|
Name |
Accession |
Description |
Interval |
E-value |
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
91-906 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 1378.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 91 MFERFTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGRGSGFVAVEIPF 170
Cdd:CHL00095 1 MFERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 171 TPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPSNIRTQVIRMVGESNEAvgaSVGGGTSGQ 250
Cdd:CHL00095 81 TPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIGEIIEA---ILGAEQSRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 251 KMPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGKK 330
Cdd:CHL00095 158 KTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 331 VITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLD 410
Cdd:CHL00095 238 VITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 411 EYRKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLIDEA 490
Cdd:CHL00095 318 EYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 491 GSRVRLRHAQLPEEAKELEKELRQITKEKNEAVRGQDFEKAGELRDREMDLKAQITALIdknkEVSKAESEAADTGPLVT 570
Cdd:CHL00095 398 GSRVRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAII----QSKKTEEEKRLEVPVVT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 571 EADIQHIVSSWTGIPVEKVSTDESDRLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKS 650
Cdd:CHL00095 474 EEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 651 ELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQ 730
Cdd:CHL00095 554 ELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 731 ILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEKGGRRIGFDL-DFDEKDSSYNRIKSLVTEELKQYFRPEFLNRLDEM 809
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLGFELsENQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEI 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 810 IVFRQLTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKE 889
Cdd:CHL00095 714 IVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKP 793
|
810
....*....|....*..
gi 565359707 890 GDSVIVDVDSDGNVTVL 906
Cdd:CHL00095 794 GDIIIVDVNDEKEVKIL 810
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
91-901 |
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: 1291.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 91 MFERFTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGRGSGF--VAVEI 168
Cdd:COG0542 2 NFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVsgSSGQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 169 PFTPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPSNIRTQVIRMVGESneavgaSVGGGTS 248
Cdd:COG0542 82 YLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGS------RVTSQNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 249 GQKMPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEG 328
Cdd:COG0542 156 ESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 329 KKVITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSD-EIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGAT 407
Cdd:COG0542 236 KRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEgNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 408 TLDEYRKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLI 487
Cdd:COG0542 316 TLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 488 DEAGSRVRLRHAQLPEEAKELEKELRQITKEKNEAVRGQD---FEKAGELRDREMDLKAQITAL---------------- 548
Cdd:COG0542 396 DEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALkarweaekelieeiqe 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 549 ------------IDKNKEVSKAESEAADTGPL----VTEADIQHIVSSWTGIPVEKVSTDESDRLLKMEETLHTRIIGQD 612
Cdd:COG0542 476 lkeeleqrygkiPELEKELAELEEELAELAPLlreeVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQD 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 613 EAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYV 692
Cdd:COG0542 556 EAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYV 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 693 GYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIekggrrigf 772
Cdd:COG0542 636 GYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELI--------- 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 773 dLDFDEKDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRV 852
Cdd:COG0542 707 -LDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFL 785
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 565359707 853 VDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKEGDSVIVDVDSDG 901
Cdd:COG0542 786 AEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
95-901 |
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: 1006.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 95 FTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGR-----GSGfvaVEIP 169
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERlpkvsGPG---GQVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 170 FTPRAKRVLELSLEEARQLGHNYIgSEHLLLGLLREGEGVAARVLENLGADPSNIRTQVIRMVGesneavGASVGGGTSG 249
Cdd:TIGR03346 78 LSPDLNRLLNLAEKLAQKRGDEFI-SSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRG------GQKVTDANAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 250 QKMPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGK 329
Cdd:TIGR03346 151 DQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 330 KVITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSD-EIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATT 408
Cdd:TIGR03346 231 RLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEgQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 409 LDEYRKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLID 488
Cdd:TIGR03346 311 LDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 489 EAGSRVRLRHAQLPEEAKELEKELRQ-------ITKEKNEAV--RGQDFEKA-GELRDREMDLKAQITA----------- 547
Cdd:TIGR03346 391 EAAARIRMEIDSKPEELDELDRRIIQleiereaLKKEKDEASkkRLEDLEKElADLEEEYAELEEQWKAekasiqgiqqi 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 548 ------------------------------LIDKNKEVSKAESEAADTGPL-----VTEADIQHIVSSWTGIPVEKVSTD 592
Cdd:TIGR03346 471 keeieqvrleleqaeregdlakaaelqygkLPELEKQLQAAEQKLGEEQNRllreeVTAEEIAEVVSRWTGIPVSKMLEG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 593 ESDRLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDM 672
Cdd:TIGR03346 551 EREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDM 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 673 SEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLL 752
Cdd:TIGR03346 631 SEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVI 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 753 IMTSNVGSSVIEKGGRrigfdldfdekDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEVF 832
Cdd:TIGR03346 711 IMTSNLGSDFIQELAG-----------GDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLR 779
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 833 ERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKEGDSVIVDVDSDG 901
Cdd:TIGR03346 780 KRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
93-900 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 773.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 93 ERFTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGR-----GSGFvavE 167
Cdd:PRK10865 4 DRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRlpqveGTGG---D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 168 IPFTPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAaRVLENLGADPSNIRTQVIRMVGesneavGASVGGGT 247
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLA-DILKAAGATTANITQAIEQMRG------GESVNDQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 248 SGQKMPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIE 327
Cdd:PRK10865 154 AEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 328 GKKVITLDMGLLVAGTKYRGEFEERLKKLMEEI-KQSDEIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGA 406
Cdd:PRK10865 234 GRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 407 TTLDEYRKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDL 486
Cdd:PRK10865 314 TTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 487 IDEAGSRVRL--------------RHAQLPEEAKELEKELRQITKEKNEAVRGQDFEKAGELRDREMDLKAQITAL---- 548
Cdd:PRK10865 394 IDEAASSIRMqidskpeeldrldrRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLsgtq 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 549 -IDKNKEVSKAESEAA----DTGPL--------------------------------VTEADIQHIVSSWTGIPVEKVST 591
Cdd:PRK10865 474 tIKAELEQAKIAIEQArrvgDLARMselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIPVSRMLE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 592 DESDRLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLD 671
Cdd:PRK10865 554 SEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRID 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 672 MSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTL 751
Cdd:PRK10865 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 752 LIMTSNVGSSVIEKggrRIGfdldfdekDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEV 831
Cdd:PRK10865 714 VIMTSNLGSDLIQE---RFG--------ELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRL 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 832 FERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKEGDSVIVDVDSD 900
Cdd:PRK10865 783 YKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
95-897 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 758.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 95 FTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAakVLKSMGINLKDARVEVEKIIGRG----SGFVAVEIPF 170
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENlpviPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 171 TPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADpsniRTQVIRMVGESNEAVGASVGGGTSGQ 250
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGIT----RLDILNYISHGISKDDGKDQLGEEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 251 KMPT-----LEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPET 325
Cdd:TIGR02639 155 KEEEkgqdaLEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 326 IEGKKVITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLIGAGA-AEGAIDAANILKPALARGELQCI 404
Cdd:TIGR02639 235 LKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 405 GATTLDEYRKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAI 484
Cdd:TIGR02639 315 GSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 485 DLIDEAGSRVRLRhaqlpeeakelekelrqitkekneavrgqdfekagelrdremdlkaqitaliDKNKEvskaeseaad 564
Cdd:TIGR02639 395 DVIDEAGAAFRLR----------------------------------------------------PKAKK---------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 565 tGPLVTEADIQHIVSSWTGIPVEKVSTDESDRLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGP 644
Cdd:TIGR02639 413 -KANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGP 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 645 TGVGKSELAKALATyYFGSEeaMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDV 724
Cdd:TIGR02639 492 TGVGKTELAKQLAE-ELGVH--LLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDI 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 725 FNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSviEKGGRRIGFdldfdekdsSYNRIKSLVTEELKQYFRPEFLN 804
Cdd:TIGR02639 569 YNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGAS--EMSKPPIGF---------GGENRESKSLKAIKKLFSPEFRN 637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 805 RLDEMIVFRQLTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLA 884
Cdd:TIGR02639 638 RLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILF 717
|
810
....*....|...
gi 565359707 885 GEIKEGDSVIVDV 897
Cdd:TIGR02639 718 GKLKKGGSVKISL 730
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
110-886 |
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: 681.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 110 ARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIG---RGSGFVAVeipFTPRakrvLELSLEEA- 185
Cdd:TIGR03345 16 CVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDklpRGNTRTPV---FSPH----LVELLQEAw 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 186 ----RQLGHNYI--GSEHLLLGLLREGEGVAARVLENLGA-DPSNIRTQVIRMVGESNEA-----VGASVGGGTSGQKMP 253
Cdd:TIGR03345 89 llasLELGDGRIrsGHLLLALLTDPELRRLLGSISPELAKiDREALREALPALVEGSAEAsaaaaDAAPAGAAAGAAGTS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 254 TLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGKKVIT 333
Cdd:TIGR03345 169 ALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 334 LDMGLLVAGTKYRGEFEERLKKLMEEIKQSDE-IILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEY 412
Cdd:TIGR03345 249 LDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAATTWAEY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 413 RKHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLIDEAGS 492
Cdd:TIGR03345 329 KKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDTACA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 493 RVRLRHAQLPEEAKELEKELRQITKEKNEAVRGQDF-----EKAGELRD-----------------REMDLKAQITALID 550
Cdd:TIGR03345 409 RVALSQNATPAALEDLRRRIAALELELDALEREAALgadhdERLAELRAelaaleaelaalearwqQEKELVEAILALRA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 551 KNKEVSKAESEAAD------------------TGPL----VTEADIQHIVSSWTGIPVEKVSTDESDRLLKMEETLHTRI 608
Cdd:TIGR03345 489 ELEADADAPADDDDalraqlaeleaalasaqgEEPLvfpeVDAQAVAEVVADWTGIPVGRMVRDEIEAVLSLPDRLAERV 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 609 IGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIGSP 688
Cdd:TIGR03345 569 IGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQEAHTVSRLKGSP 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 689 PGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEKggr 768
Cdd:TIGR03345 649 PGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNAGSDLIMA--- 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 769 rigFDLDFDEKDSSyNRIKSLVTEELKQYFRPEFLNRLdEMIVFRQLTKLEVKEIADIMLKEVFERLKVK-EIELQVTER 847
Cdd:TIGR03345 726 ---LCADPETAPDP-EALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKENhGAELVYSEA 800
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 565359707 848 FRDRVVDEGYNPSYGARP----LRRAIMRLLEDSMAEKMLAGE 886
Cdd:TIGR03345 801 LVEHIVARCTEVESGARNidaiLNQTLLPELSRQILERLAAGE 843
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
255-916 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 582.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 255 LEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGKKVITL 334
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 335 DMGLLVAGTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLIGAGAAEGA-IDAANILKPALARGELQCIGATTLDEYR 413
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 414 KHIEKDPALERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLIDEAGSR 493
Cdd:PRK11034 329 NIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 494 VRLrhaqlpeeakelekelrqitkekneavrgqdfekagelrdremdlkaqitALIDKNKEVskaeseaadtgplVTEAD 573
Cdd:PRK11034 409 ARL--------------------------------------------------MPVSKRKKT-------------VNVAD 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 574 IQHIVSSWTGIPVEKVSTDESDRLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSE-- 651
Cdd:PRK11034 426 IESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEvt 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 652 --LAKALATyyfgseeAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMML 729
Cdd:PRK11034 506 vqLSKALGI-------ELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 730 QILEDGRLTDSKGRTVDFKNTLLIMTSNVGssVIEKGGRRIGfdldFDEKDSSYNRIkslvtEELKQYFRPEFLNRLDEM 809
Cdd:PRK11034 579 QVMDNGTLTDNNGRKADFRNVVLVMTTNAG--VRETERKSIG----LIHQDNSTDAM-----EEIKKIFTPEFRNRLDNI 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 810 IVFRQLTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKE 889
Cdd:PRK11034 648 IWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVD 727
|
650 660
....*....|....*....|....*..
gi 565359707 890 GDSVIVDVDSDGNVTVLNGSSGTPSDP 916
Cdd:PRK11034 728 GGQVTVALDKEKNELTYGFQSAQKHKA 754
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
596-812 |
6.23e-103 |
|
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: 317.58 E-value: 6.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 596 RLLKMEETLHTRIIGQDEAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEF 675
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 676 MERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMT 755
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 565359707 756 SNvgssviekggrrigfdldfdekdssynrikslvteelkqYFRPEFLNRLDEMIVF 812
Cdd:cd19499 161 SN---------------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
634-808 |
4.71e-88 |
|
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: 277.54 E-value: 4.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 634 RPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVL 713
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 714 FDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEkggrrigfDLDFDEKDSSYNRIKSLVTEE 793
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKIS--------DASRLGDSPDYELLKEEVMDL 152
|
170
....*....|....*
gi 565359707 794 LKQYFRPEFLNRLDE 808
Cdd:pfam07724 153 LKKGFIPEFLGRLPI 167
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
435-536 |
2.05e-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: 149.94 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 435 TVDETIQILKGLRERYEIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLIDEAGSRVRLRHAQLPEEAKELEKELRQ 514
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|..
gi 565359707 515 ITKEKNEAVRGQDFEKAGELRD 536
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAK 102
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
815-895 |
6.15e-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, 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: 104.79 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 815 LTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKEGDSVI 894
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 565359707 895 V 895
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, ... |
815-903 |
3.59e-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: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 815 LTKLEVKEIADIMLKEVFERLKVKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAGEIKEGDSVI 894
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 565359707 895 VDVDSDGNV 903
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
275-427 |
4.61e-21 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 90.67 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 275 VGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPetiegkkVITLDMGLLVAGTKYRGEFEERLK 354
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565359707 355 KLMEEIKQSDE-IILFIDEVHTLiGAGAAEGAIDAANILKPALA-RGELQCIGATTLDEYRKhieKDPALERRFQ 427
Cdd:cd00009 74 RLLFELAEKAKpGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
609-757 |
5.05e-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: 81.81 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 609 IGQDEAVKAISRAIRRarvglknpnRPIASFIFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIgsp 688
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 689 pgyvGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTdskgrTVDFKNTLLIMTSN 757
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
106-158 |
1.21e-15 |
|
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: 71.78 E-value: 1.21e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 565359707 106 AQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIG 158
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
297-427 |
4.38e-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: 72.63 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 297 CLIGEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMGLLVAgtKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTL 376
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 377 IGAGAAEG---AIDAANILKPAL-----ARGELQCIGATTldeyrkHIEK-DPALERRFQ 427
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
640-777 |
2.34e-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: 71.25 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 640 IFSGPTGVGKSELAKALATYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQ----LTEAVRRRPYTVVLFD 715
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565359707 716 EIEKAHPDVFNMMLQILEDGRLTDSKGRtvdFKNTLLIMTSNVGSSVIEKG-GRRIGFDLDFD 777
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPALlRRRFDRRIVLL 145
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
148-444 |
4.63e-13 |
|
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: 71.87 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 148 DARVEVEKIIGRGSGFVAVEIPFTPRAKRVLELSLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPSNIRTQ 227
Cdd:COG0464 29 LLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 228 VIRMVGESNEAVGASVGGGTSGQKMPTLEEYGTNLTKLA----EEGKLDPVVGRQPQIERVTQILGRRTKNNP------- 296
Cdd:COG0464 109 LLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEEllelREAILDDLGGLEEVKEELRELVALPLKRPElreeygl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 297 ------CLIGEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMGLLVAgtKYRGEFEERLKKLMEEIKQSDEIILFI 370
Cdd:COG0464 189 ppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 371 DEVHTLIGAGAAEGAIDAA---NILKPALA--RGELQCIGATtldeYRKHIeKDPALERRFQ-PVKVPEPTVDETIQILK 444
Cdd:COG0464 257 DEADALAGKRGEVGDGVGRrvvNTLLTEMEelRSDVVVIAAT----NRPDL-LDPALLRRFDeIIFFPLPDAEERLEIFR 331
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
638-757 |
8.50e-11 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 60.38 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 638 SFIFSGPTGVGKSELAKALATYYFGSEEAMIRldMSEFMerhTVSKLIGS--PPGYVGYTEGGQLTEAVRRRpyTVVLFD 715
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDT---TEEDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 565359707 716 EIEKAHPDVFNMMLQILEDGRLTDSKGRT---VDFKNTLLIMTSN 757
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
451-872 |
1.58e-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: 61.08 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 451 EIHHKLRYTDEALVAAAQLSYQYISDRFLPDKAIDLIDEAGSRVRLRHAQLPEEAKELEKELRQITKEKNEAVRGQDFEK 530
Cdd:COG0464 3 ELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 531 AGELRDREMDLKAQITALIDKNKEVSKAESEAADTGPLVTEADIQHIVSSWTGIPVEKVSTDESDRLLKMEETLHtRIIG 610
Cdd:COG0464 83 AALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD-DLGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 611 QDEAVKAISRAI--------RRARVGLKNPNRpiasFIFSGPTGVGKSELAKALATYyfgSEEAMIRLDMSEFmerhtVS 682
Cdd:COG0464 162 LEEVKEELRELValplkrpeLREEYGLPPPRG----LLLYGPPGTGKTLLARALAGE---LGLPLIEVDLSDL-----VS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 683 KligsppgYVGYTEGG--QLTEAVRRRPYTVVLFDEIEKAHPD-----------VFNMMLQILEDGRltdskgrtvdfKN 749
Cdd:COG0464 230 K-------YVGETEKNlrEVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 750 TLLIMTSNvgssviekggrrigfdlDFDEKDssynrikslvteelkqyfrPEFLNRLDEMIVFRQLTKLEVKEIADIMLK 829
Cdd:COG0464 292 VVVIAATN-----------------RPDLLD-------------------PALLRRFDEIIFFPLPDAEERLEIFRIHLR 335
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 565359707 830 evfERLKVKEIELqvtERFRDRvvDEGYNPSYGARPLRRAIMR 872
Cdd:COG0464 336 ---KRPLDEDVDL---EELAEA--TEGLSGADIRNVVRRAALQ 370
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
292-426 |
3.59e-09 |
|
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: 56.23 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 292 TKNNPCLIGEPGVGKTAIAEGLAQRIAngdvpetIEGKKVITLDM------------GLLVAGTKYRGEFEERLKKLMEE 359
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-------PPGGGVIYIDGedileevldqllLIIVGGKKASGSGELRLRLALAL 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 360 IKQSDEIILFIDEVHTLIGAG--AAEGAIDAANILKPALARGELQCIGATTldeyRKHIEKDPALERRF 426
Cdd:smart00382 74 ARKLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRF 138
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
613-757 |
4.95e-09 |
|
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: 56.14 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 613 EAVKAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALATyYFGSEeaMIRLDMSEFMERhtvskligsppgYV 692
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAG-ELGLP--LIVVKLSSLLSK------------YV 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 693 GYTEG--GQLTEAVRRRPYTVVLFDEIEKAHPD------------VFNMMLQILEDGRLTDskgrtvdfkNTLLIMTSN 757
Cdd:cd19481 68 GESEKnlRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
298-471 |
8.21e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.12 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 298 LIGEPGVGKTAIAEGLAQRIangDVPetiegkkVITLDMGLLVagTKYRGEFEERLKKLMEEIKQsDEIILFIDEVHTLi 377
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARR-APCVIFFDEFDAI- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 378 gaGAAEGAIDaanilkpalARGE--------LQC----------IGATtldeYRKHIeKDPALERRFQPV-KVPEPTVDE 438
Cdd:COG1223 106 --AKDRGDQN---------DVGEvkrvvnalLQEldglpsgsvvIAAT----NHPEL-LDSALWRRFDEViEFPLPDKEE 169
|
170 180 190
....*....|....*....|....*....|....
gi 565359707 439 TIQILKGLRERYEIhhKLRYTDEALVAAAQ-LSY 471
Cdd:COG1223 170 RKEILELNLKKFPL--PFELDLKKLAKKLEgLSG 201
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
297-376 |
1.66e-07 |
|
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: 51.90 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 297 CLIGEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMGLLVagTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTL 376
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
608-718 |
2.32e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 52.96 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 608 IIGQDEAVKAISRAIR-------RARVGLKNPNRpiasFIFSGPTGVGKSELAKALATyyfgseEAMIRLdmsefmerHT 680
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAG------ELKLPL--------LT 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 565359707 681 V--SKLIGSppgYVGYTEG--GQLTEAVRRRPyTVVLFDEIE 718
Cdd:COG1223 66 VrlDSLIGS---YLGETARnlRKLFDFARRAP-CVIFFDEFD 103
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
297-426 |
8.16e-07 |
|
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: 49.21 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 297 CLIGEPGVGKTAIAEGLAQRIANgDVPETIEGKKVIT---LDMGLLVAGtkyrGEFEERLKKLMEEIKQSDeiILFIDEV 373
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSN-RPVFYVQLTRDTTeedLFGRRNIDP----GGASWVDGPLVRAAREGE--IAVLDEI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565359707 374 HtligagaaEGAIDAANILKPAL---------ARGELQC------IGATTLDEYRKHIEKDPALERRF 426
Cdd:pfam07728 76 N--------RANPDVLNSLLSLLderrlllpdGGELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
542-718 |
1.01e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 51.93 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 542 KAQITALIDKNKEVSKAESEAADTGPLVTEADIQHIVSS-WTGIPVEKVSTDESDrllkmeetlhtrIIGQDEAVKAISR 620
Cdd:COG1222 25 LGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPrGTAVPAESPDVTFDD------------IGGLDEQIEEIRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 621 AIRRarvGLKNPN-------RPIASFIFSGPTGVGKSELAKALATyyfgseEAM---IRLDMSEFmerhtVSKLIGsppg 690
Cdd:COG1222 93 AVEL---PLKNPElfrkygiEPPKGVLLYGPPGTGKTLLAKAVAG------ELGapfIRVRGSEL-----VSKYIG---- 154
|
170 180 190
....*....|....*....|....*....|...
gi 565359707 691 yvgytEGGQL-----TEAVRRRPyTVVLFDEIE 718
Cdd:COG1222 155 -----EGARNvrevfELAREKAP-SIIFIDEID 181
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
608-659 |
1.52e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 51.35 E-value: 1.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 565359707 608 IIGQDEAVKAISRAIRRARVGlknpnrpiASFIFSGPTGVGKSELAKALATY 659
Cdd:COG2812 12 VVGQEHVVRTLKNALASGRLA--------HAYLFTGPRGVGKTTLARILAKA 55
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
640-757 |
5.78e-06 |
|
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: 46.43 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 640 IFSGPTGVGKSELAKALATYYFGSeeaMIRLDMSEFmerhtVSKLIGSPPGYVgytegGQLTEAVRRRPYTVVLFDEIEK 719
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSEL-----VSKYVGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 565359707 720 AHP-----------DVFNMMLQILEdgrltdskGRTVDFKNTLLIMTSN 757
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
298-486 |
8.89e-06 |
|
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: 49.52 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 298 LIGEPGVGKTAIAEGLAQRIanGDVPETIEGKKVITldmgllvagtKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLI 377
Cdd:TIGR01243 217 LYGPPGTGKTLLAKAVANEA--GAYFISINGPEIMS----------KYYGESEERLREIFKEAEENAPSIIFIDEIDAIA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 378 -----GAGAAEGAIDAA--NILKPALARGELQCIGATTLDEyrkhiEKDPALER--RFQP---VKVPEPtvDETIQILK- 444
Cdd:TIGR01243 285 pkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReivIRVPDK--RARKEILKv 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 565359707 445 -----------GLRERYEIHHKlrYTDEALVAAAQLSYQYISDRFLPDKAIDL 486
Cdd:TIGR01243 358 htrnmplaedvDLDKLAEVTHG--FVGADLAALAKEAAMAALRRFIREGKINF 408
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
298-444 |
1.12e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 48.46 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 298 LIGEPGVGKTAIAEGLAQRiangdvpetiegkkvitLDMGLL-VAGT----KYRGEFEERLKKLMEEIKQSDEIILFIDE 372
Cdd:COG1222 117 LYGPPGTGKTLLAKAVAGE-----------------LGAPFIrVRGSelvsKYIGEGARNVREVFELAREKAPSIIFIDE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 373 VHTLIGAGAAEGAIDAANILKPAL--------ARGELQCIGATTldeyrkHIEK-DPALER--RF-QPVKVPEPTVDETI 440
Cdd:COG1222 180 IDAIAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATN------RPDLlDPALLRpgRFdRVIEVPLPDEEARE 253
|
....
gi 565359707 441 QILK 444
Cdd:COG1222 254 EILK 257
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
273-398 |
2.94e-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: 45.57 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 273 PVVGRQPQIERVTQILGRRTKNNPCLI---GEPGVGKTAIAEGLAQRIaNGDVPETIEGKKVITLDMGLLVAGTKYRGEF 349
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPPSVlltGEAGTGKTTLLRELLRAL-ERDGGYFLRGKCDENLPYSPLLEALTREGLL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 565359707 350 EERLkkLMEEIKQSDEIILFIDEVHTLIGAGAAEGAIDAANILKPALAR 398
Cdd:pfam13191 80 RQLL--DELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDL 126
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
513-544 |
5.31e-05 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 40.84 E-value: 5.31e-05
10 20 30
....*....|....*....|....*....|..
gi 565359707 513 RQITKEKNEAVRGQDFEKAGELRDREMDLKAQ 544
Cdd:pfam02151 5 KELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
298-426 |
5.35e-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: 44.59 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 298 LIGEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMGLLVAgtKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLI 377
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDALA 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 565359707 378 -----GAGAAEGAIDAA--NILKPALARGELQCIGATTLDEyrkHIekDPALER--RF 426
Cdd:cd19503 107 pkreeDQREVERRVVAQllTLMDGMSSRGKVVVIAATNRPD---AI--DPALRRpgRF 159
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
298-373 |
1.60e-04 |
|
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: 43.19 E-value: 1.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565359707 298 LIGEPGVGKTAIAEGLAQRIanGDVPETIEGKKVITldmgllvagtKYRGEFEERLKKLMEEIKQSDEIILFIDEV 373
Cdd:cd19519 39 LYGPPGTGKTLIARAVANET--GAFFFLINGPEIMS----------KLAGESESNLRKAFEEAEKNAPAIIFIDEI 102
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
296-432 |
2.29e-04 |
|
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: 42.96 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 296 PCL--IGEPGVGKTAIAEGLAQR---IANGDVPEtiegKKVITLDM-------GLLVA-----GTKYR-----GEFEERL 353
Cdd:pfam05621 36 PNLllVGDSNNGKTMIVERFARLhppTDDEDAEI----VPVVVVQMppkpdekRLYVAilealGAPFRprdrlSKLEQQV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 354 KKLMEEIKQSdeiILFIDEVHTLIgAGAAEGAIDAANILKpALARgELQC--IGATTLDEYRkHIEKDPALERRFQPVKV 431
Cdd:pfam05621 112 LRLLRAVGVR---MLIIDEFHNLL-AGSARKQREFLNVLK-SLGN-ELRIpiVGVGTREAVR-AIRTDPQLASRFEPIAL 184
|
.
gi 565359707 432 P 432
Cdd:pfam05621 185 P 185
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
300-426 |
2.63e-04 |
|
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: 42.50 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 300 GEPGVGKTAIAEGLAQRIANGDVPETI---EGKKVITldmgllvagtKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTL 376
Cdd:cd19517 41 GPPGTGKTLMARALAAECSKGGQKVSFfmrKGADCLS----------KWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 377 IGAGAAEGAIDAANILKPALA-------RGELQCIGATT-LDEYrkhiekDPALER--RF 426
Cdd:cd19517 111 APVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGATNrPDAL------DPALRRpgRF 164
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
300-408 |
3.90e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.92 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 300 GEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMglLVAGTKyrgefeeRLKKLMEEIKQSDE----IILFIDEVHT 375
Cdd:PRK13342 43 GPPGTGKTTLARIIAGAT----------DAPFEALSA--VTSGVK-------DLREVIEEARQRRSagrrTILFIDEIHR 103
|
90 100 110
....*....|....*....|....*....|....*...
gi 565359707 376 LigagaaegaidaaN-----ILKPALARGELQCIGATT 408
Cdd:PRK13342 104 F-------------NkaqqdALLPHVEDGTITLIGATT 128
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
602-719 |
4.09e-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: 42.37 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 602 ETLHTRIIGQDEAVKAISRAIR----RARV--GLKNPNRPiASFIFSGPTGVGKSELAKALATYyfgSEEAMIRLDMSEF 675
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRnrwrRMQLpeELRDEVTP-KNILMIGPTGVGKTEIARRLAKL---AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 565359707 676 MErhtvskligsppgyVGYTeGGQLTEAVRRRPYTVVLFDEIEK 719
Cdd:cd19498 83 TE--------------VGYV-GRDVESIIRDLVEGIVFIDEIDK 111
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
608-738 |
5.19e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.53 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 608 IIGQDEAV---KAISRAIRRARvglknpnrpIASFIFSGPTGVGKSELAKALATyYFGSEeaMIRL--------DMSEFM 676
Cdd:PRK13342 14 VVGQEHLLgpgKPLRRMIEAGR---------LSSMILWGPPGTGKTTLARIIAG-ATDAP--FEALsavtsgvkDLREVI 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565359707 677 ERHtvskligsppgyvgyteggqltEAVRRRPYTVVLF-DEIE---KAHPDVFnmmLQILEDGRLT 738
Cdd:PRK13342 82 EEA----------------------RQRRSAGRRTILFiDEIHrfnKAQQDAL---LPHVEDGTIT 122
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
611-757 |
6.17e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 42.65 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 611 QDEAVKAISRAIRRARvglkNPNrpiaSFIFSGPTGVGKSELAKALATYYFGSEEAmirlDMSEFMERHTVSKLIGSPPG 690
Cdd:COG0470 1 QEEAWEQLLAAAESGR----LPH----ALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 691 Y--VGYTEGG---------QLTEAVRRRPYT----VVLFDEIEKAHPDVFNMMLQILEDGRltdskgrtvdfKNTLLIMT 755
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 565359707 756 SN 757
Cdd:COG0470 138 AN 139
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
298-373 |
8.29e-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: 40.81 E-value: 8.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565359707 298 LIGEPGVGKTAIAEGLAQRIangdvpetieGKKVITLDMGLLVAGtkYRGEFEERLKKLMEEIKQSDEIILFIDEV 373
Cdd:cd19507 36 LVGIQGTGKSLTAKAIAGVW----------QLPLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEI 99
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
290-427 |
1.70e-03 |
|
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: 40.35 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 290 RRTKNNPCLIGEPGVGKTAIAEGLAqriangdvpeTIEGKKVITLDMGLLVagTKYRGEFEERLKKLMEEIKQSDEIILF 369
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA----------TECGTTFFNVSSSTLT--SKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565359707 370 IDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHI----------EKDPALERRFQ 427
Cdd:cd19522 98 IDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
610-733 |
1.99e-03 |
|
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: 39.89 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 610 GQDEAVKAISRAIRRarvglknpNRPIASFIFSGPTGVGKSELAKALATYYFGSEEamirlDMSEFMERHTVSKLI--GS 687
Cdd:pfam13177 1 GQPEAIQLLQNSLEN--------GRLSHAYLFSGPEGVGKLELALAFAKALFCEEP-----GDDLPCGQCRSCRRIesGN 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 565359707 688 PPGYVGYTEGGQ---------LTEAVRRRPYT----VVLFDEIEKAHPDVFNMMLQILE 733
Cdd:pfam13177 68 HPDLVIIEPEGQsikidqireLQKEFSKSPYEgkkkVYIIEDAEKMTASAANSLLKFLE 126
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
606-657 |
3.02e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 40.65 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 565359707 606 TRIIGQDEAVKAISRAIRRARvglknpnrpIA-SFIFSGPTGVGKSELAKALA 657
Cdd:PRK07399 4 ANLIGQPLAIELLTAAIKQNR---------IApAYLFAGPEGVGRKLAALCFI 47
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
181-233 |
5.20e-03 |
|
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: 35.96 E-value: 5.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 565359707 181 SLEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPSNIRTQVIRMVG 233
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
607-678 |
6.34e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 39.97 E-value: 6.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565359707 607 RIIGQDEAVKAISRAIrrarvglKNPNRPiaSFIFSGPTGVGKSELAKALATYYFGS--EEAMIRLDMSEFMER 678
Cdd:PRK12402 16 DILGQDEVVERLSRAV-------DSPNLP--HLLVQGPPGSGKTAAVRALARELYGDpwENNFTEFNVADFFDQ 80
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
298-393 |
6.92e-03 |
|
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: 38.30 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565359707 298 LIGEPGVGKTAIAEGLAqriangdvpeTIEGKKVITLDMGLLVagTKYRGEFEERLKKLMEEIKQSDEIILFIDEVHTLI 377
Cdd:cd19521 45 LYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLC 112
|
90
....*....|....*.
gi 565359707 378 GAgAAEGAIDAANILK 393
Cdd:cd19521 113 GT-RGEGESEASRRIK 127
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
639-677 |
8.19e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.51 E-value: 8.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565359707 639 FIFSGPTGVGKSELAKAL-------------AT-------------YYFGSEEAMIRL-DMSEFME 677
Cdd:cd00071 2 IVLSGPSGVGKSTLLKRLleefdpnfgfsvsHTtrkprpgevdgvdYHFVSKEEFERLiENGEFLE 67
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
300-373 |
8.25e-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: 38.15 E-value: 8.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565359707 300 GEPGVGKTAIAEGLAQRIangDVPetiegkkVITLDMGLLVAGTKyrGEFEERLKKLMEEIKQSDEIILFIDEV 373
Cdd:cd19518 41 GPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEI 102
|
|
| |
