|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-759 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1596.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSsDSASQPGS 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSS-DPGSQPNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 161 EEQTGGEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEV 240
Cdd:PRK11034 160 EEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 241 MADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVI 320
Cdd:PRK11034 240 MADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 321 GSTTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPDKAI 400
Cdd:PRK11034 320 GSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 401 DVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKSLGDRLKMLVFGQDKAIEALTEAIKMSRA 480
Cdd:PRK11034 400 DVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 481 GLGHDHKPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHA 560
Cdd:PRK11034 480 GLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 561 VLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPE 640
Cdd:PRK11034 560 VLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 641 FRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:PRK11034 640 FRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANE 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 446856817 721 LLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKPEAAH 759
Cdd:PRK11034 720 LLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH 758
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-736 |
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: 1126.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPaSEEERDTQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 82 LSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEpsqSSSDSASQPGSE 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDD---GKDQLGEEAGKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 162 EQTGgEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 241
Cdd:TIGR02639 157 EEKG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 242 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 321
Cdd:TIGR02639 236 KNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 322 STTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPDKAID 401
Cdd:TIGR02639 316 STTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 402 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKSLGDRLKMLVFGQDKAIEALTEAIKMSRAG 481
Cdd:TIGR02639 396 VIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 482 LGHDHKPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 561
Cdd:TIGR02639 476 LGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 562 LLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIhQDNSTDAMEE-IKKIFTPE 640
Cdd:TIGR02639 556 LLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 641 FRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:TIGR02639 635 FRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDE 714
|
730
....*....|....*.
gi 446856817 721 LLFGSLVDGGQVTVAL 736
Cdd:TIGR02639 715 ILFGKLKKGGSVKISL 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-744 |
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: 853.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQTTPVLPASEeerdtQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEglAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSR---LDVVNFISHGTRKDEPsqsssds 154
Cdd:COG0542 81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLealREALEELRGGSRVTSQ------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 155 asqpGSEEQTGGedrMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQ 234
Cdd:COG0542 154 ----NPESKTPA---LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 235 GDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLS 313
Cdd:COG0542 227 GDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 314 SGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDR 393
Cdd:COG0542 306 RGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 394 HLPDKAIDVIDEAGARARLMPVSK-------------------------------------------------------- 417
Cdd:COG0542 386 FLPDKAIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarwea 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 418 ------------------------------------------RKKTVNVADIESVVARIARIPEKSVSQSDRDTLKSLGD 455
Cdd:COG0542 466 ekelieeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 456 RLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFAGPTGVGKTEvtvqLAKAL-----GIE--LLRFDMSEYMER 528
Cdd:COG0542 546 ELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTE----LAKALaeflfGDEdaLIRIDMSEYMEK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 529 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 608
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 609 GVRE-TERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEA 687
Cdd:COG0542 702 GSELiLDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAA 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 446856817 688 RNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTValDKEKNELT 744
Cdd:COG0542 782 KDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITV--DVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
17-740 |
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: 672.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 17 AREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQttpvLPA-SEEERDTQPTLSFQRVLQRAVF 93
Cdd:TIGR03346 16 ALGRDHQQIEPEHLLKALLdqEGGLARPLLQKAGVNVGALRQALEKELER----LPKvSGPGGQVYLSPDLNRLLNLAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 94 HVQSSGRSEVTGANVLVAIfSEQESQAAYLLRKHEVSRLDVVNFIsHGTRKDEpsqsssdSASQPGSEEQtggEDRMENF 173
Cdd:TIGR03346 92 LAQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAI-NAVRGGQ-------KVTDANAEDQ---YEALEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 174 TTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGS 253
Cdd:TIGR03346 160 ARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 254 LLAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIF 332
Cdd:TIGR03346 240 LIAGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHCIGATTLDEYRKYI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 333 EKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPDKAIDVIDEAGARARL 412
Cdd:TIGR03346 319 EKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 413 ----MP-------------------------------------------------------------------------- 414
Cdd:TIGR03346 399 eidsKPeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqqikeeieqvr 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 415 ----VSKR-------------------------------------KKTVNVADIESVVARIARIPEKSVSQSDRDTLKSL 453
Cdd:TIGR03346 479 leleQAERegdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHM 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 454 GDRLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFAGPTGVGKTEvtvqLAKALGIEL-------LRFDMSEYM 526
Cdd:TIGR03346 559 EEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTE----LAKALAEFLfdsedamVRIDMSEYM 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 527 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTT 606
Cdd:TIGR03346 635 EKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTS 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 607 NAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQE 686
Cdd:TIGR03346 715 NLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDA 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 446856817 687 ARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 740
Cdd:TIGR03346 795 ALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-741 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 669.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 1 MLNQELelslnmafarAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQTTPVLpASEeerdT 78
Cdd:CHL00095 14 MLSQEE----------ARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFV-AVE----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVS----RLDVVNFIShgtrkdepsqssSDS 154
Cdd:CHL00095 79 PFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLIG------------EII 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 155 ASQPGSEEQTGGEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQ 234
Cdd:CHL00095 147 EAILGAEQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 235 GDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSS 314
Cdd:CHL00095 227 RDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 315 GKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRH 394
Cdd:CHL00095 306 GELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 395 LPDKAIDVIDEAGARARLM-----------------------------------------------------------PV 415
Cdd:CHL00095 386 LPDKAIDLLDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 416 SKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKSLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFA 495
Cdd:CHL00095 466 RLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 496 GPTGVGKTEVTVQLAKAL-GIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHP 572
Cdd:CHL00095 546 GPTGVGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHP 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 573 DVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAG--VRETERKSIGLIHQDNSTD----------AMEEIKKIFTPE 640
Cdd:CHL00095 626 DIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGskVIETNSGGLGFELSENQLSekqykrlsnlVNEELKQFFRPE 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 641 FRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:CHL00095 706 FLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEE 785
|
810 820
....*....|....*....|.
gi 446856817 721 LLFGSLVDGGQVTVALDKEKN 741
Cdd:CHL00095 786 VLSFKIKPGDIIIVDVNDEKE 806
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-739 |
8.43e-180 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 536.35 E-value: 8.43e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--SAREALEACSVDLVALRQELEAFIEQttpvLPASE-EERDT 78
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEggSVRPLLTSAGINAGQLRTDINQALSR----LPQVEgTGGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFsEQESQAAYLLRKHEVSRLDVVNFISHgTRKDEpsqsssdSASQP 158
Cdd:PRK10865 82 QPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQ-MRGGE-------SVNDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 159 GSEEQtggEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP 238
Cdd:PRK10865 153 GAEDQ---RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 239 EVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKI 317
Cdd:PRK10865 230 EGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 318 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPD 397
Cdd:PRK10865 309 HCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 398 KAIDVIDEAGARARLMPVSK---------------------RKKT----------------------------------- 421
Cdd:PRK10865 389 KAIDLIDEAASSIRMQIDSKpeeldrldrriiqlkleqqalMKESdeaskkrldmlneelsdkerqyseleeewkaekas 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 422 --------------------------------------------------------------VNVADIESVVARIARIPE 439
Cdd:PRK10865 469 lsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIPV 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 440 KSVSQSDRDTLKSLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFAGPTGVGKTEVTVQLAKAL---GIE 516
Cdd:PRK10865 549 SRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDA 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 517 LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKAD 596
Cdd:PRK10865 629 MVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVD 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 597 FRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQ 676
Cdd:PRK10865 709 FRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEE 788
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 677 KGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKE 739
Cdd:PRK10865 789 RGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-722 |
1.28e-178 |
|
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: 532.98 E-value: 1.28e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQttpvLPASEEERdtq 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDK----LPRGNTRT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 80 PTLS--FQRVLQRAvFHVQSS--GRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISH---GTRKDEPSQSSS 152
Cdd:TIGR03345 74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPELRRLLGSISPELAKIDREALREAlpaLVEGSAEASAAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 153 DSASQPGSEEQTGGEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRI 232
Cdd:TIGR03345 153 ADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 233 VQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLIKPL 311
Cdd:TIGR03345 233 AAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLLKPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 312 LSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYIN 391
Cdd:TIGR03345 312 LARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 392 DRHLPDKAIDVIDEAGARARL----------------------------------------------------------- 412
Cdd:TIGR03345 392 GRQLPDKAVSLLDTACARVALsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaalea 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 413 ------------------------MPVSKRKKT------------------------VNVADIESVVARIARIPEKSVSQ 444
Cdd:TIGR03345 472 rwqqekelveailalraeleadadAPADDDDALraqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGRMVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 445 SDRDTLKSLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFAGPTGVGKTEVTVQLAKAL-GIE--LLRFD 521
Cdd:TIGR03345 552 DEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnLITIN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 522 MSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVV 601
Cdd:TIGR03345 632 MSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 602 LVMTTNAGVRETERKSIGLiHQDNSTDAMEE-----IKKIFTPEFRNRLdNIIWFDHLSTDVIHQVVDKFIVELQVQL-D 675
Cdd:TIGR03345 712 ILLTSNAGSDLIMALCADP-ETAPDPEALLEalrpeLLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLkE 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 446856817 676 QKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 722
Cdd:TIGR03345 790 NHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
450-651 |
1.04e-85 |
|
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: 268.66 E-value: 1.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 450 LKSLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHDHKPVGSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYM 526
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 527 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTT 606
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446856817 607 NAgvreterksiglihqdnstdameeikkiFTPEFRNRLDNIIWF 651
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
487-648 |
8.32e-77 |
|
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: 244.80 E-value: 8.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 487 KPVGSFLFAGPTGVGKTEVTVQLAKALGI---ELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLL 563
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 564 LDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNST---DAMEEIKKIFTPE 640
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160
|
....*...
gi 446856817 641 FRNRLDNI 648
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
351-453 |
3.92e-37 |
|
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: 134.15 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 351 SIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPDKAIDVIDEAGARARLmpvSKRKKTVNVADIESV 430
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
|
90 100
....*....|....*....|...
gi 446856817 431 VARIARIPEKSVSQSDRDTLKSL 453
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERL 100
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
654-734 |
9.30e-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, 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: 109.80 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 654 LSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 733
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 446856817 734 V 734
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, ... |
654-743 |
3.94e-27 |
|
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: 105.22 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 654 LSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 733
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 446856817 734 VALDKEKNEL 743
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
190-345 |
8.02e-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: 92.59 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 190 IGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPevmadctIYSLDIGSLLAGTKYRGDFE-KRF 268
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446856817 269 KALLKQLEQDTNSILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSSGKIRVIGSTTYqefSNIFEKDRALARRFQKI 345
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNR---PLLGDLDRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
212-345 |
3.04e-16 |
|
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: 75.71 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWrivqgdvpevMADCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK----------ELGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446856817 292 IGAGAASGGQV--DAANLIKPLL-----SSGKIRVIGSTTYqefsnIFEKDRALARRFQKI 345
Cdd:pfam00004 70 AGSRGSGGDSEsrRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
17-388 |
3.74e-16 |
|
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: 81.11 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 17 AREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQ 96
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 97 SSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSSDSASQPGSEEQTGGEDRMEnfttn 176
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 177 lnqLARVGGIDPLIGREKELERAIQVLCRRRKNNP-------LLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiYSL 249
Cdd:COG0464 156 ---LDDLGGLEEVKEELRELVALPLKRPELREEYGlppprglLLYGPPGTGKTLLARALA-GELGLPL---------IEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 250 DIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDA----------ANLIKPLLssgkirV 319
Cdd:COG0464 223 DLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvntlltemEELRSDVV------V 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 320 IGsTTYQeFSNIfekDRALARRFQ-KIDITEPSIDETVQIINGLKPKYEAHHDV----------RYTAKAIRAAVELAVK 388
Cdd:COG0464 295 IA-ATNR-PDLL---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVdleelaeateGLSGADIRNVVRRAAL 369
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
462-618 |
2.57e-13 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 67.94 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 462 FGQDKAIEALTEAIKmsraglghdHKPVGSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYMERHTVSRLIgap 538
Cdd:cd00009 1 VGQEEAIEALREALE---------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 539 pgyvGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGtltdnNGRKADFRNVVLVMTTNAGVRETERKSI 618
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
491-607 |
4.80e-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: 66.93 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 491 SFLFAGPTGVGKTEVTVQLAKAL-GIELLRFDMSEYMerhTVSRLIGappGYVGFDQGGLLTDAVI----KHPHaVLLLD 565
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDT---TEEDLFG---RRNIDPGGASWVDGPLvraaREGE-IAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446856817 566 EIEKAHPDVFNILLQVMDNGTLTDNNGR---KADFRNVVLVMTTN 607
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
207-345 |
3.76e-12 |
|
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: 64.70 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 207 RKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLL-----AGTKYRGDFEKRFKALLKQLEQDTNS 281
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446856817 282 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSSGKIRVIGSTTYQEFSnifeKDRALARRFQKI 345
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTNDEKDL----GPALLRRRFDRR 141
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
1.49e-11 |
|
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: 59.84 E-value: 1.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446856817 13 AFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIE 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDglAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
212-345 |
2.63e-10 |
|
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: 59.60 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 292 IGAGAASGGQVDAA-------NLIKPLLSSGKIRVIGSTtyqefSNIFEKDRALAR--RFQKI 345
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT-----NRPDLLDPALLRpgRFDEV 155
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
467-607 |
6.80e-10 |
|
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: 58.45 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 467 AIEALTEAIKMSRAGLGhdhkPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTvsrligappGYVGfDQ 546
Cdd:cd19481 8 AVEAPRRGSRLRRYGLG----LPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE-KN 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 547 GGLLTDAVIKHPHAVLLLDEIEKAHPD------------VFNILLQVMDNGTLTDnngrkadfrNVVLVMTTN 607
Cdd:cd19481 74 LRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
187-405 |
1.25e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 59.51 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 187 DPLIGRE---KELERAIQVLCRRRK---------NNPLLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSL 254
Cdd:COG1223 2 DDVVGQEeakKKLKLIIKELRRRENlrkfglwppRKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 255 LagTKYRGDFEKRFKALLKQLEQdTNSILFIDEIHTIigagaasGGQVDAANL---IKPLLSS---------GKIRVIGS 322
Cdd:COG1223 72 I--GSYLGETARNLRKLFDFARR-APCVIFFDEFDAI-------AKDRGDQNDvgeVKRVVNAllqeldglpSGSVVIAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 323 TTYQEFSnifekDRALARRFQ-KIDITEPSIDETVQI----INGLKPKYEAHHD--------------VRYTAKAIRAAV 383
Cdd:COG1223 142 TNHPELL-----DSALWRRFDeVIEFPLPDKEERKEIlelnLKKFPLPFELDLKklakkleglsgadiEKVLKTALKKAI 216
|
250 260
....*....|....*....|..
gi 446856817 384 ELAVKYINDRHLpDKAIDVIDE 405
Cdd:COG1223 217 LEDREKVTKEDL-EEALKQRKE 237
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
493-652 |
2.25e-09 |
|
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: 56.06 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 493 LFAGPTGVGKTEVTVQLAKALGIELLRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTDAVIKHPHaVLLLDEIEKAHP 572
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAPC-VIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 573 -----------DVFNILLQVMDngtltdnnGRKADFRNVVLVMTTNagvreterkSIGLIhqdnstdameeikkifTPEF 641
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN---------RPDKL----------------DPAL 118
|
170
....*....|.
gi 446856817 642 RNRLDNIIWFD 652
Cdd:pfam00004 119 LGRFDRIIEFP 129
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
493-607 |
4.73e-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: 52.76 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 493 LFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGG----LLTDAVIKHPHAVLLLD 565
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446856817 566 EIEKAHPDVFNILLQVMDNGTLTDNNGRKadfRNVVLVMTTN 607
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTN 124
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
212-441 |
6.42e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 55.01 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 292 IGA--GAASGGQVDaaNLIKPLL-------SSGKIRVIGSTTYQEfsnifEKDRALAR--RF-QKIDITEPSIDETVQII 359
Cdd:COG1222 184 AARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 360 NGLKPKYEAHHDVRYTAKAIRA----AVELAVkyindrhlpdkaidVIDEAGARArlmpVSKRKKTVNVADIESVVARIA 435
Cdd:COG1222 257 KIHLRDMPLADDVDLDKLAKLTegfsGADLKA--------------IVTEAGMFA----IREGRDTVTMEDLEKAIEKVK 318
|
....*.
gi 446856817 436 RIPEKS 441
Cdd:COG1222 319 KKTETA 324
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
212-344 |
8.09e-08 |
|
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: 52.35 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 292 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 344
Cdd:cd19509 104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
212-344 |
1.00e-07 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain] Cd Length: 170 Bit Score: 52.56 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 292 igAGAASGGQVDAANLIKPLL---------SSGKIRVIGSTtyqefsNI-FEKDRALARRFQK 344
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
212-516 |
2.69e-07 |
|
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: 54.14 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRI----VQGDVPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFIDE 287
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAgayfISINGPEIM----------------SKYYGESEERLREIFKEAEENAPSIIFIDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 288 IHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTTYQEfsnifEKDRALAR--RFQK-IDITEPSIDETVQI 358
Cdd:TIGR01243 280 IDAIAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 359 INGLKPKYEAHHDVR----------YTAKAIRAAVELAVKYINDRHLPDKAIDVIDEAGARARL--MPVSKRKKTVNVAD 426
Cdd:TIGR01243 355 LKVHTRNMPLAEDVDldklaevthgFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 427 IESVVARIARIPEKSVSQSDRDTLKSLGDRLKMLVFGQDKAIEALteaikmSRAGLghdHKPVGSFLFaGPTGVGKTevt 506
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF------EKMGI---RPPKGVLLF-GPPGTGKT--- 501
|
330
....*....|
gi 446856817 507 vQLAKALGIE 516
Cdd:TIGR01243 502 -LLAKAVATE 510
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
335-683 |
3.03e-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: 53.38 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 335 DRALARRFQKIDITEPSIDETVQIINGLKPKYEAHHDVRYTAKAIRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMP 414
Cdd:COG0464 29 LLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 415 VSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKSLGDRLKMLVF----GQDKAIEALTEAIK--------MSRAGL 482
Cdd:COG0464 109 LLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlgGLEEVKEELRELVAlplkrpelREEYGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 483 ghdhKPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEymerhtvsrLIGappGYVG---------FDQgglltda 553
Cdd:COG0464 189 ----PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVGeteknlrevFDK------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 554 VIKHPHAVLLLDEIEKAHPD-----------VFNILLQVMDNGTltdnngrkadfRNVVLVMTTNagvreterksigliH 622
Cdd:COG0464 246 ARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN--------------R 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446856817 623 QDNStDameeikkiftPEFRNRLDNIIWFDHLSTDVIHQVvdkfiveLQVQLDQKGVSLEV 683
Cdd:COG0464 301 PDLL-D----------PALLRRFDEIIFFPLPDAEERLEI-------FRIHLRKRPLDEDV 343
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
205-344 |
5.67e-06 |
|
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: 47.29 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 205 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 284
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 285 IDEIHTIIGAgAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNI----------FEKDRALARRFQK 344
Cdd:cd19522 98 IDEIDSICSR-RGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLEK 166
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
461-513 |
5.80e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 49.03 E-value: 5.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446856817 461 VFGQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR--LAH------AYLFTGPRGVGKTTLARILAKAL 56
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
493-607 |
9.63e-06 |
|
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: 46.78 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 493 LFAGPTGVGKTEVTVQLAKALGIELLRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTDAVIKHPhaVLLLD 565
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446856817 566 EIEK----AHPDVFNILLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 607
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
183-323 |
2.19e-05 |
|
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: 45.36 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 183 VGGIDPLIGREKEL----------ERAIQVLCRRrknNPLLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIG 252
Cdd:cd19503 2 IGGLDEQIASLKELielplkypelFRALGLKPPR---GVLLHGPPGTGKTLLARAVANE----------AGANFLSISGP 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446856817 253 SLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGST 323
Cdd:cd19503 69 SIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
188-247 |
3.32e-05 |
|
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: 44.80 E-value: 3.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 188 PLIGREKELERAIQVLCRRRKNNP---LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIY 247
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEN 63
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
212-346 |
4.64e-05 |
|
first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain] Cd Length: 166 Bit Score: 44.35 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLA------WRIVQGdvPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFI 285
Cdd:cd19519 38 LLYGPPGTGKTLIARAVAnetgafFFLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446856817 286 DEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTtyqefSNIFEKDRALaRRFQKID 346
Cdd:cd19519 100 DEIDAIAPKREKTHGEVERRivsqllTLMDGLKQRAHVIVMAAT-----NRPNSIDPAL-RRFGRFD 160
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
208-291 |
9.17e-05 |
|
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: 44.90 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 208 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTiysldigSLL-AGtkYRG-DFEKRFKALLK----QLEQDTNS 281
Cdd:cd19497 50 KSNILLIGPTGSGKTLLAQTLA-KIL--DVPFAIADAT-------TLTeAG--YVGeDVENILLKLLQaadyDVERAQRG 117
|
90
....*....|
gi 446856817 282 ILFIDEIHTI 291
Cdd:cd19497 118 IVYIDEIDKI 127
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
212-300 |
1.47e-04 |
|
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: 42.74 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLA--WRIvqgdvpevmadcTIYSLDIGSLLAGtkYRGDFEKRFKALLKQLEQDTNSILFIDEIH 289
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAgvWQL------------PLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
|
90
....*....|.
gi 446856817 290 TIIGaGAASGG 300
Cdd:cd19507 101 KGFS-NADSKG 110
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
463-513 |
2.73e-04 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 42.20 E-value: 2.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446856817 463 GQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:pfam13177 1 GQPEAIQLLQNSLENGR--LSH------AYLFSGPEGVGKLELALAFAKAL 43
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
212-344 |
4.19e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. 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: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.90 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 292 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTTYQEfsnifEKDRALARRFQK 344
Cdd:cd19525 127 L--SQRGEGEHESSRRIKTEFlvqldgattsSEDRILVVGATNRPQ-----EIDEAARRRLVK 182
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
493-569 |
4.84e-04 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 41.60 E-value: 4.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446856817 493 LFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGLLTDAVikhpHAVLLLDEIEK 569
Cdd:cd19498 50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
189-324 |
5.48e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.15 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 189 LIGREKELERAIQvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDigSLLAGTKyrgDFEKRF 268
Cdd:PRK13342 20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTLARIIA----------GATDAPFEALS--AVTSGVK---DLREVI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446856817 269 KALLKQLEQDTNSILFIDEIHTIigagaaSGGQVDAanLIkPLLSSGKIRVIGSTT 324
Cdd:PRK13342 82 EEARQRRSAGRRTILFIDEIHRF------NKAQQDA--LL-PHVEDGTITLIGATT 128
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
5-237 |
5.90e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 5 ELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSF 84
Cdd:COG3899 105 LLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 85 QRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSSDSASQPGSEEQT 164
Cdd:COG3899 185 AALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAAL 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446856817 165 GGEDRMENFTTNLNQLARVGGIDPLIGREKELERAIQVL--CRRRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDV 237
Cdd:COG3899 265 LLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALerARAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
183-312 |
1.16e-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: 40.83 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 183 VGGIDPLIGREKELERAIQVLCRRR---------------KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTIY 247
Cdd:cd19498 6 VSELDKYIIGQDEAKRAVAIALRNRwrrmqlpeelrdevtPKNILMIGPTGVGKTEIARRLA-KLA--GAPFIKVEATKF 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446856817 248 SlDIGsllagtkYRG-DFEKRFKALlkqleqdTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLL 312
Cdd:cd19498 83 T-EVG-------YVGrDVESIIRDL-------VEGIVFIDEIDKIAKRGGSSGPDVSREGVQRDLL 133
|
|
| PRK14969 |
PRK14969 |
DNA polymerase III subunits gamma and tau; Provisional |
463-516 |
1.20e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237873 [Multi-domain] Cd Length: 527 Bit Score: 42.04 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446856817 463 GQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKALGIE 516
Cdd:PRK14969 20 GQEHVVRALTNALEQQR--LHH------AYLFTGTRGVGKTTLARILAKSLNCE 65
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
185-341 |
1.36e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 41.96 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 185 GIDPLIGREKELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiysLDIGSLLAGTKyrgDF 264
Cdd:PRK13341 32 GQDHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446856817 265 EKRFKALLKQLEQ-DTNSILFIDEIHTIIGAgaasggQVDAanlIKPLLSSGKIRVIGSTTYQEFsniFEKDRALARR 341
Cdd:PRK13341 94 RAEVDRAKERLERhGKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
208-245 |
1.56e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 41.68 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446856817 208 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCT 245
Cdd:PRK05342 108 KSNILLIGPTGSGKTLLAQTLA-RIL--DVPFAIADAT 142
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
212-344 |
1.58e-03 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain] Cd Length: 164 Bit Score: 39.83 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVA------------AESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446856817 292 IgaGAASGGQVDAANLIKP--------LLSSG--KIRVIGSTTYQEfsnifEKDRALARRFQK 344
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGddRVLVMGATNRPQ-----ELDDAVLRRFTK 160
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
182-288 |
1.90e-03 |
|
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: 39.85 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 182 RVGGIDPLIgreKELERAIQvLCR---RRKNNP----LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYS-LDIGS 253
Cdd:cd19499 12 RVVGQDEAV---KAVSDAIR-RARaglSDPNRPigsfLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMeKHSVS 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 446856817 254 LLAGT--KYRGdFEKRFKaLLKQLEQDTNSILFIDEI 288
Cdd:cd19499 88 RLIGAppGYVG-YTEGGQ-LTEAVRRKPYSVVLLDEI 122
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
463-513 |
2.56e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446856817 463 GQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:PRK12323 20 GQEHVVRALTHALEQQR--LHH------AYLFTGTRGVGKTTLSRILAKSL 62
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
205-289 |
2.93e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 205 RRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP----EVMADCTIYSLdIGSLLAGTKYRGDFEKRFKALLKQLEQ--- 277
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDL-LRALLRALGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 446856817 278 --DTNSILFIDEIH 289
Cdd:pfam13401 81 alAVAVVLIIDEAQ 94
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
212-344 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446856817 292 IGAGAASGGQVDAA------NLIKPLLSSGKIRVI--GSTtyqefSNIFEKDRALARRFQK 344
Cdd:cd19520 107 LRQRSSTDHEATAMmkaefmSLWDGLSTDGNCRVIvmGAT-----NRPQDLDEAILRRMPK 162
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
490-586 |
4.51e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 490 GSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYME----RHTVSRLIGAPPgyVGFDQGGLLTDAVIKH----- 557
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
|
90 100
....*....|....*....|....*....
gi 446856817 558 PHAVLLLDEIEKAHPDVFNILLQVMDNGT 586
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
187-411 |
6.54e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 39.54 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 187 DPLIGREKELE---RAIQVLCR-RRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVPE-------VMADCTIYS------L 249
Cdd:TIGR02928 15 DRIVHRDEQIEelaKALRPILRgSRPSNVFIYGKTGTGKTAVTKYVM-KELEEAAEDrdvrvvtVYVNCQILDtlyqvlV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 250 DIGSLLAGTK----YRG-DFEKRFKALLKQLEQDTNSILFI-DEIHTIIGAG---------AASGGQVDAAnlikpllss 314
Cdd:TIGR02928 94 ELANQLRGSGeevpTTGlSTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDddllyqlsrARSNGDLDNA--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 315 gKIRVIGSTTYQEF-SNIFEKDRAlarRFQKIDITEPSIDETvQIINGLKPKYE-AHHDVRYTAKAIRAAVELAVKYIND 392
Cdd:TIGR02928 165 -KVGVIGISNDLKFrENLDPRVKS---SLCEEEIIFPPYDAE-ELRDILENRAEkAFYDGVLDDGVIPLCAALAAQEHGD 239
|
250 260
....*....|....*....|
gi 446856817 393 -RhlpdKAIDVIDEAGARAR 411
Cdd:TIGR02928 240 aR----KAIDLLRVAGEIAE 255
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
461-513 |
6.60e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 39.81 E-value: 6.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446856817 461 VFGQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:PRK14953 18 VIGQEIVVRILKNAVKLQR--VSH------AYIFAGPRGTGKTTIARILAKVL 62
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
463-516 |
6.89e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 39.72 E-value: 6.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446856817 463 GQDKAIEALTEAIKMSRagLGHdhkpvgSFLFAGPTGVGKTEVTVQLAKALGIE 516
Cdd:PRK14965 20 GQEHVSRTLQNAIDTGR--VAH------AFLFTGARGVGKTSTARILAKALNCE 65
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
195-345 |
7.35e-03 |
|
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.
Pssm-ID: 428547 Cd Length: 189 Bit Score: 38.34 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 195 ELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWR---IVQGD---VPEVMADC-------TIYSLDIGSLLAGTKYR 261
Cdd:pfam05621 22 RLEDLLDYPKRLRMPNLLLVGDSNNGKTMIVERFARLhppTDDEDaeiVPVVVVQMppkpdekRLYVAILEALGAPFRPR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 262 GDFEKRFKALLKQLEQDTNSILFIDEIHTIIgAGAASgGQVDAANLIKPLLSSGKIRVIGSTTyQEFSNIFEKDRALARR 341
Cdd:pfam05621 102 DRLSKLEQQVLRLLRAVGVRMLIIDEFHNLL-AGSAR-KQREFLNVLKSLGNELRIPIVGVGT-REAVRAIRTDPQLASR 178
|
....
gi 446856817 342 FQKI 345
Cdd:pfam05621 179 FEPI 182
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
461-513 |
8.68e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 39.11 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446856817 461 VFGQDKAIEALTEAIKMSRAGLGhdhkpvgsFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:PRK07399 6 LIGQPLAIELLTAAIKQNRIAPA--------YLFAGPEGVGRKLAALCFIEGL 50
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
212-291 |
9.02e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-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: 410926 [Multi-domain] Cd Length: 169 Bit Score: 37.77 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446856817 212 LLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSLLAGTKyrGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
|
| |
