|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-812 |
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: 1261.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 1 MDELFTESAKAVLAIAQEEAKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIEHLSGYGTMQSPMGNNn 80
Cdd:COG0542 2 NFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 81 lyLPYSPRAKQIFAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLKKMGvsepnsaqrRRN 160
Cdd:COG0542 81 --PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRG---------GSR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 161 GQSKNAPQGTPTLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREV 240
Cdd:COG0542 150 VTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 241 PEDMQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQ-DGQVILFIDELHTLIGAGGAEGAIDASNILKPALARGEL 319
Cdd:COG0542 230 PESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 320 QTIGATTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPD 399
Cdd:COG0542 310 RCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 400 KAIDLMDESAAKVRLDKADQPSEINELRTEISQLITEKEEAIQNQ---SFESAARIRQKEKQVMEKLEEL---------- 466
Cdd:COG0542 390 KAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQdeaSFERLAELRDELAELEEELEALkarweaekel 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 467 ----IAVKEKSLSGY------------------------STQVTEEDVAGVVSQWTGVPLQQLEKKESERLMELETILHQ 518
Cdd:COG0542 470 ieeiQELKEELEQRYgkipelekelaeleeelaelapllREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 519 RVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIG 598
Cdd:COG0542 550 RVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIG 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 599 SPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTDAKGRKVDFRNTILIMTSNLGATAIREE 678
Cdd:COG0542 630 APPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDL 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 679 khvgfnvKDISKNHELMQKRIMEELKKAFRPEFLNRIDETVVFHSLKQEEIHEIVKIMSQSVVKRMAEQEVKVKITPAAI 758
Cdd:COG0542 710 -------AEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAK 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 488287731 759 EVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVTLGASKGKIT 812
Cdd:COG0542 783 DFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-802 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 983.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 1 MDELFTESAKAVLAIAQEEAKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIEHLSGYGTmqspmGNNN 80
Cdd:CHL00095 1 MFERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGT-----GFVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 81 LYLPYSPRAKQIFAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLKKMGvsEPNSAQRRRN 160
Cdd:CHL00095 76 VEIPFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIG--EIIEAILGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 161 GQSknapQGTPTLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREV 240
Cdd:CHL00095 154 QSR----SKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 241 PEDMQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLIGAGGAEGAIDASNILKPALARGELQ 320
Cdd:CHL00095 230 PDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 321 TIGATTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDK 400
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 401 AIDLMDESAAKVRLDKADQPSEINELRTEISQLITEKEEAIQNQSFESAARIRQKEKQVMEKLEELIAVK--EKSLSGYS 478
Cdd:CHL00095 390 AIDLLDEAGSRVRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIIQSKktEEEKRLEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 479 TQVTEEDVAGVVSQWTGVPLQQLEKKESERLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTG 558
Cdd:CHL00095 470 PVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTG 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 559 VGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFN 638
Cdd:CHL00095 550 VGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFN 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 639 ILLQVLDDGHLTDAKGRKVDFRNTILIMTSNLGATAI-REEKHVGFN---VKDISKNHELMQKRIMEELKKAFRPEFLNR 714
Cdd:CHL00095 630 LLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIeTNSGGLGFElseNQLSEKQYKRLSNLVNEELKQFFRPEFLNR 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 715 IDETVVFHSLKQEEIHEIVKIMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSG 794
Cdd:CHL00095 710 LDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSF 789
|
....*...
gi 488287731 795 QIQLGDKV 802
Cdd:CHL00095 790 KIKPGDII 797
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
5-812 |
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: 976.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 5 FTESAKAVLAIAQEEAKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIE-HLSGYGTMQSPMGNNNLyl 83
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEkELERLPKVSGPGGQVYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 84 pySPRAKQIFAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILAsRILVNLGLSLSKMRQLLlkkmgvsepNSAQRRRNGQS 163
Cdd:TIGR03346 79 --SPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLG-KLLKEAGATADALEAAI---------NAVRGGQKVTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 164 KNAPQGTPTLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPED 243
Cdd:TIGR03346 147 ANAEDQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 244 MQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIY-QDGQVILFIDELHTLIGAGGAEGAIDASNILKPALARGELQTI 322
Cdd:TIGR03346 227 LKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 323 GATTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDKAI 402
Cdd:TIGR03346 307 GATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 403 DLMDESAAKVRLDKADQPSEINELRTEISQLITEK------------------EEAIQNQSFESAA--RIRQKEKQVMEK 462
Cdd:TIGR03346 387 DLIDEAAARIRMEIDSKPEELDELDRRIIQLEIERealkkekdeaskkrledlEKELADLEEEYAEleEQWKAEKASIQG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 463 L----EELIAVK--------------------------EKSLSGYS------------TQVTEEDVAGVVSQWTGVPLQQ 500
Cdd:TIGR03346 467 IqqikEEIEQVRleleqaeregdlakaaelqygklpelEKQLQAAEqklgeeqnrllrEEVTAEEIAEVVSRWTGIPVSK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 501 LEKKESERLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALI 580
Cdd:TIGR03346 547 MLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMV 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 581 RVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTDAKGRKVDFR 660
Cdd:TIGR03346 627 RIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFR 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 661 NTILIMTSNLGATAIREEKhvgfnvkdISKNHELMQKRIMEELKKAFRPEFLNRIDETVVFHSLKQEEIHEIVKIMSQSV 740
Cdd:TIGR03346 707 NTVIIMTSNLGSDFIQELA--------GGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRL 778
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488287731 741 VKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVTLGASKGKIT 812
Cdd:TIGR03346 779 RKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
5-812 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 747.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 5 FTESAKAVLAIAQEEAKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIEHlsGYGTMQSPMGNNNLYLP 84
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQ--ALSRLPQVEGTGGDVQP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 85 ySPRAKQIFAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILASrilvnlglslskmrqlLLKKMGVSEPN---SAQRRRNG 161
Cdd:PRK10865 84 -SQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLAD----------------ILKAAGATTANitqAIEQMRGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 162 QSKN---APQGTPTLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNR 238
Cdd:PRK10865 147 ESVNdqgAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIING 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 239 EVPEDMQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIY-QDGQVILFIDELHTLIGAGGAEGAIDASNILKPALARG 317
Cdd:PRK10865 227 EVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAkQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 318 ELQTIGATTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQL 397
Cdd:PRK10865 307 ELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 398 PDKAIDLMDESAAKVRLDKADQPSEINELRTEISQLITEkEEAIQNQSFESA--------ARIRQKEKQVMEkLEELIAV 469
Cdd:PRK10865 387 PDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLE-QQALMKESDEASkkrldmlnEELSDKERQYSE-LEEEWKA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 470 KEKSLSGYST-------------------------------------------------------QVTEEDVAGVVSQWT 494
Cdd:PRK10865 465 EKASLSGTQTikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnKVTDAEIAEVLARWT 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 495 GVPLQQLEKKESERLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAMFG 574
Cdd:PRK10865 545 GIPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFD 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 575 SEEALIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTDAKG 654
Cdd:PRK10865 625 SDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 655 RKVDFRNTILIMTSNLGATAIREekHVGfnvkdiSKNHELMQKRIMEELKKAFRPEFLNRIDETVVFHSLKQEEIHEIVK 734
Cdd:PRK10865 705 RTVDFRNTVVIMTSNLGSDLIQE--RFG------ELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQ 776
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488287731 735 IMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVTLGASKGKIT 812
Cdd:PRK10865 777 IQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIV 854
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
5-806 |
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: 722.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 5 FTESAKAVLAIAQEEAKYFRHQSVGSEHLLLALVLEPNGIAgkTLRQLNTDTEDIREEIEHLSGYGTMQSPMGNNnlYLP 84
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENLPVIPEDID--EEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 85 -YSPRAKQIFAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLKKMGvSEPNSAQRRRNGQS 163
Cdd:TIGR02639 77 eQTVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGIS-KDDGKDQLGEEAGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 164 KNAPQGTPtLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPED 243
Cdd:TIGR02639 156 EEEKGQDA-LEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 244 MQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLIGAG-GAEGAIDASNILKPALARGELQTI 322
Cdd:TIGR02639 235 LKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGaTSGGSMDASNLLKPALSSGKIRCI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 323 GATTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDKAI 402
Cdd:TIGR02639 315 GSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 403 DLMDESAAKVRLDKADQPSEInelrteisqlitekeeaiqnqsfesaarirqkekqvmekleeliavkekslsgystqVT 482
Cdd:TIGR02639 395 DVIDEAGAAFRLRPKAKKKAN---------------------------------------------------------VN 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 483 EEDVAGVVSQWTGVPLQQLEKKESERLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKT 562
Cdd:TIGR02639 418 VKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKT 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 563 ELAKALAEAMfGSEeaLIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQ 642
Cdd:TIGR02639 498 ELAKQLAEEL-GVH--LLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQ 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 643 VLDDGHLTDAKGRKVDFRNTILIMTSNLGATAIREEKhVGFnvkdISKNHElmqKRIMEELKKAFRPEFLNRIDETVVFH 722
Cdd:TIGR02639 575 VMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPP-IGF----GGENRE---SKSLKAIKKLFSPEFRNRLDAIIHFN 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 723 SLKQEEIHEIVKIMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKV 802
Cdd:TIGR02639 647 DLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSV 726
|
....
gi 488287731 803 TLGA 806
Cdd:TIGR02639 727 KISL 730
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
20-793 |
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: 692.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 20 AKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIEH-LSGYgtmqsPMGNNNlYLPYSP------RAKQI 92
Cdd:TIGR03345 16 CVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARaLDKL-----PRGNTR-TPVFSPhlvellQEAWL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 93 FAYAgdeakRLGAQKIGTEHLLLGLLRDEEIlaSRILVNLGLSLSKMRQLLLKKM------GVSEPNSAQRRRNG-QSKN 165
Cdd:TIGR03345 90 LASL-----ELGDGRIRSGHLLLALLTDPEL--RRLLGSISPELAKIDREALREAlpalveGSAEASAAAADAAPaGAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 166 APQGTPTLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPEDMQ 245
Cdd:TIGR03345 163 GAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 246 GKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQ-VILFIDELHTLIGAGGAEGAIDASNILKPALARGELQTIGA 324
Cdd:TIGR03345 243 NVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 325 TTLDEYQKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDKAIDL 404
Cdd:TIGR03345 323 TTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 405 MDESAAKVRLDKADQPSEINELRTEISQL-----------------------ITEKEEAIQNQSFESAARIrQKEKQVME 461
Cdd:TIGR03345 403 LDTACARVALSQNATPAALEDLRRRIAALeleldalereaalgadhderlaeLRAELAALEAELAALEARW-QQEKELVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 462 KLEEL---------------------IAVKEKSLSGY-------STQVTEEDVAGVVSQWTGVPLQQLEKKESERLMELE 513
Cdd:TIGR03345 482 AILALraeleadadapaddddalraqLAELEAALASAqgeeplvFPEVDAQAVAEVVADWTGIPVGRMVRDEIEAVLSLP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 514 TILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYST 593
Cdd:TIGR03345 562 DRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQEAHTV 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 594 SRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTDAKGRKVDFRNTILIMTSNLGAT 673
Cdd:TIGR03345 642 SRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNAGSD 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 674 AIREEkhvgFNVKDISKNHELMQKRIMEELKKAFRPEFLNRIdeTVV-FHSLKQEEIHEIVKIMSQSVVKRMAEQ-EVKV 751
Cdd:TIGR03345 722 LIMAL----CADPETAPDPEALLEALRPELLKVFKPAFLGRM--TVIpYLPLDDDVLAAIVRLKLDRIARRLKENhGAEL 795
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 488287731 752 KITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLS 793
Cdd:TIGR03345 796 VYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
13-825 |
5.57e-180 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 535.96 E-value: 5.57e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 13 LAIAQEEAKYFRHQSVGSEHLLLALVLEPNgiAGKTLRQLNTDTEDIREEIEHLSGYGTMQSPMGNNNLYLPYSPRAKQI 92
Cdd:PRK11034 10 LNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 93 FAYAGDEAKRLGAQKIGTEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLKKMGVSEP-NSAQRRRNGQSKNAPQGTP 171
Cdd:PRK11034 88 LQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPsQSSDPGSQPNSEEQAGGEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 172 TLDSLARDLTKLAREQSLDPVVGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPEDMQGKRLMM 251
Cdd:PRK11034 168 RMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 252 LDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLIGAGGAEGA-IDASNILKPALARGELQTIGATTLDEY 330
Cdd:PRK11034 248 LDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 331 QKYIEKDAALERRFARIQVAEPTPEEAEEILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDKAIDLMDESAA 410
Cdd:PRK11034 328 SNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 411 KVRLDKADQpseinelrteisqlitekeeaiqnqsfesaariRQKEKQVmekleeliavkekslsgystqvteEDVAGVV 490
Cdd:PRK11034 408 RARLMPVSK---------------------------------RKKTVNV------------------------ADIESVV 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 491 SQWTGVPLQQLEKKESERLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAE 570
Cdd:PRK11034 431 ARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSK 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 571 AMfGSEeaLIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLT 650
Cdd:PRK11034 511 AL-GIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 651 DAKGRKVDFRNTILIMTSNLGaTAIREEKHVGFNVKDISKNhelmqkrIMEELKKAFRPEFLNRIDETVVFHSLKQEEIH 730
Cdd:PRK11034 588 DNNGRKADFRNVVLVMTTNAG-VRETERKSIGLIHQDNSTD-------AMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIH 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 731 EIVKIMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVTLGASKGK 810
Cdd:PRK11034 660 QVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
|
810
....*....|....*
gi 488287731 811 ITLNVRAPKAPKTEA 825
Cdd:PRK11034 740 NELTYGFQSAQKHKA 754
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
508-721 |
7.87e-105 |
|
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: 320.28 E-value: 7.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 508 RLMELETILHQRVVGQNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEF 587
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 588 MEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTDAKGRKVDFRNTILIMT 667
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488287731 668 SNlgataireekhvgfnvkdisknhelmqkrimeelkkAFRPEFLNRIDETVVF 721
Cdd:cd19499 161 SN------------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
546-718 |
5.96e-92 |
|
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: 286.01 E-value: 5.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 546 RPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQLTEKIRQRPYSVIL 625
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 626 LDEVEKAHPDVFNILLQVLDDGHLTDAKGRKVDFRNTILIMTSNLGATAIREEKHVGfnvkdISKNHELMQKRIMEELKK 705
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLG-----DSPDYELLKEEVMDLLKK 155
|
170
....*....|...
gi 488287731 706 AFRPEFLNRIDET 718
Cdd:pfam07724 156 GFIPEFLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
360-456 |
7.06e-42 |
|
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: 148.02 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 360 ILKGLRSRYEKHHGVEITDEALHAAVQLSIRYLNDRQLPDKAIDLMDESAAKVRLDKADQPSEINELRTEISQLITEKEE 439
Cdd:pfam17871 8 ILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAKLEIEKEA 87
|
90
....*....|....*..
gi 488287731 440 AIQNQSFESAARIRQKE 456
Cdd:pfam17871 88 LEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
724-804 |
3.36e-26 |
|
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: 102.48 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 724 LKQEEIHEIVKIMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVT 803
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 488287731 804 L 804
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, ... |
724-813 |
3.25e-25 |
|
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: 100.21 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 724 LKQEEIHEIVKIMSQSVVKRMAEQEVKVKITPAAIEVIGKVGFDPEYGARPIRRALQKEVEDRLSEALLSGQIQLGDKVT 803
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 488287731 804 LGASKGKITL 813
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
521-669 |
7.30e-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: 84.12 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 521 VGQNEAVEAVSRAIRRarsglkdpaRPIGSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIgsp 600
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488287731 601 pgyvGYEEGGQLTEKIRQRPYSVILLDEVEKAHPDVFNILLQVLDDGHLTdakgrKVDFRNTILIMTSN 669
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
193-347 |
5.83e-18 |
|
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: 81.42 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 193 VGRGTEVRRLIQILSRRTKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPedmqgkrLMMLDMGALVAGTKYRGEFEDRLK 272
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488287731 273 KVVDEIYQDGQV-ILFIDELHTLiGAGGAEGAIDASNILKPALA-RGELQTIGATTLDEyqkYIEKDAALERRFARI 347
Cdd:cd00009 74 RLLFELAEKAKPgVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPL---LGDLDRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
216-348 |
2.73e-15 |
|
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: 73.01 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 216 LVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDMGALVAgtKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLI 295
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488287731 296 GAGGAEG---AIDASNILKPALARGELQT-----IGATTldeyqkYIEK-DAALERRFARIQ 348
Cdd:pfam00004 71 GSRGSGGdseSRRVVNQLLTELDGFTSSNskvivIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
550-669 |
1.37e-14 |
|
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: 71.17 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 550 SFMFLGPTGVGKTELAKALAEAMFGSEeaLIRVDMSEFMekySTSRLIGsppgyvGYEEGGQLTEKIRQ------RPYSV 623
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRP--VFYVQLTRDT---TEEDLFG------RRNIDPGGASWVDGplvraaREGEI 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488287731 624 ILLDEVEKAHPDVFNILLQVLDDGHLTDAKGR---KVDFRNTILIMTSN 669
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
552-676 |
6.20e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 69.71 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 552 MFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIGSPPGYVGYEEGGQ----LTEKIRQRPYSVILLD 627
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488287731 628 EVEKAHPDVFNILLQVLDDGHLtdaKGRKVDFRNTILIMTSNLGATAIR 676
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRL---LLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
525-670 |
3.73e-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: 62.30 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 525 EAVEAVSRAIRRARSGLKDPArpigSFMFLGPTGVGKTELAKALAeAMFGSEeaLIRVDMSEFMEKYStsrligsppgYV 604
Cdd:cd19481 7 EAVEAPRRGSRLRRYGLGLPK----GILLYGPPGTGKTLLAKALA-GELGLP--LIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488287731 605 GYEEGGQLTEKIRQRPYSVILLDEVEKAHPD------------VFNILLQVLDDGHLTDakgrkvdfrNTILIMTSNL 670
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNR 138
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
110-347 |
4.47e-11 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 65.70 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 110 TEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLKKMGVSEPNSAQRRRNGQSKNAPQGTPTLDSLARDLTKLAREQSL 189
Cdd:COG0464 77 ALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 190 DPVVGRgTEVRRLIQILSRRTKNNP--------------VLVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDMG 255
Cdd:COG0464 157 DDLGGL-EEVKEELRELVALPLKRPelreeyglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 256 ALVAgtKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLIGAGGAEGAIDASNILkpalarGELQT-----------IGA 324
Cdd:COG0464 226 DLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVV------NTLLTemeelrsdvvvIAA 297
|
250 260
....*....|....*....|....
gi 488287731 325 TTLdeyqkyIEK-DAALERRFARI 347
Cdd:COG0464 298 TNR------PDLlDPALLRRFDEI 315
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
16-68 |
1.57e-10 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 57.15 E-value: 1.57e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488287731 16 AQEEAKYFRHQSVGSEHLLLALVLEPNGIAGKTLRQLNTDTEDIREEIEHLSG 68
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
552-669 |
1.34e-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: 56.83 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 552 MFLGPTGVGKTELAKALAEAMFGSeeaLIRVDMSEFMEKYstsrlIGSPPGYVgyeegGQLTEKIRQRPYSVILLDEVEK 631
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488287731 632 AHP-----------DVFNILLQVLDdghltdakGRKVDFRNTILIMTSN 669
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
374-736 |
5.92e-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: 59.15 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 374 VEITDEALHAAVQLSIRYLNDRQLPDKAIDLMDESAAKVRLDKADQPSEINELRTEISQLITEKEEAIQNQSFESAARIR 453
Cdd:COG0464 18 LDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 454 QKEKQVMEKLEELIAVKEKSLSGYSTQVTEEDVAGVVSQWTGVPLQQLEKKESERLMELETI-LHQRVVGQ-NEAVEAVS 531
Cdd:COG0464 98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLgGLEEVKEElRELVALPL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 532 RAIR-RARSGLkdpaRPIGSFMFLGPTGVGKTELAKALAEAMFGSeeaLIRVDMSEFMEKYstsrlIGSPPGYVgyeegG 610
Cdd:COG0464 178 KRPElREEYGL----PPPRGLLLYGPPGTGKTLLARALAGELGLP---LIEVDLSDLVSKY-----VGETEKNL-----R 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 611 QLTEKIRQRPYSVILLDEVEKAHPD-----------VFNILLQVLDDGHltdakgrkvdfRNTILIMTSNLgataireek 679
Cdd:COG0464 241 EVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATNR--------- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488287731 680 hvgfnvkdisknhelmqkriMEELKkafrPEFLNRIDETVVFHSLKQEEIHEIVKIM 736
Cdd:COG0464 301 --------------------PDLLD----PALLRRFDEIIFFPLPDAEERLEIFRIH 333
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-349 |
3.60e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 210 TKNNPVLVGEPGVGKTAIAEGLAQKIVNREVPE-----DMQGKRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQV 284
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488287731 285 ILFIDELHTLIGAG--GAEGAIDASNILKPALARGELQTIGATTLDEyqkyIEKDAALERRFARIQV 349
Cdd:smart00382 81 VLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIV 143
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
96-145 |
4.71e-08 |
|
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: 49.83 E-value: 4.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488287731 96 AGDEAKRLGAQKIGTEHLLLGLLRDEEILASRILVNLGLSLSKMRQLLLK 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEK 50
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
435-630 |
6.22e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 52.32 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 435 TEKEEAIQNQSFESAARIRQKEKQVMEKLEELIAVKEKSLSGYSTQVTEEDVAGVVSQWTGVPLQQLEKKESERLMElet 514
Cdd:COG1222 2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 515 ilhqRVVGQNEAVEAVSRAIRRarsGLKDP-------ARPIGSFMFLGPTGVGKTELAKALAEAmfgSEEALIRVDMSEF 587
Cdd:COG1222 79 ----DIGGLDEQIEEIREAVEL---PLKNPelfrkygIEPPKGVLLYGPPGTGKTLLAKAVAGE---LGAPFIRVRGSEL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488287731 588 MEKYstsrlIGsppgyvgyeEGGQLT----EKIRQRPYSVILLDEVE 630
Cdd:COG1222 149 VSKY-----IG---------EGARNVrevfELAREKAPSIIFIDEID 181
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
516-631 |
7.75e-07 |
|
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: 50.07 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 516 LHQRVVGQNEAVEAVSRAIR------RARSGLKDPARPIGSFMfLGPTGVGKTELAKALAEAMfgsEEALIRVDMSEFME 589
Cdd:cd19498 9 LDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTPKNILM-IGPTGVGKTEIARRLAKLA---GAPFIKVEATKFTE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488287731 590 KystsrligsppGYVGYEeggqLTEKIRQRPYSVILLDEVEK 631
Cdd:cd19498 85 V-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
216-349 |
3.79e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 47.66 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 216 LVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDMGALVagTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLI 295
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488287731 296 GAGGAEGAIDASNILKPAL--------ARGELQTIGATTLDEyqkyiEKDAALeRRFARIQV 349
Cdd:cd19481 99 RKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD-----LLDPAL-LRPGRFDE 154
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
185-326 |
1.36e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.54 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 185 REQSLDPVVG------RGTEVRRLIQilsrrtKNNP---VLVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDmg 255
Cdd:PRK13342 7 RPKTLDEVVGqehllgPGKPLRRMIE------AGRLssmILWGPPGTGKTTLARIIAGAT----------DAPFEALS-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 256 ALVAGTKyrgefedRLKKVVDEIYQD----GQVILFIDELHTLigaggaegaidasN-----ILKPALARGELQTIGATT 326
Cdd:PRK13342 69 AVTSGVK-------DLREVIEEARQRrsagRRTILFIDEIHRF-------------NkaqqdALLPHVEDGTITLIGATT 128
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
215-344 |
1.37e-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: 45.36 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 215 VLVGEPGVGKTAIAEGLAQKIVNREV----------PEDMQGKRLMMLDMGALVAGTKYRgefEDRLKKVV--DEIYQDG 282
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR---AAREGEIAvlDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488287731 283 QVILfiDELHTLIgaggAEGAIDASNILKPALARGELQTIGATTLDEYQKYIEKDAALERRF 344
Cdd:pfam07728 80 PDVL--NSLLSLL----DERRLLLPDGGELVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
520-646 |
2.01e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 46.80 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIR--RARSGLKD----PARPIgsfMFLGPTGVGKTELAKALA-EAMFgseeALIRVDMSEfmekys 592
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelRRRENLRKfglwPPRKI---LFYGPPGTGKTMLAEALAgELKL----PLLTVRLDS------ 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 593 tsrLIGSppgYVGyeEGG----QLTEKIRQRPySVILLDEVE---------KAHPD---VFNILLQVLDD 646
Cdd:COG1223 71 ---LIGS---YLG--ETArnlrKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
510-669 |
2.79e-05 |
|
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: 46.70 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 510 MELETI---LHQRVVGQNEAVEAVSRAIRrARsglkdpaRPIgsfmfL--GPTGVGKTELAKALAEAMFGSeeaLIRVdm 584
Cdd:COG0714 1 MTEARLraeIGKVYVGQEELIELVLIALL-AG-------GHL-----LleGVPGVGKTTLAKALARALGLP---FIRI-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 585 sEFMEKYSTSRLIGSppgYVgYEEGGQlTEKIRQRPY--SVILLDEVEKAHPDVFNILLQVLDDGHLTdAKGRKVDFRNT 662
Cdd:COG0714 63 -QFTPDLLPSDILGT---YI-YDQQTG-EFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLPEP 135
|
....*...
gi 488287731 663 -ILIMTSN 669
Cdd:COG0714 136 fLVIATQN 143
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
216-302 |
7.92e-05 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 43.90 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 216 LVGEPGVGKTAIAEGLAqkivnrevpeDMQGKRLMMLDMGALVAGtkYRGEFEDRLKKVVDEIYQDGQVILFIDELHTLI 295
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA----------GVWQLPLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIEKGF 103
|
....*..
gi 488287731 296 GAGGAEG 302
Cdd:cd19507 104 SNADSKG 110
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
216-294 |
1.14e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.49 E-value: 1.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488287731 216 LVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDMGALVagTKYRGEFEDRLKKVVDEIYQDGqVILFIDELHTL 294
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGEL----------KLPLLTVRLDSLI--GSYLGETARNLRKLFDFARRAP-CVIFFDEFDAI 105
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
523-644 |
1.27e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 44.97 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 523 QNEAVEAVSRAIRRARSGlkdPArpigsFMFLGPTGVGKTELAKALAEAMFGSEealiRVDMSEFMEKYSTSRLIGSPPG 602
Cdd:COG0470 1 QEEAWEQLLAAAESGRLP---HA-----LLLHGPPGIGKTTLALALARDLLCEN----PEGGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488287731 603 Y--VGYEEGG---------QLTEKIRQRPYS----VILLDEVEKAHPDVFNILLQVL 644
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTL 125
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
520-573 |
1.61e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 44.80 E-value: 1.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488287731 520 VVGQNEAVEAVSRAIRRARsglkdparpIG-SFMFLGPTGVGKTELAKALAEAMF 573
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALN 57
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
215-634 |
2.49e-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: 44.90 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 215 VLVGEPGVGKTAIAEGLAQKIVNREVPedMQGKRLMmldmgalvagTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTL 294
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGAYFIS--INGPEIM----------SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 295 I-----GAGGAEGAIDAS--NILKPALARGELQTIGATTLDEyqkyiEKDAALER--RFAR-IQVAEPTPEEAEEILKgl 364
Cdd:TIGR01243 284 ApkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEILK-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 365 rsryekhhgVEITDEALHAAVQLSirYLNDRQLPDKAIDL--MDESAAKVRLDKADQPSEINELRTEISQLITEKEEAIQ 442
Cdd:TIGR01243 357 ---------VHTRNMPLAEDVDLD--KLAEVTHGFVGADLaaLAKEAAMAALRRFIREGKINFEAEEIPAEVLKELKVTM 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 443 NQSFESAARIRQKEKQvmeklEELIAVKEkslsgystqVTEEDVAGVVsqwtgvplqqlEKKESERlmeletilhqrvvg 522
Cdd:TIGR01243 426 KDFMEALKMVEPSAIR-----EVLVEVPN---------VRWSDIGGLE-----------EVKQELR-------------- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 523 qneavEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAmfgSEEALIRVDMSEFMEKystsrligsppg 602
Cdd:TIGR01243 467 -----EAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATE---SGANFIAVRGPEILSK------------ 526
|
410 420 430
....*....|....*....|....*....|....
gi 488287731 603 YVGYEEGG--QLTEKIRQRPYSVILLDEVEKAHP 634
Cdd:TIGR01243 527 WVGESEKAirEIFRKARQAAPAIIFFDEIDAIAP 560
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
191-240 |
3.93e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 42.11 E-value: 3.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488287731 191 PVVGRGTEVRRLIQILSRRTKNNP---VLVGEPGVGKTAIAEGLAQKIVNREV 240
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
185-297 |
4.22e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 43.51 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 185 REQSLDPVVG------RGTEVRRLIQilsrrtKNNP---VLVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDmg 255
Cdd:COG2256 20 RPRTLDEVVGqehllgPGKPLRRAIE------AGRLssmILWGPPGTGKTTLARLIANAT----------DAEFVALS-- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488287731 256 ALVAGTKyrgefedRLKKVVDE----IYQDGQVILFIDELH-------------------TLIGA 297
Cdd:COG2256 82 AVTSGVK-------DIREVIEEarerRAYGRRTILFVDEIHrfnkaqqdallphvedgtiTLIGA 139
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
216-294 |
5.05e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.51 E-value: 5.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488287731 216 LVGEPGVGKTAIAEGLAQKIvnrevpedmqGKRLMMLDMGALVAgtKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTL 294
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
208-346 |
6.56e-04 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 41.51 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 208 RRTKNNPVLVGEPGVGKTAIAEGLAQKIvnrevpedmqgkRLMMLDMGALVAGTKYRGEFEDRLKKVVDEIYQDGQVILF 287
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC------------GTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488287731 288 IDELHTLIGAGGAEGAIDASNILKPALARGELQTIGATTLDEYQKYI----------EKDAALERRFAR 346
Cdd:cd19522 98 IDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
555-645 |
6.77e-04 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 43.15 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 555 GPTGVGKTELAKALAEAMFGsEEALIRVDMSEFMEKYSTSRLI-GSPPGYVGYEEGG----QLTEKIRQRPYS--VILLD 627
Cdd:PRK11331 201 GPPGVGKTFVARRLAYLLTG-EKAPQRVNMVQFHQSYSYEDFIqGYRPNGVGFRRKDgifyNFCQQAKEQPEKkyVFIID 279
|
90
....*....|....*....
gi 488287731 628 EVEKAH-PDVFNILLQVLD 645
Cdd:PRK11331 280 EINRANlSKVFGEVMMLME 298
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
407-583 |
6.78e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 42.93 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 407 ESAAKVRLDKADQPSEINELRTEISQLiteKE--EAIQNQSFESAARIRQKEKQVMEKLEELiavkekslsGYSTQVTEE 484
Cdd:COG1419 60 AAAAPAAASAAAEEEELEELRRELAEL---KEllEEQLSGLAGESARLPPELAELLERLLEA---------GVSPELARE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 485 DVAGVvsqwtgvplqqLEKKESERLMELetilhqrvvgqneAVEAVSRAIRRARSGLKDPARPIgsfMFLGPTGVGKT-E 563
Cdd:COG1419 128 LLEKL-----------PEDLSAEEAWRA-------------LLEALARRLPVAEDPLLDEGGVI---ALVGPTGVGKTtT 180
|
170 180
....*....|....*....|....
gi 488287731 564 LAKaLAeAMFGSEE----ALIRVD 583
Cdd:COG1419 181 IAK-LA-ARFVLRGkkkvALITTD 202
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
520-605 |
8.49e-04 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 42.76 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIR---RaRSGLKDPAR----PIGSFMfLGPTGVGKTE----LAKaLAEAMFgseealIRVDMSEFM 588
Cdd:PRK05201 17 IIGQDDAKRAVAIALRnrwR-RMQLPEELRdevtPKNILM-IGPTGVGKTEiarrLAK-LANAPF------IKVEATKFT 87
|
90
....*....|....*..
gi 488287731 589 EKystsrligsppGYVG 605
Cdd:PRK05201 88 EV-----------GYVG 93
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
520-660 |
1.95e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 39.69 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIRR-ARSGLkdparpigSFMFLGPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYSTSRLIG 598
Cdd:pfam00158 1 IIGESPAMQEVLEQAKRvAPTDA--------PVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFG 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488287731 599 -----------SPPGYVGYEEGGqltekirqrpysVILLDEVEKAHPDVFNILLQVLDDGHLT---DAKGRKVDFR 660
Cdd:pfam00158 73 hekgaftgadsDRKGLFELADGG------------TLFLDEIGELPLELQAKLLRVLQEGEFErvgGTKPIKVDVR 136
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
523-634 |
3.03e-03 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. 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: 410937 [Multi-domain] Cd Length: 159 Bit Score: 39.02 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 523 QNEAVEAVSRAIRRARSGLKDPARPIGSFMFLGPTGVGKTELAKALAEAmfgSEEALIRVDMSEFMEKystsrligsppg 602
Cdd:cd19529 2 KQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE---SNANFISVKGPELLSK------------ 66
|
90 100 110
....*....|....*....|....*....|....
gi 488287731 603 YVGYEEGG--QLTEKIRQRPYSVILLDEVEKAHP 634
Cdd:cd19529 67 WVGESEKAirEIFRKARQVAPCVIFFDEIDSIAP 100
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
520-630 |
3.20e-03 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain] Cd Length: 171 Bit Score: 39.14 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIrrarSGLKDP-------ARPIGSFMFLGPTGVGKTELAKALAeamfgsEEA---LIRVDMSEFME 589
Cdd:cd19501 6 VAGCEEAKEELKEVV----EFLKNPekftklgAKIPKGVLLVGPPGTGKTLLAKAVA------GEAgvpFFSISGSDFVE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488287731 590 KYstsrlIGsppgyVGYEEGGQLTEKIRQRPYSVILLDEVE 630
Cdd:cd19501 76 MF-----VG-----VGASRVRDLFEQAKKNAPCIVFIDEID 106
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
511-570 |
3.60e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 39.89 E-value: 3.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488287731 511 ELETILHQRVVGQNEAVEAVSRAI----RRARSGLKDPARPI----GSFMFLGPTGVGKTELAKALAE 570
Cdd:cd19497 5 EIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAK 72
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
215-291 |
3.63e-03 |
|
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: 38.96 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 215 VLVGEPGVGKTAIAEGLAQK------IVNRevPEDMqgkrlmmldmgalvagTKYRGEFEDRLKKVVDEIYQDGQVILFI 288
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANEtgafffLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
...
gi 488287731 289 DEL 291
Cdd:cd19519 100 DEI 102
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
520-605 |
3.74e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.80 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIR---RaRSGLKDPAR----PIGSFMfLGPTGVGKTE----LAKaLAEAMFgseealIRVDMSEFM 588
Cdd:COG1220 17 IIGQDEAKRAVAIALRnrwR-RQQLPEELRdeitPKNILM-IGPTGVGKTEiarrLAK-LANAPF------IKVEATKFT 87
|
90
....*....|....*..
gi 488287731 589 EKystsrligsppGYVG 605
Cdd:COG1220 88 EV-----------GYVG 93
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
555-648 |
3.99e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 555 GPTGVGKTELAKALAEAMFGSEEALIRVDMSEFMEKYS-----TSRLIGSPPGYVGYEEGGQLTEKI--RQRPYSVILLD 627
Cdd:pfam13401 12 GESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDllralLRALGLPLSGRLSKEELLAALQQLllALAVAVVLIID 91
|
90 100
....*....|....*....|.
gi 488287731 628 EVEKAHPDVFNILLQVLDDGH 648
Cdd:pfam13401 92 EAQHLSLEALEELRDLLNLSS 112
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
520-646 |
4.21e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 40.70 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIRRARSGlkdparpiGSFMFLGPTGVGKTELAKALAEAM-----FGSEEALIRVDMSEFMEKYSTS 594
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLncenpIGNEPCNECTSCLEITKGISSD 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488287731 595 RLIGSPPGYVGYEEGGQLTEKIRQRP----YSVILLDEVEKAHPDVFNILLQVLDD 646
Cdd:PRK14956 92 VLEIDAASNRGIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
180-426 |
4.56e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 40.42 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 180 LTKLAREQSLDPVVGR------GTEVRRLIQI--LSrrtknNPVLVGEPGVGKTAiaegLAQKIVNRevpedmqgKRLMM 251
Cdd:PRK13341 18 LADRLRPRTLEEFVGQdhilgeGRLLRRAIKAdrVG-----SLILYGPPGVGKTT----LARIIANH--------TRAHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 252 LDMGALVAGTKyrgefedRLKKVVDEIYQ-----DGQVILFIDELHTLIGAGGaegaiDAsniLKPALARGELQTIGATT 326
Cdd:PRK13341 81 SSLNAVLAGVK-------DLRAEVDRAKErlerhGKRTILFIDEVHRFNKAQQ-----DA---LLPWVENGTITLIGATT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 327 LDeyqKYIEKDAALERRfARIqvaeptpeeaeEILKGLrsryekhhgveiTDEALHAAVQlsiRYLNDRQ--LPDKAIDL 404
Cdd:PRK13341 146 EN---PYFEVNKALVSR-SRL-----------FRLKSL------------SDEDLHQLLK---RALQDKErgYGDRKVDL 195
|
250 260
....*....|....*....|...
gi 488287731 405 MDESAAK-VRLDKADQPSEINEL 426
Cdd:PRK13341 196 EPEAEKHlVDVANGDARSLLNAL 218
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
215-346 |
4.84e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 38.64 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 215 VLVGEPGVGKTAIAEGLAQKIVNREvpedmqGKRLMMLDMGALVAgTKYRGEFEDRLKKVVDEIYQDGQVILFIDELHTL 294
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGG------QKVSFFMRKGADCL-SKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488287731 295 IGAGGAEGAIDASNILKPALA-------RGELQTIGATT-LDEYqkyiekDAALER--RFAR 346
Cdd:cd19517 111 APVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGATNrPDAL------DPALRRpgRFDR 166
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
215-291 |
5.15e-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: 38.54 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488287731 215 VLVGEPGVGKTAIAEGLAQKIvnrEVPedmqgkrLMMLDMGALVAGTKyrGEFEDRLKKVVDEIYQDGQVILFIDEL 291
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEI 102
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
547-630 |
7.52e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN 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: 410910 [Multi-domain] Cd Length: 171 Bit Score: 38.09 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 547 PIGSFMFlGPTGVGKTELAKALAEAmfgSEEALIRVDMSEFMEKYstsrlIGsppgyvgyeEGGQLTEKI----RQRPYS 622
Cdd:cd19502 37 PKGVLLY-GPPGTGKTLLAKAVANH---TDATFIRVVGSELVQKY-----IG---------EGARLVRELfemaREKAPS 98
|
....*...
gi 488287731 623 VILLDEVE 630
Cdd:cd19502 99 IIFIDEID 106
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
537-630 |
8.18e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain] Cd Length: 159 Bit Score: 38.03 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488287731 537 ARSGLKDPArpigSFMFLGPTGVGKTELAKALAeamfgSEEAL--IRVDMSEFMEKystsrligsppgYVGYEEGG--QL 612
Cdd:cd19511 20 KRLGIRPPK----GVLLYGPPGCGKTLLAKALA-----SEAGLnfISVKGPELFSK------------YVGESERAvrEI 78
|
90
....*....|....*...
gi 488287731 613 TEKIRQRPYSVILLDEVE 630
Cdd:cd19511 79 FQKARQAAPCIIFFDEID 96
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
520-569 |
9.52e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.52 E-value: 9.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488287731 520 VVGQNEAVEAVSRAIRRARSGlkDPARPIgsfMFLGPTGVGKTELAKALA 569
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKAL---LLYGPPGVGKTSLAHALA 60
|
|
| |
