVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVietnsggl 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 549 ---LFSEKYCPMQVAR--ERVIQKVKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKSAL 623
Cdd:CHL00095 674 gfeLSENQLSEKQYKRlsNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIK 753
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1775893503 624 DFVLDQSFDPVYGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVYVDANDDGK 676
Cdd:CHL00095 754 TLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
3-662 |
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: 612.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 3 KSALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARI 82
Cdd:TIGR03345 167 TSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 83 VELDMGAIMAGTIWRGQLEERLKDVMTEVKGSEGKVIVFIDEIHMLVRSDHQ---GTAAEILKPALGRGGFRCIGATTLK 159
Cdd:TIGR03345 247 LSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQagqGDAANLLKPALARGELRTIAATTWA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 160 EYKRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEA 239
Cdd:TIGR03345 327 EYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDTA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 240 SACMRVQLDTQSEELDELQNEKSKLEAEA--------------------KKELNDVNNQLQPLLSKYQKQKSEMEKLTKL 299
Cdd:TIGR03345 407 CARVALSQNATPAALEDLRRRIAALELELdalereaalgadhderlaelRAELAALEAELAALEARWQQEKELVEAILAL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 300 KqkkqEILVEIQAAQKRQDLIRAADLR--RQKLDDVElkiGDvERRIRKHgfiekdtVGPEEIADEVSRWTGVPVSRLTG 377
Cdd:TIGR03345 487 R----AELEADADAPADDDDALRAQLAelEAALASAQ---GE-EPLVFPE-------VDAQAVAEVVADWTGIPVGRMVR 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 378 EEKEWVMGLAGRLKKRVVGQNEAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRID 457
Cdd:TIGR03345 552 DEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITIN 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 458 MSEYMEKHSVSRLIGSPPGYVGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTV 537
Cdd:TIGR03345 632 MSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTV 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 538 IIMTSNLG----AGHLFSEKYCPMQVARERVIQ-KVKEHFKPEFVNRLdEILIFRPLSKIQQRRVTKSMMKDVARRLSEK 612
Cdd:TIGR03345 712 ILLTSNAGsdliMALCADPETAPDPEALLEALRpELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKEN 790
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1775893503 613 -GIAMAVTKSALDFVLDQSFDPVYGARPIRRWLEKKVVTNIS-----KMLMKEEIG 662
Cdd:TIGR03345 791 hGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSrqileRLAAGEPIE 846
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
3-657 |
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: 609.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 3 KSALETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARI 82
Cdd:TIGR02639 161 QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNAKI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 83 VELDMGAIMAGTIWRGQLEERLKDVMTEVKGSEGKvIVFIDEIHMLVRSDHQG----TAAEILKPALGRGGFRCIGATTL 158
Cdd:TIGR02639 241 YSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGATSggsmDASNLLKPALSSGKIRCIGSTTY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 159 KEYKRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDE 238
Cdd:TIGR02639 320 EEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 239 ASACMRvqldtqseeldelqnekskLEAEAKKelndvnnqlqpllskyqkqksemekltklkqkkqeilveiqaaqkrqd 318
Cdd:TIGR02639 400 AGAAFR-------------------LRPKAKK------------------------------------------------ 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 319 liraadlrrqklddvelkigdverrirkhgfieKDTVGPEEIADEVSRWTGVPVSRLTGEEKEWVMGLAGRLKKRVVGQN 398
Cdd:TIGR02639 413 ---------------------------------KANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQD 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 399 EAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELfndENRMVRIDMSEYMEKHSVSRLIGSPPGYV 478
Cdd:TIGR02639 460 EAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFDMSEYMEKHTVSRLIGSPPGYV 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 479 GYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNLGAghlfSE-KYCPM 557
Cdd:TIGR02639 537 GFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGA----SEmSKPPI 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 558 QVARERVIQK----VKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKSALDFVLDQSFDP 633
Cdd:TIGR02639 613 GFGGENRESKslkaIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDE 692
|
650 660
....*....|....*....|....
gi 1775893503 634 VYGARPIRRWLEKKVVTNISKMLM 657
Cdd:TIGR02639 693 EFGARPLARVIQEEIKKPLSDEIL 716
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
6-684 |
1.17e-141 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 433.88 E-value: 1.17e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 6 LETYGHDLVEKAEKQTLDPIFGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARIVEL 85
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 86 DMGAIMAGTIWRGQLEERLKDVMTEVKgSEGKVIVFIDEIHMLV----RSDHQGTAAEILKPALGRGGFRCIGATTLKEY 161
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIgagaASGGQVDAANLIKPLLSSGKIRVIGSTTYQEF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 162 KRYIEKDGALARRFKQVYVNEPSVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEASA 241
Cdd:PRK11034 328 SNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 242 CMRvqldtqseeldelqnekskleaeakkelndvnnqLQPllskyqkqksemekltklkqkkqeilveiqaaqkrqdlir 321
Cdd:PRK11034 408 RAR----------------------------------LMP---------------------------------------- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 322 aadlrrqklddvelkigdVERRirkhgfieKDTVGPEEIADEVSRWTGVPVSRLTGEEKEWVMGLAGRLKKRVVGQNEAV 401
Cdd:PRK11034 414 ------------------VSKR--------KKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAI 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 402 DSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTE----LAKGLAHELfndenrmVRIDMSEYMEKHSVSRLIGSPPGY 477
Cdd:PRK11034 468 EALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLSKALGIEL-------LRFDMSEYMERHTVSRLIGAPPGY 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 478 VGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNLGAGHLFSEKYCPM 557
Cdd:PRK11034 541 VGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 558 QVARER-VIQKVKEHFKPEFVNRLDEILIFRPLSK--IQQrrVTKSMMKDVARRLSEKGIAMAVTKSALDFVLDQSFDPV 634
Cdd:PRK11034 621 HQDNSTdAMEEIKKIFTPEFRNRLDNIIWFDHLSTdvIHQ--VVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRA 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1775893503 635 YGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVYVDANDDGKDLKYNVEK 684
Cdd:PRK11034 699 MGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQS 748
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
389-586 |
4.57e-97 |
|
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: 297.55 E-value: 4.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 389 RLKKRVVGQNEAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVS 468
Cdd:cd19499 8 RLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMEKHSVS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 469 RLIGSPPGYVGYHEGGQLTEPVKRRPYCVVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNlgagh 548
Cdd:cd19499 88 RLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSN----- 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1775893503 549 lfsekycpmqvarerviqkvkeHFKPEFVNRLDEILIF 586
Cdd:cd19499 163 ----------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
421-583 |
4.23e-85 |
|
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: 265.98 E-value: 4.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 421 PNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIGSPPGYVGYHEGGQLTEPVKRRPYCVVLL 500
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 501 DEVEKAHVDVLNILLQVLDDGRLTDGQGSTVDFRNTVIIMTSNLGAGHL----FSEKYCPMQVARERVIQKVKEHFKPEF 576
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKIsdasRLGDSPDYELLKEEVMDLLKKGFIPEF 161
|
....*..
gi 1775893503 577 VNRLDEI 583
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 ... |
184-287 |
9.72e-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: 127.60 E-value: 9.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 184 SVEDSINILRVLKERYEKHHVLIIKDSALIAAAKLSHRYITGRRLPDKAIDLVDEASACMRVQLDTQSEELDELQNEKSK 263
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 1775893503 264 LEAEAKKELNDVNNQLQPLLSKYQ 287
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
416-552 |
2.24e-21 |
|
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: 91.05 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 416 ALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIgsppgyvGYHEGGQLTEPVKRRPY 495
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF-------GHFLVRLLFELAEKAKP 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1775893503 496 CVVLLDEVEKAHVDVLNILLQVLDDGRLTdgqgsTVDFRNTVIIMTSNLGAGHLFSE 552
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGDLDR 137
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
26-178 |
3.52e-19 |
|
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: 84.89 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 26 FGRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKfaagnvpAKLSGARIVELDMGAIMAGTIWRGQLEERLK 105
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANE-------LFRPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1775893503 106 DVMTEVKGSEGKVIVFIDEIHMLVRSDHQG---TAAEILKPALGRGGFRCIGATTLKEykrYIEKDGALARRFKQV 178
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSLSRGAQNAllrVLETLNDLRIDRENVRVIGATNRPL---LGDLDRALYDRLDIR 146
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
589-669 |
5.31e-16 |
|
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: 73.21 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 589 LSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKSALDFVLDQSFDPVYGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVY 668
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1775893503 669 V 669
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
589-675 |
9.31e-15 |
|
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: 70.17 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 589 LSKIQQRRVTKSMMKDVARRLSEKGIAMAVTKSALDFVLDQSFDPVYGARPIRRWLEKKVVTNISKMLMKEEIGEEYTVY 668
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*..
gi 1775893503 669 VDANDDG 675
Cdd:smart01086 81 VDVDDGE 87
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
421-545 |
1.59e-13 |
|
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: 68.55 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 421 PNGSFLFLGPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIGSPPGYVGYHEGGQ----LTEPVKRRPYC 496
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1775893503 497 VVLLDEVEKAHVDVLNILLQVLDDGRLTDGQGStvdFRNTVIIMTSNLG 545
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
424-543 |
1.69e-13 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 68.09 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 424 SFLFLGPSGVGKTELAKGLAHELFNDENRMVRidMSEYMEKhsvSRLIGsppgyvGYHEGGQLTE----PVKR--RPYCV 497
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFG------RRNIDPGGASwvdgPLVRaaREGEI 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1775893503 498 VLLDEVEKAHVDVLNILLQVLDDGRLTDGQGST---VDFRNTVIIMTSN 543
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
48-175 |
7.30e-13 |
|
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: 66.08 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKfaagnvpaklSGARIVELDMGAIMAGtiWRGQLEERLKDVMTEVKgSEGKVIVFIDEIHM 127
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKE----------LGAPFIEISGSELVSK--YVGESEKRLRELFEAAK-KLAPCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 128 LVRSDHQGT------AAEILKPALGR-----GGFRCIGATTlkeykrYIEK-DGALARRF 175
Cdd:pfam00004 69 LAGSRGSGGdsesrrVVNQLLTELDGftssnSKVIVIAATN------RPDKlDPALLGRF 122
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
399-544 |
1.04e-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: 63.46 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 399 EAVDSVAEAVMRFRAGLALPNQPNGSFLFLGPSGVGKTELAKGLAHELFNDenrMVRIDMSEYMEKhsvsrligsppgYV 478
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSK------------YV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 479 GYHEG--GQLTEPVKRRPYCVVLLDEVEKA------------HVDVLNILLQVLDDGRLTDgqgstvdfrNTVIIMTSNL 544
Cdd:cd19481 68 GESEKnlRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATNR 138
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
48-198 |
1.53e-09 |
|
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: 60.70 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALaqkfaagnvpAKLSGARIVELDMGAIMAGtiWRGQLEERLKDVMTEVKGSEGkVIVFIDEIHM 127
Cdd:COG0464 195 LLYGPPGTGKTLLARAL----------AGELGLPLIEVDLSDLVSK--YVGETEKNLREVFDKARGLAP-CVLFIDEADA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 128 LVR---SDHQGTA----AEILK--PALGRGGFrCIGATTLKEykryiEKDGALARRF-KQVYVNEPSVEDSINILRV-LK 196
Cdd:COG0464 262 LAGkrgEVGDGVGrrvvNTLLTemEELRSDVV-VIAATNRPD-----LLDPALLRRFdEIIFFPLPDAEERLEIFRIhLR 335
|
..
gi 1775893503 197 ER 198
Cdd:COG0464 336 KR 337
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
426-543 |
2.75e-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: 52.98 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 426 LFLGPSGVGKTELAKGLAHELFndeNRMVRIDMSEYMEKHsvsrlIGSPPGYVgyhegGQLTEPVKRRPYCVVLLDEVEK 505
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG---APFIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1775893503 506 -----------AHVDVLNILLQVLDdgrltdgqGSTVDFRNTVIIMTSN 543
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-175 |
8.27e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKFaagnvpaKLSGARIVELDMGAIMAGTIWRGQL------------EERLKDVMTEVKGSE 115
Cdd:smart00382 6 LIVGPPGSGKTTLARALAREL-------GPPGGGVIYIDGEDILEEVLDQLLLiivggkkasgsgELRLRLALALARKLK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775893503 116 GKVIvFIDEIHMLVRSDHQG-----TAAEILKPALGRGGFRCIGATTLkeykRYIEKDGALARRF 175
Cdd:smart00382 79 PDVL-ILDEITSLLDAEQEAlllllEELRLLLLLKSEKNLTVILTTND----EKDLGPALLRRRF 138
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
48-219 |
2.31e-07 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 53.94 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKFaagnvpaklsGARIVELDmgAIMAGTiwrgqleERLKDVMTEVK---GSEGKVIVFIDE 124
Cdd:PRK13342 40 ILWGPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGV-------KDLREVIEEARqrrSAGRRTILFIDE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 125 IHMLVRSdHQgtaaEILKPALGRGGFRCIGATTlkEyKRYIEKDGALARRfKQVYVNEP-SVEDSINIL-RVLKERYEKh 202
Cdd:PRK13342 101 IHRFNKA-QQ----DALLPHVEDGTITLIGATT--E-NPSFEVNPALLSR-AQVFELKPlSEEDIEQLLkRALEDKERG- 170
|
170
....*....|....*..
gi 1775893503 203 hVLIIKDSALIAAAKLS 219
Cdd:PRK13342 171 -LVELDDEALDALARLA 186
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
394-520 |
2.49e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 52.58 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 394 VVGQNEAVDSVAEAVMRFRAGLALP---NQPNGSFLFLGPSGVGKTELAKGLAHELfndenrMVRIDMSEYmekhsvSRL 470
Cdd:COG1223 4 VVGQEEAKKKLKLIIKELRRRENLRkfgLWPPRKILFYGPPGTGKTMLAEALAGEL------KLPLLTVRL------DSL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1775893503 471 IGSppgYVGyhEGG----QLTEPVKRRPyCVVLLDEVE---------KAHVD---VLNILLQVLDD 520
Cdd:COG1223 72 IGS---YLG--ETArnlrKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
305-604 |
4.69e-07 |
|
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: 52.61 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 305 EILVEIQAAQKRQDLIRAADLRRQKLDDVELKIGDVERRIRKHGFIEKDTVGPEEIADEVSRWTGVPVSRLTGEEKEWVM 384
Cdd:COG0464 70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 385 GLAGRLKKRVVGQNEAVDSVAEAVMRFRAGLALPNQ----PNGSFLFLGPSGVGKTELAKGLAHELfndENRMVRIDMSE 460
Cdd:COG0464 150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 461 ymekhsvsrLIGsppGYVGyhEggqlTEP--------VKRRPYCVVLLDEVEKAHVD-----------VLNILLQVLDDG 521
Cdd:COG0464 227 ---------LVS---KYVG--E----TEKnlrevfdkARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEEL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 522 RltdgqgstvdfRNTVIIMTSNLgaghlfsekycpmqvarerviqkvKEHFKPEFVNRLDEILIFRPLSKIQQRRVTKSM 601
Cdd:COG0464 289 R-----------SDVVVIAATNR------------------------PDLLDPALLRRFDEIIFFPLPDAEERLEIFRIH 333
|
...
gi 1775893503 602 MKD 604
Cdd:COG0464 334 LRK 336
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
48-157 |
9.09e-07 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 51.98 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKfaagnvpaklSGARIVELDmgAIMAGTiwrgqleERLKDVMTEVK---GSEGKVIVFIDE 124
Cdd:COG2256 53 ILWGPPGTGKTTLARLIANA----------TDAEFVALS--AVTSGV-------KDIREVIEEARerrAYGRRTILFVDE 113
|
90 100 110
....*....|....*....|....*....|....*
gi 1775893503 125 IHMLVRS--DhqgtaaeILKPALGRGGFRCIGATT 157
Cdd:COG2256 114 IHRFNKAqqD-------ALLPHVEDGTITLIGATT 141
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
48-125 |
9.62e-06 |
|
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: 46.52 E-value: 9.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKfaagnvpaklSGARIVELDMGAIMAGtiWRGQLEERLKDVMTEVKgSEGKVIVFIDEI 125
Cdd:cd19503 38 LLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVSK--YLGESEKNLREIFEEAR-SHAPSIIFIDEI 102
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
48-175 |
1.59e-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: 44.98 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKFAAGNV-----PAKLSGARIV---ELDMGaimaGTIWRGQleerlkDVMTEVKGSEgkvI 119
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqlTRDTTEEDLFgrrNIDPG----GASWVDG------PLVRAAREGE---I 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1775893503 120 VFIDEIHMLVRSdhqgtAAEILKPAL---------GRG-------GFRCIgATTLKEYKRYIEKDGALARRF 175
Cdd:pfam07728 70 AVLDEINRANPD-----VLNSLLSLLderrlllpdGGElvkaapdGFRLI-ATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
48-126 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKfaAGNVPAKLSGARIVEldmgaimagtIWRGQLEERLKDVMTEVKgSEGKVIVFIDEIH 126
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGE--LGLPLIVVKLSSLLS----------KYVGESEKNLRKIFERAR-RLAPCILFIDEID 95
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
394-540 |
4.10e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 46.15 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 394 VVGQNEAVDSVAEAVMRF--------RAGLalpnQPNGSFLFLGPSGVGKTELAKGLAHEL---FndenrmVRIDMSEYM 462
Cdd:COG1222 80 IGGLDEQIEEIREAVELPlknpelfrKYGI----EPPKGVLLYGPPGTGKTLLAKAVAGELgapF------IRVRGSELV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 463 EKhsvsrligsppgYVGyhEGGQLTEPV-----KRRPyCVVLLDEVE---KAHVD---------VLNILLQVLDDgrltd 525
Cdd:COG1222 150 SK------------YIG--EGARNVREVfelarEKAP-SIIFIDEIDaiaARRTDdgtsgevqrTVNQLLAELDG----- 209
|
170
....*....|....*
gi 1775893503 526 gqgstVDFRNTVIIM 540
Cdd:COG1222 210 -----FESRGDVLII 219
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
48-179 |
6.38e-05 |
|
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: 43.95 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALaqkfaagnvpAKLSGARIVELDMGAIMAGtiWRGQlEERLKDVMTEVKGSEGKVIVFIDEIHM 127
Cdd:cd19520 39 LLYGPPGCGKTMLAKAT----------AKEAGARFINLQVSSLTDK--WYGE-SQKLVAAVFSLASKLQPSIIFIDEIDS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1775893503 128 LVR----SDHQGTA---AEILKPALG-RGGFRC----IGATTlkeykRYIEKDGALARRFKQVY 179
Cdd:cd19520 106 FLRqrssTDHEATAmmkAEFMSLWDGlSTDGNCrvivMGATN-----RPQDLDEAILRRMPKRF 164
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
382-463 |
7.05e-05 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 45.75 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 382 WVMGLAGRLKKRVVGQNEAVDSVAEAVmrfraglALPNQPNgsFLFLGPSGVGKTELAKGLAHELFND--ENRMVRIDMS 459
Cdd:PRK12402 5 WTEKYRPALLEDILGQDEVVERLSRAV-------DSPNLPH--LLVQGPPGSGKTAAVRALARELYGDpwENNFTEFNVA 75
|
....
gi 1775893503 460 EYME 463
Cdd:PRK12402 76 DFFD 79
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
422-522 |
2.89e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.17 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 422 NGSFLFL-GPSGVGKTELAKGLAHELFNDENRMVRIDMSEYMEKHSVSRLIGS-----PPGYVGYHEGGQLTEP--VKRR 493
Cdd:pfam13401 4 GAGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRalglpLSGRLSKEELLAALQQllLALA 83
|
90 100
....*....|....*....|....*....
gi 1775893503 494 PYCVVLLDEVEKAHVDVLNILLQVLDDGR 522
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
230-345 |
7.33e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.43 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 230 DKAIDLVDEASACMRVQLDTQSEELDELQNEKSKLEA---EAKKELNDVNNQLQPLLSKYQKQKSemekltklkqkkqei 306
Cdd:pfam15619 45 EKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEkerDLERKLKEKEAELLRLRDQLKRLEK--------------- 109
|
90 100 110
....*....|....*....|....*....|....*....
gi 1775893503 307 LVEIQAAQKRQDLIRAADLRRQKLDDVELKIGDVERRIR 345
Cdd:pfam15619 110 LSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLE 148
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
28-223 |
8.34e-04 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 42.97 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 28 RHKEICRLLTILCRKtkcNPILIGEPGVGKTAIVEALAQKfaagnvpaklSGARIVELDMGAIMAGtiWRGQLEERLKDV 107
Cdd:TIGR01243 199 KHPELFEHLGIEPPK---GVLLYGPPGTGKTLLAKAVANE----------AGAYFISINGPEIMSK--YYGESEERLREI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 108 MTEVKgSEGKVIVFIDEIHMLV--RSDHQGTAAEILKPAL--------GRGGFRCIGATTlkeykRYIEKDGALAR--RF 175
Cdd:TIGR01243 264 FKEAE-ENAPSIIFIDEIDAIApkREEVTGEVEKRVVAQLltlmdglkGRGRVIVIGATN-----RPDALDPALRRpgRF 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1775893503 176 -KQVYVNEPSVEDSINILRVlkeryEKHHVLIIKDSALIAAAKLSHRYI 223
Cdd:TIGR01243 338 dREIVIRVPDKRARKEILKV-----HTRNMPLAEDVDLDKLAEVTHGFV 381
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
48-180 |
8.45e-04 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). 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: 410917 [Multi-domain] Cd Length: 163 Bit Score: 40.80 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKfaagnvpaklSGARIVELDMGAIMAGtiWRGQlEERLKDVMTEVKGSEGKVIVFIDEIHM 127
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASE----------SGSTFFSISASSLVSK--WVGE-SEKIVRALFALARELQPSIIFIDEIDS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1775893503 128 LVR----SDHQGTA---AEILK-----PALGRGGFRCIGATTLKEykryiEKDGALARRF-KQVYV 180
Cdd:cd19509 103 LLSergsGEHEASRrvkTEFLVqmdgvLNKPEDRVLVLGATNRPW-----ELDEAFLRRFeKRIYI 163
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
397-543 |
1.17e-03 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 41.50 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 397 QNEAVDSVAEAVMRFRAGLALpnqpngsfLFLGPSGVGKTELAKGLAHELFNDEnrmvRIDMSEYMEKHSVSRLIGSPPG 476
Cdd:COG0470 1 QEEAWEQLLAAAESGRLPHAL--------LLHGPPGIGKTTLALALARDLLCEN----PEGGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 477 Y--VGYHEGG---------QLTEPVKRRPYC----VVLLDEVEKAHVDVLNILLQVLDDGRltdgqgstvdfRNTVIIMT 541
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 1775893503 542 SN 543
Cdd:COG0470 138 AN 139
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
394-453 |
1.23e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 41.78 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 394 VVGQNEAVdsvaEAVMRFRAGLALPNqpngsFLFLGPSGVGKTELAKGLAHELFNDENRM 453
Cdd:PRK00440 19 IVGQEEIV----ERLKSYVKEKNMPH-----LLFAGPPGTGKTTAALALARELYGEDWRE 69
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
21-128 |
1.28e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 21 TLDPIF----GRHKEICRLLTILCRKTKCNPILIGEPGVGKTAIVEALAQKFAAGNVPAKLSGARIVELDM-GAIMAG-- 93
Cdd:COG3267 16 TPDPRFlflsPSHREALARLEYALAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNPQLSPAELlRAIADElg 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 1775893503 94 ----TIWRGQLEERLKDVMTEVKGSEGKVIVFIDEIHML 128
Cdd:COG3267 96 lepkGASKADLLRQLQEFLLELAAAGRRVVLIIDEAQNL 134
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
24-207 |
1.45e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 24 PIFGRHKEICRLLTILCRKTKCNP---ILIGEPGVGKTAIVEALAQKFAAGNVpaKLSGARIVELDMGAIMAGTIWRGQL 100
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG--YFLRGKCDENLPYSPLLEALTREGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 101 EERLKDVMTEVKGSEGKviVFIDEIHMLVRSDHqGTAAEILKPALGrggfRCIGATTLKEYKRYIEKDGA-LARrfkqvy 179
Cdd:pfam13191 79 LRQLLDELESSLLEAWR--AALLEALAPVPELP-GDLAERLLDLLL----RLLDLLARGERPLVLVLDDLqWAD------ 145
|
170 180
....*....|....*....|....*...
gi 1775893503 180 vnepsvEDSINILRVLKERYEKHHVLII 207
Cdd:pfam13191 146 ------EASLQLLAALLRLLESLPLLVV 167
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
48-141 |
1.65e-03 |
|
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: 39.66 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKFaagNVPaklsgarIVELDMGAIMAGTIwrGQLEERLKDVMTEVKGSeGKVIVFIDEIH- 126
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAGVW---QLP-------LLRLDMGRLFGGLV--GESESRLRQMIQTAEAI-APCVLWIDEIEk 101
|
90
....*....|....*....
gi 1775893503 127 ----MLVRSDHqGTAAEIL 141
Cdd:cd19507 102 gfsnADSKGDS-GTSSRVL 119
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
389-443 |
2.81e-03 |
|
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: 39.29 E-value: 2.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1775893503 389 RLKKRVVGQNEAVDSVAEAV------MRFRAGLALPNQPNgSFLFLGPSGVGKTELAKGLA 443
Cdd:cd19498 8 ELDKYIIGQDEAKRAVAIALrnrwrrMQLPEELRDEVTPK-NILMIGPTGVGKTEIARRLA 67
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-329 |
5.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 234 DLVDEASAcMRVQLDTQSEELDELQNEKSKLEaEAKKELNDVNNQLQPLLSKYQKQKSEMEKLTKLKQKKQEILVEIQAA 313
Cdd:COG3883 116 DFLDRLSA-LSKIADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
90
....*....|....*.
gi 1775893503 314 QKRQDLIRAADLRRQK 329
Cdd:COG3883 194 AEAQLAELEAELAAAE 209
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
35-66 |
5.75e-03 |
|
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: 39.38 E-value: 5.75e-03
10 20 30
....*....|....*....|....*....|...
gi 1775893503 35 LLTILCRKtkcnPILI-GEPGVGKTAIVEALAQ 66
Cdd:COG0714 25 LIALLAGG----HLLLeGVPGVGKTTLAKALAR 53
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
48-194 |
6.25e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.60 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 48 ILIGEPGVGKTAIVEALAQKFaagNVP-AKLSGARIVeldmgaimagTIWRGQLEERLKDVMTEVKgSEGKVIVFIDEIH 126
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGEL---GAPfIRVRGSELV----------SKYIGEGARNVREVFELAR-EKAPSIIFIDEID 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 127 MLVRS-DHQGTAAEI--LKPAL--------GRGGFRCIGATTlkeykRYIEKDGALAR--RF-KQVYVNEPSVEDSINIL 192
Cdd:COG1222 182 AIAARrTDDGTSGEVqrTVNQLlaeldgfeSRGDVLIIAATN-----RPDLLDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
..
gi 1775893503 193 RV 194
Cdd:COG1222 257 KI 258
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
402-519 |
6.80e-03 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 38.31 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1775893503 402 DSVAEAVMRFRAGLALPNQPNGSFL-FLGPSGVGKTELAKGLAHELfndENRMVRIDMSEYmekHSVSRLIGSPPGYVGY 480
Cdd:cd19500 16 EDVKERILEYLAVRKLKGSMKGPILcLVGPPGVGKTSLGKSIARAL---GRKFVRISLGGV---RDEAEIRGHRRTYVGA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1775893503 481 HEG---GQLTEPVKRRPycVVLLDEVEK----AHVDVLNILLQVLD 519
Cdd:cd19500 90 MPGriiQALKKAGTNNP--VFLLDEIDKigssFRGDPASALLEVLD 133
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
426-445 |
9.32e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 38.22 E-value: 9.32e-03
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
390-446 |
9.69e-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: 38.35 E-value: 9.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1775893503 390 LKKRVVGQNEAVDSVAEAV----MRFRAGLALPNQ----PNGSFLFLGPSGVGKTELAKGLAHEL 446
Cdd:cd19497 10 LDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDdvelEKSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| |
