|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
6-853 |
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: 1243.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 6 NFLTDNMLSNLESAASLAIHSKNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSSNVNrENIR 85
Cdd:COG0542 4 EKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSS-GQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 86 FSNELINSLENAKGLMSANGDSYLSVDTWLVS--ESQKSPTKEILAQF-LDLREFQKELESLRAGRKIDSKTSDETLDSL 162
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLAllREGEGVAARILKKLgITLEALREALEELRGGSRVTSQNPESKTPAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 163 NKFGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVIALD 242
Cdd:COG0542 163 DKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 243 MSALIAGAKYRGEFEDRLKAVVNEVIKSE-NIILFIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYRK 321
Cdd:COG0542 243 LGALVAGAKYRGEFEERLKAVLDEVKKSEgNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEYRK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 322 YFEKDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAAAEL 401
Cdd:COG0542 323 YIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAARV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 402 KMQIESEPSSLRKVRKDIETLEVENEALKMENDEKNQKRLDEIAKELANLKEKQNALNSQFENEKSVFDGISAKKKEIdl 481
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL-- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 482 lkneaslakargefqkaaELEYGKIPSLEKEVEILEDKWKKMSEngvLLKNQVDEDLVAGILSKWTGISVQKMLTSEKQK 561
Cdd:COG0542 481 ------------------EQRYGKIPELEKELAELEEELAELAP---LLREEVTEEDIAEVVSRWTGIPVGKLLEGEREK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 562 FLEVEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFM 641
Cdd:COG0542 540 LLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYM 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 642 EKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILTS 721
Cdd:COG0542 620 EKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTS 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 722 NIASSAIMNLSGKEQE-----DVVKNELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIKASLSE 796
Cdd:COG0542 700 NIGSELILDLAEDEPDyeemkEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTD 779
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1204950885 797 NAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDAKDDEII 853
Cdd:COG0542 780 AAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
8-852 |
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: 1130.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 8 LTDNMLSNLESAASLAIHSKNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSSNVNrENIRFS 87
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPG-GQVYLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 88 NELINSLENAKGLMSANGDSYLSVDTWLVSESQ-KSPTKEILAQF-LDLREFQKELESLRAGRKIDSKTSDETLDSLNKF 165
Cdd:TIGR03346 80 PDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDdKGTLGKLLKEAgATADALEAAINAVRGGQKVTDANAEDQYEALEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 166 GIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVIALDMSA 245
Cdd:TIGR03346 160 ARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 246 LIAGAKYRGEFEDRLKAVVNEVIKSE-NIILFIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYRKYFE 324
Cdd:TIGR03346 240 LIAGAKYRGEFEERLKAVLNEVTKSEgQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 325 KDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAAAELKMQ 404
Cdd:TIGR03346 320 KDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRME 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 405 IESEPSSLRKVRKDIETLEVENEALKMENDEKNQKRLDEIAKELANLKEKQNALNSQFENEKSVFDGISAKKKEIDLLKN 484
Cdd:TIGR03346 400 IDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 485 EASLAKARGEFQKAAELEYGKIPSLEKEVEILEDkwKKMSENGVLLKNQVDEDLVAGILSKWTGISVQKMLTSEKQKFLE 564
Cdd:TIGR03346 480 ELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQ--KLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLH 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 565 VEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEKH 644
Cdd:TIGR03346 558 MEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKH 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 645 SVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILTSNIA 724
Cdd:TIGR03346 638 SVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 725 SSAIMNLSGKEQEDVVK----NELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIKASLSENAAL 800
Cdd:TIGR03346 718 SDFIQELAGGDDYEEMReavmEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALD 797
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1204950885 801 LIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDAKDDEI 852
Cdd:TIGR03346 798 FLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 849
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
8-856 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 854.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 8 LTDNMLSNLESAASLAIHSKNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSSNVNREnIRFS 87
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD-VQPS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 88 NELINSLENAKGLMSANGDSYLSVDTWLVS--ESQKSPTKEILAQFLDLREFQKELESLRAGRKIDSKTSDETLDSLNKF 165
Cdd:PRK10865 85 QDLVRVLNLCDKLAQKRGDNFISSELFVLAalESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 166 GIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVIALDMSA 245
Cdd:PRK10865 165 TIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 246 LIAGAKYRGEFEDRLKAVVNEVIKSE-NIILFIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYRKYFE 324
Cdd:PRK10865 245 LVAGAKYRGEFEERLKGVLNDLAKQEgNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 325 KDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAAAELKMQ 404
Cdd:PRK10865 325 KDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 405 IESEPSSLRKVRKDIETLEVENEALKMENDEKNQKRLDEIAKELANLKEKQNALNSQFENEKSVFDGISAKKKEIDLLKN 484
Cdd:PRK10865 405 IDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 485 EASLAKARGEFQKAAELEYGKIPSLEKEVEI---LEDKWKKmsengvLLKNQVDEDLVAGILSKWTGISVQKMLTSEKQK 561
Cdd:PRK10865 485 AIEQARRVGDLARMSELQYGKIPELEKQLAAatqLEGKTMR------LLRNKVTDAEIAEVLARWTGIPVSRMLESEREK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 562 FLEVEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFM 641
Cdd:PRK10865 559 LLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 642 EKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILTS 721
Cdd:PRK10865 639 EKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTS 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 722 NIASSAIM----NLSGKEQEDVVKNELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIKASLSEN 797
Cdd:PRK10865 719 NLGSDLIQerfgELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDE 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1204950885 798 AALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDAKDDEIIIKK 856
Cdd:PRK10865 799 ALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAVQ 857
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
27-854 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 783.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 27 KNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSSNVNRENI-RFSNELINSLENAKGLmsanG 105
Cdd:CHL00095 24 GHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPFTpRAKRVLEMSLEEARDL----G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 106 DSYlsVDTW-----LVSESQKSPT---KEILAQFLDLR-EFQKELESLrAGRKIDSKTSDETLDSLNKFGIDLTLKASEG 176
Cdd:CHL00095 100 HNY--IGTEhlllaLLEEGEGVAArvlENLGVDLSKIRsLILNLIGEI-IEAILGAEQSRSKTPTLEEFGTNLTKEAIDG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 177 KLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVIALDMSALIAGAKYRGEF 256
Cdd:CHL00095 177 NLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 257 EDRLKAVVNEVIKSENIILFIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYRKYFEKDAALQRRFQPV 336
Cdd:CHL00095 257 EERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPALERRFQPV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 337 NVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAAAELKMQIESEPSSLRKVR 416
Cdd:CHL00095 337 YVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRVRLINSRLPPAARELD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 417 KDI-ETLEVENEALKMENDEKNQKRLDEiakelanlkekqnalnsqfenEKSVFDGISAKKKEIdllkneaslakargef 495
Cdd:CHL00095 417 KELrEILKDKDEAIREQDFETAKQLRDR---------------------EMEVRAQIAAIIQSK---------------- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 496 qKAAELEYGKIPSlekeveiledkwkkmsengvllknqVDEDLVAGILSKWTGISVQKMLTSEKQKFLEVEKHLKESVIG 575
Cdd:CHL00095 460 -KTEEEKRLEVPV-------------------------VTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 576 QDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEKHSVSRLLGAPPG 655
Cdd:CHL00095 514 QDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPG 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 656 YIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILTSNIASSAIMNLSG-- 733
Cdd:CHL00095 594 YVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGgl 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 734 ----------KEQEDVVKN----ELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIKASLSENAA 799
Cdd:CHL00095 674 gfelsenqlsEKQYKRLSNlvneELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIK 753
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1204950885 800 LLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDAKDD-EIII 854
Cdd:CHL00095 754 TLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDVNDEkEVKI 809
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
8-833 |
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: 726.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 8 LTDNMLSNLESAASLAIHSKNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSsnvNRENIRFS 87
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRG---NTRTPVFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 88 NELINSLENAKGLMSAN-GDSYLSVDtWLVSESQKSPTKEILAQFLdLREFQK-ELESLRAGRKIDSKTSDETL------ 159
Cdd:TIGR03345 78 PHLVELLQEAWLLASLElGDGRIRSG-HLLLALLTDPELRRLLGSI-SPELAKiDREALREALPALVEGSAEASaaaada 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 160 ------------DSLNKFGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKK 227
Cdd:TIGR03345 156 apagaaagaagtSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 228 DVPKSLQNKKVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSEN-IILFIDEIHTIVGAGASEGSMDAANILKPALARG 306
Cdd:TIGR03345 236 DVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALARG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 307 ELHTIGATTLKEYRKYFEKDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFL 386
Cdd:TIGR03345 316 ELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 387 PDKAIDLIDEAAAELKMQIESEPSSLRKVRKDIETLEVENEALKMEN--DEKNQKRLDEIAKELANLKEKQNALNSQFEN 464
Cdd:TIGR03345 396 PDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 465 EKSVFDGISAkkkeidllkneaslakARGEFQKAAELEYGKIPSLEKEVEILEDKWKKMSENGVLLKNQVDEDLVAGILS 544
Cdd:TIGR03345 476 EKELVEAILA----------------LRAELEADADAPADDDDALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 545 KWTGISVQKMLTSEKQKFLEVEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKF 624
Cdd:TIGR03345 540 DWTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAEL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 625 LFDDEKAMIRFDMSEFMEKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATD 704
Cdd:TIGR03345 620 LYGGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMED 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 705 SKGVTVDFKNTIIILTSNIASSAIMNLSGKEQE--------DVVKNELKNFFKPEFLNRLdDIITFNPLGKDEAYEIVKL 776
Cdd:TIGR03345 700 GEGREIDFKNTVILLTSNAGSDLIMALCADPETapdpeallEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRL 778
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1204950885 777 LFKDLQMSL-ENKGIKASLSENAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMIL 833
Cdd:TIGR03345 779 KLDRIARRLkENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
8-847 |
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: 685.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 8 LTDNMLSNLESAASLAIHSKNNEVAPLHLLWALSVDSTSIlnQILNKLNISKEALELEIKSRIS-KLATSSNVNRENIRF 86
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAI--EILEECGGDVELLRKRLEDYLEeNLPVIPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 87 SNELINSLENAKGLMSANGDSYLSVDTWLVS--ESQKSPTKEILAQ----FLDLREFQKEL---ESLRAGRKIDSKTSDE 157
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVAlfDEEDSHASYFLKSqgitRLDILNYISHGiskDDGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 158 TL-DSLNKFGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNK 236
Cdd:TIGR02639 159 KGqDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 237 KVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIVGAGA-SEGSMDAANILKPALARGELHTIGATT 315
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGSTT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 316 LKEYRKYFEKDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLID 395
Cdd:TIGR02639 319 YEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 396 EAAAELKMQIESEPsslrkvrkdietlevenealkmendeknqkrldeiaKELANLKEkqnalnsqfeneksvfdgisak 475
Cdd:TIGR02639 399 EAGAAFRLRPKAKK------------------------------------KANVNVKD---------------------- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 476 kkeidllkneaslakargefqkaaeleygkipslekeveiledkwkkmsengvllknqvdedlVAGILSKWTGISVQKML 555
Cdd:TIGR02639 421 ---------------------------------------------------------------IENVVAKMAKIPVKTVS 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 556 TSEKQKFLEVEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRF 635
Cdd:TIGR02639 438 SDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRF 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 636 DMSEFMEKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNT 715
Cdd:TIGR02639 515 DMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNV 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 716 IIILTSNIASS----AIMNLSGKEQEDVVKNELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIK 791
Cdd:TIGR02639 595 ILIMTSNAGASemskPPIGFGGENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIE 674
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1204950885 792 ASLSENAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDA 847
Cdd:TIGR02639 675 LELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
160-851 |
2.00e-165 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 499.36 E-value: 2.00e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 160 DSLNKFGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVI 239
Cdd:PRK11034 167 ERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIY 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 240 ALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIVGAG-ASEGSMDAANILKPALARGELHTIGATTLKE 318
Cdd:PRK11034 247 SLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGaASGGQVDAANLIKPLLSSGKIRVIGSTTYQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 319 YRKYFEKDAALQRRFQPVNVGEPSVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAA 398
Cdd:PRK11034 327 FSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 399 AELKMQiesePSSLRKvrKDIETLEVENEALKMendeknqkrldeiakelANLKEKQnalnsqfeneksvfdgISAKKKe 478
Cdd:PRK11034 407 ARARLM----PVSKRK--KTVNVADIESVVARI-----------------ARIPEKS----------------VSQSDR- 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 479 iDLLKNeaslakargefqkaaeleygkipslekeveiLEDKWkkmsengvllknqvdedlvagilskwtgisvqKMLtse 558
Cdd:PRK11034 447 -DTLKN-------------------------------LGDRL--------------------------------KML--- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 559 kqkflevekhlkesVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRFDMS 638
Cdd:PRK11034 460 --------------VFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 639 EFMEKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIII 718
Cdd:PRK11034 523 EYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLV 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 719 LTSNIASSAIMNLS-GKEQEDVVKN---ELKNFFKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLENKGIKASL 794
Cdd:PRK11034 603 MTTNAGVRETERKSiGLIHQDNSTDameEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEV 682
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1204950885 795 SENAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSIIIDAKDDE 851
Cdd:PRK11034 683 SQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEK 739
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
561-762 |
2.28e-96 |
|
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: 298.71 E-value: 2.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 561 KFLEVEKHLKESVIGQDKALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEF 640
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 641 MEKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILT 720
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1204950885 721 SniassaimnlsgkeqedvvknelkNFFKPEFLNRLDDIITF 762
Cdd:cd19499 161 S------------------------NHFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
599-759 |
2.40e-84 |
|
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: 266.75 E-value: 2.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 599 KPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEKHSVSRLLGAPPGYIGHEEGGELTEAVRRKPYSVLL 678
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 679 FDEVEKAHKDVFNVLLGILDDGRATDSKGVTVDFKNTIIILTSNIASSAIMNLSG-------KEQEDVVKNELKNFFKPE 751
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRlgdspdyELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1204950885 752 FLNRLDDI 759
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
342-444 |
1.71e-40 |
|
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: 144.17 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 342 SVNEALAMLRGIKEKLEIHHNVTINDSALVAAAKLSKRYIADRFLPDKAIDLIDEAAAELKMQIESEPSSLRKVRKDIET 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|...
gi 1204950885 422 LEVENEALKMENDEKNQKRLDEI 444
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKL 103
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
765-854 |
5.70e-22 |
|
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: 90.97 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 765 LGKDEAYEIVKLLFKDLQMSLENKGIKASLSENAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSII 844
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1204950885 845 IDAKDDEIII 854
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
765-845 |
1.24e-21 |
|
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: 89.39 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 765 LGKDEAYEIVKLLFKDLQMSLENKGIKASLSENAALLIAKDGFDPDFGARPLRRAIYDLIEDKLSDMILADELHENDSII 844
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1204950885 845 I 845
Cdd:pfam10431 81 V 81
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
182-334 |
5.56e-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: 90.28 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 182 IGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPkslqnkkVIALDMSALIAGAKYRGEFEDRLK 261
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1204950885 262 AVVNEVIK-SENIILFIDEIHTIvGAGASEGSMDAANILKPALA-RGELHTIGATTLKEYRKyfeKDAALQRRFQ 334
Cdd:cd00009 74 RLLFELAEkAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
574-764 |
7.70e-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: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 574 IGQDKALSALARAIKRNkaglnadnkPIGSFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEKHSVSRLlgap 653
Cdd:cd00009 1 VGQEEAIEALREALELP---------PPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 654 pgyIGHEEGGELTEAVRRKPYSVLLFDEVEKAHKDVFNVLLGILDDGratdsKGVTVDFKNTIIILTSNIASSAImnlsg 733
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGD----- 134
|
170 180 190
....*....|....*....|....*....|.
gi 1204950885 734 keqedvvknelknfFKPEFLNRLDDIITFNP 764
Cdd:cd00009 135 --------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-334 |
6.45e-14 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 69.16 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMSALIAgaKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 284 VGAGASEG---SMDAANILKPAL-----ARGELHTIGATTlkeyrkYFEK-DAALQRRFQ 334
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
603-732 |
2.61e-13 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 67.70 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 603 SFLFLGPTGVGKTQSAKALAKFLFDDEKAMIRfdMSEFMEKhsvSRLLGA--PPGYIGHEEGGELTEAVRRKpySVLLFD 680
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1204950885 681 EVEKAHKDVFNVLLGILDDGRATDSKGVT---VDFKNTIIILTSNIASSAIMNLS 732
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMNPLDRGLNELS 128
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
605-722 |
2.07e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.47 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 605 LFLGPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEKHSVSRLLGAPPGYIGHEEGGE----LTEAVRRKPYSVLLFD 680
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1204950885 681 EVEKAHKDVFNVLLGILDDGRATDSKGVtvdFKNTIIILTSN 722
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTN 124
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
168-367 |
1.10e-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: 67.63 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 168 DLTLKASEGKLDPVIGREEEIERLMQIL--------IRKTKNNP-----ILLGEPGVGKTAIVEALAQRIikkdvpkslq 234
Cdd:COG0464 146 EELLELREAILDDLGGLEEVKEELRELValplkrpeLREEYGLPpprglLLYGPPGTGKTLLARALAGEL---------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 235 NKKVIALDMSALIAgaKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIVGAGASEGSMDAA---NILKPALA--RGELH 309
Cdd:COG0464 216 GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvNTLLTEMEelRSDVV 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1204950885 310 TIGATTLKEyrkyfEKDAALQRRFQ-PVNVGEPSVNEALAMLRGIKEKLEIHHNVTIND 367
Cdd:COG0464 294 VIAATNRPD-----LLDPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEE 347
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
564-786 |
1.16e-10 |
|
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: 64.55 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 564 EVEKHLKESVIGQdkalsaLARAIKRNKAGLnadnKPIGSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRFDMSEFMEK 643
Cdd:COG0464 164 EVKEELRELVALP------LKRPELREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDLVSK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 644 hsvsrllgappgYIGHEEGG--ELTEAVRRKPYSVLLFDEVEKAHKD-----------VFNVLLGILDDGRatdskgvtv 710
Cdd:COG0464 231 ------------YVGETEKNlrEVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR--------- 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1204950885 711 dfKNTIIILTSNiassAIMNLsgkeqeDvvknelknffkPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLE 786
Cdd:COG0464 290 --SDVVVIAATN----RPDLL------D-----------PALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDED 342
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
578-722 |
2.64e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 59.60 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 578 KALSALARAIKRNKAGLNADNKPIGSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRFDMSEFMEKHSVSrllgappgyi 657
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSKYVGE---------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1204950885 658 GHEEGGELTEAVRRKPYSVLLFDEVEKA------------HKDVFNVLLGILDDGRATDskgvtvdfkNTIIILTSN 722
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
571-697 |
4.85e-08 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 55.97 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 571 ESVIGQDKALSALARAIKRNKaglnadnkpIG-SFLFLGPTGVGKTQSAKALAKFLF-----DDE--------KAMIRF- 635
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALNcengpTGEpcgecescRAIAAGs 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1204950885 636 --DMSEfmekhsvsrlLGAPPGYIGHEEGGELTEAVRRKPYS----VLLFDEVEKAHKDVFNVLLGIL 697
Cdd:COG2812 81 hpDVIE----------IDAEASNIGVDDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALLKTL 138
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
199-333 |
1.34e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 199 TKNNPILLGEPGVGKTAIVEALAQRIIKKdvpkslqNKKVIALDMSALIAGA------------KYRGEFEDRLKAVVNE 266
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-------GGGVIYIDGEDILEEVldqllliivggkKASGSGELRLRLALAL 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1204950885 267 VIKSENIILFIDEIHTIVGAGASEGSMDAA--NILKPALARGELHTIGATTlkeyRKYFEKDAALQRRF 333
Cdd:smart00382 74 ARKLKPDVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRF 138
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
204-333 |
3.04e-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: 50.37 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIIKkdvpkslQNKKVIAL--DMSA--LIAGAKYR-GEFEDRLKAVVNEVIKSEniILFID 278
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSN-------RPVFYVQLtrDTTEedLFGRRNIDpGGASWVDGPLVRAAREGE--IAVLD 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 279 EIHtivgagasEGSMDAANILKPALARGELHT---------------IGATTLKEYRKYFEKDAALQRRF 333
Cdd:pfam07728 74 EIN--------RANPDVLNSLLSLLDERRLLLpdggelvkaapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
204-334 |
3.28e-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: 50.74 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILL-GEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMSALIagAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHT 282
Cdd:cd19481 29 ILLyGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1204950885 283 IVGAGASEGSMDAANILKPAL--------ARGELHTIGATTLKEyrkyfEKDAALQR--RFQ 334
Cdd:cd19481 97 IGRKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD-----LLDPALLRpgRFD 153
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
605-722 |
1.04e-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: 48.74 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 605 LFLGPTGVGKTQSAKALAKFLFDDekaMIRFDMSEFMEKhsvsrllgappgYIGHEEGG--ELTEAVRRKPYSVLLFDEV 682
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSK------------YVGESEKRlrELFEAAKKLAPCVIFIDEI 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1204950885 683 EK-----------AHKDVFNVLLGILDdgratdskGVTVDFKNTIIILTSN 722
Cdd:pfam00004 67 DAlagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
564-625 |
2.10e-06 |
|
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: 49.91 E-value: 2.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 564 EVEKHLKESVIGQDKALSALARAI----KRNKAGLNADNKPI----GSFLFLGPTGVGKTQSAKALAKFL 625
Cdd:cd19497 5 EIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
180-305 |
3.01e-06 |
|
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: 48.27 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 180 PVIGREEEIERLMQILIRKTKNNP---ILLGEPGVGKTAIVEALAQRIIKKDVpKSLQNKKVIALDMSALIAGAKYRGEF 256
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG-YFLRGKCDENLPYSPLLEALTREGLL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1204950885 257 EDRLKAVVNEVIksENIILFIDEIHTIVGAGASEGSMDAANILKPALAR 305
Cdd:pfam13191 80 RQLLDELESSLL--EAWRAALLEALAPVPELPGDLAERLLDLLLRLLDL 126
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
571-786 |
1.55e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.19 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 571 ESVIGQDKALSALARAIK-------RNKAGLNADNKpigsFLFLGPTGVGKTQSAKALAKFLfDDEKAMIRFD--MSEFM 641
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGEL-KLPLLTVRLDslIGSYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 642 EKhSVSRLlgappgyigheegGELTEAVRRKPySVLLFDEVEKAHKD------------VFNVLLGILDDGRAtdskgvt 709
Cdd:COG1223 77 GE-TARNL-------------RKLFDFARRAP-CVIFFDEFDAIAKDrgdqndvgevkrVVNALLQELDGLPS------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1204950885 710 vdfkNTIIILTSNiassaimnlsgkeQEDVVknelknffKPEFLNRLDDIITFNPLGKDEAYEIVKLLFKDLQMSLE 786
Cdd:COG1223 135 ----GSVVIAATN-------------HPELL--------DSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFE 186
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
204-281 |
1.82e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.16 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALdmSALIAGAKyrgefedRLKAVVNEVIKS----ENIILFIDE 279
Cdd:PRK13342 40 ILWGPPGTGKTTLARIIAGAT----------DAPFEAL--SAVTSGVK-------DLREVIEEARQRrsagRRTILFIDE 100
|
..
gi 1204950885 280 IH 281
Cdd:PRK13342 101 IH 102
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
19-71 |
1.95e-05 |
|
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: 42.51 E-value: 1.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1204950885 19 AASLAIHSKNNEVAPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRIS 71
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
204-281 |
2.55e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 47.74 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALdmSALIAGAKyrgefedRLKAVVNE----VIKSENIILFIDE 279
Cdd:COG2256 53 ILWGPPGTGKTTLARLIANAT----------DAEFVAL--SAVTSGVK-------DIREVIEEarerRAYGRRTILFVDE 113
|
..
gi 1204950885 280 IH 281
Cdd:COG2256 114 IH 115
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
165-224 |
2.73e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 2.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1204950885 165 FGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILL---GEPGVGKTAIVEALAQRI 224
Cdd:COG3899 273 AAAGRRLLARRLIPQPLVGREAELAALLAALERARAGRGELVlvsGEAGIGKSRLVRELARRA 335
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
178-351 |
3.14e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 46.42 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 178 LDPVIGREEEIERLMQIL--------IRKTKNNP---ILL-GEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMSA 245
Cdd:COG1223 1 LDDVVGQEEAKKKLKLIIkelrrrenLRKFGLWPprkILFyGPPGTGKTMLAEALAGEL----------KLPLLTVRLDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 246 LIagAKYRGEFEDRLKAVVnEVIKSENIILFIDEIHTIVGA-GASEGSMDAANILKPALA-----RGELHTIGATTLKEy 319
Cdd:COG1223 71 LI--GSYLGETARNLRKLF-DFARRAPCVIFFDEFDAIAKDrGDQNDVGEVKRVVNALLQeldglPSGSVVIAATNHPE- 146
|
170 180 190
....*....|....*....|....*....|...
gi 1204950885 320 rkyfEKDAALQRRFQPV-NVGEPSVNEALAMLR 351
Cdd:COG1223 147 ----LLDSALWRRFDEViEFPLPDKEERKEILE 175
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
575-722 |
3.51e-05 |
|
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: 44.89 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 575 GQDKALSALARAIKRNKAGlnadnkpiGSFLFLGPTGVGKTQSAKALAKFLF----DDEKAMIRFDMSEFMEKHSVSRLL 650
Cdd:pfam13177 1 GQPEAIQLLQNSLENGRLS--------HAYLFSGPEGVGKLELALAFAKALFceepGDDLPCGQCRSCRRIESGNHPDLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 651 gappgYIGHEEGG-------ELTEAVRRKPY----SVLLFDEVEKAHKDVFNVLLGILDDGRAtdskgvtvdfkNTIIIL 719
Cdd:pfam13177 73 -----IIEPEGQSikidqirELQKEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLEEPPG-----------NTVIIL 136
|
...
gi 1204950885 720 TSN 722
Cdd:pfam13177 137 LTE 139
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
178-351 |
4.80e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 46.54 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 178 LDPVIGREEEIERLMQILIRKTKN------------NPILL-GEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMS 244
Cdd:COG1222 77 FDDIGGLDEQIEEIREAVELPLKNpelfrkygieppKGVLLyGPPGTGKTLLAKAVAGEL----------GAPFIRVRGS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 245 ALIagAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIVGAGASEGSMDAANILKPAL--------ARGELHTIGATTL 316
Cdd:COG1222 147 ELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATNR 224
|
170 180 190
....*....|....*....|....*....|....*...
gi 1204950885 317 KEyrkyfEKDAALQR--RF-QPVNVGEPSVNEALAMLR 351
Cdd:COG1222 225 PD-----LLDPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
180-283 |
5.79e-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: 44.20 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 180 PVIGREEEIERLMQILIRKTKNNP-------------ILLGEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMSAL 246
Cdd:cd19503 1 DIGGLDEQIASLKELIELPLKYPElfralglkpprgvLLHGPPGTGKTLLARAVANEA----------GANFLSISGPSI 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1204950885 247 IAgaKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:cd19503 71 VS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
564-625 |
6.47e-05 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 46.19 E-value: 6.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1204950885 564 EVEKHLKESVIGQDKALSALARAI----KRNKAGLNADNKP------IgsfLFLGPTGVGKTQSAKALAKFL 625
Cdd:COG1219 65 EIKAFLDEYVIGQERAKKVLSVAVynhyKRLNSGSKDDDDVeleksnI---LLIGPTGSGKTLLAQTLARIL 133
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
599-784 |
8.07e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.77 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 599 KPIGSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRFDMSEFMEKhsvsrllgappgYIGheEGG----ELTEAVRRKPY 674
Cdd:COG1222 110 EPPKGVLLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSELVSK------------YIG--EGArnvrEVFELAREKAP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 675 SVLLFDEVE------------KAHKDVFNVLLGILDDgraTDSKGvtvdfkNTIIILTSNiassaimnlsgkeQEDVVkn 742
Cdd:COG1222 173 SIIFIDEIDaiaarrtddgtsGEVQRTVNQLLAELDG---FESRG------DVLIIAATN-------------RPDLL-- 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1204950885 743 elknffKPEFL--NRLDDIITFNPLGKDEAYEIVKLLFKDLQMS 784
Cdd:COG1222 229 ------DPALLrpGRFDRVIEVPLPDEEAREEILKIHLRDMPLA 266
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
571-625 |
8.20e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 46.30 E-value: 8.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1204950885 571 ESVIGQDKALSALARAIKRNKAGlNAdnkpigsFLFLGPTGVGKTQSAKALAKFL 625
Cdd:PRK06647 16 NSLEGQDFVVETLKHSIESNKIA-NA-------YIFSGPRGVGKTSSARAFARCL 62
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
564-625 |
1.01e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 45.53 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1204950885 564 EVEKHLKESVIGQDKALSALARAI----KRnkagLNADNKPIGS-------FLFLGPTGVGKTQSAKALAKFL 625
Cdd:PRK05342 64 EIKAHLDQYVIGQERAKKVLSVAVynhyKR----LRHGDKKDDDvelqksnILLIGPTGSGKTLLAQTLARIL 132
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
573-699 |
1.25e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 45.32 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 573 VIGQDKALSALARAIKRNKAGlnadnkpiGSFLFLGPTGVGKTQSAKALAKFL-----FDDEKAMIRFDMSEFMEKHSVS 647
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLncenpIGNEPCNECTSCLEITKGISSD 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1204950885 648 RLLGAPPGYIGHEEGGELTEAVRRKP----YSVLLFDEVEKAHKDVFNVLLGILDD 699
Cdd:PRK14956 92 VLEIDAASNRGIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
202-332 |
1.70e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 45.43 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 202 NPILLGEPGVGKTaiveALAqRIIKKDVpkslqNKKVIALdmSALIAGAKyrgefedRLKAVVNEVIKSEN-----IILF 276
Cdd:PRK13341 54 SLILYGPPGVGKT----TLA-RIIANHT-----RAHFSSL--NAVLAGVK-------DLRAEVDRAKERLErhgkrTILF 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1204950885 277 IDEIHTIVGAgasegSMDAaniLKPALARGELHTIGATTlkeYRKYFEKDAALQRR 332
Cdd:PRK13341 115 IDEVHRFNKA-----QQDA---LLPWVENGTITLIGATT---ENPYFEVNKALVSR 159
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
571-623 |
2.14e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 44.77 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1204950885 571 ESVIGQDKALSALARAIKRNKAGlnadnkpiGSFLFLGPTGVGKTQSAKALAK 623
Cdd:PRK14971 17 ESVVGQEALTTTLKNAIATNKLA--------HAYLFCGPRGVGKTTCARIFAK 61
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
204-333 |
2.64e-04 |
|
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: 42.39 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIikkDVPkslqnkkVIALDMSALIAGAKyrGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1204950885 284 VG--AGASE-----------GSMDAANILKPALARgeLHTIGATTLKEyrkyfEKDAALQR--RF 333
Cdd:cd19518 106 TPkrESAQRemerrivsqllTCMDELNNEKTAGGP--VLVIGATNRPD-----SLDPALRRagRF 163
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
603-701 |
3.08e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 603 SFLFL-GPTGVGKTQSAKALAKFLFDDEKAMIRFDMSEFMEK----HSVSRLLGAPPGYIGHEEggELTEAV-----RRK 672
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKE--ELLAALqqlllALA 83
|
90 100
....*....|....*....|....*....
gi 1204950885 673 PYSVLLFDEVEKAHKDVFNVLLGILDDGR 701
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
181-222 |
3.14e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 43.62 E-value: 3.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1204950885 181 VIGREEEIER-LMQILIRKtknnPILL-GEPGVGKTAIVEALAQ 222
Cdd:COG0714 14 YVGQEELIELvLIALLAGG----HLLLeGVPGVGKTTLAKALAR 53
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
183-430 |
5.53e-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: 43.74 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 183 GREEEIERLMQI---------LIRKTKNNP----ILLGEPGVGKTAIVEALAQRIikkdvpkslqNKKVIALDMSALIAg 249
Cdd:TIGR01243 182 GLKEAKEKIREMvelpmkhpeLFEHLGIEPpkgvLLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIMS- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 250 aKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIV-----GAGASEGSMDAA--NILKPALARGELHTIGATTLKEyrky 322
Cdd:TIGR01243 251 -KYYGESEERLREIFKEAEENAPSIIFIDEIDAIApkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATNRPD---- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 323 fEKDAALQR--RF-QPVNVGEP------------SVNEALAMLRGIKEKLEIHHNVTINDsaLVAAAKLSKRYIADRFLP 387
Cdd:TIGR01243 326 -ALDPALRRpgRFdREIVIRVPdkrarkeilkvhTRNMPLAEDVDLDKLAEVTHGFVGAD--LAALAKEAAMAALRRFIR 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1204950885 388 DKAIDL-----IDEAAAELKMQIES--------EPSSLRKVR--------KDIETLEVENEALK 430
Cdd:TIGR01243 403 EGKINFeaeeiPAEVLKELKVTMKDfmealkmvEPSAIREVLvevpnvrwSDIGGLEEVKQELR 466
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
576-722 |
5.60e-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: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 576 QDKALSALARAIKRNKaGLNAdnkpigsFLFLGPTGVGKTQSAKALAKFLFDDEKAmirfDMSEFMEKHSVSRLLGAPPG 655
Cdd:COG0470 1 QEEAWEQLLAAAESGR-LPHA-------LLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 656 Y--IGHEEGG---------ELTEAVRRKPYS----VLLFDEVEKAHKDVFNVLLGILDDGRatdskgvtvdfKNTIIILT 720
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 1204950885 721 SN 722
Cdd:COG0470 138 AN 139
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
204-314 |
8.22e-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: 40.96 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIIKKdvpkslqNKKVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKG-------GQKVSFFMRKGADCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGL 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 1204950885 284 VGAGASEGSMDAANILKPALA-------RGELHTIGAT 314
Cdd:cd19517 111 APVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGAT 148
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
177-221 |
1.37e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 41.78 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1204950885 177 KLDPVIGREEEIERLMQILirKTKNNPILL--GEPGVGKTAIVEALA 221
Cdd:PRK00440 15 TLDEIVGQEEIVERLKSYV--KEKNMPHLLfaGPPGTGKTTAALALA 59
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
567-623 |
1.51e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 41.83 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1204950885 567 KHLKEsVIGQDKALSALARAIKRNKAGLNAdnKPIgsfLFLGPTGVGKTQSAKALAK 623
Cdd:PRK04195 11 KTLSD-VVGNEKAKEQLREWIESWLKGKPK--KAL---LLYGPPGVGKTSLAHALAN 61
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
196-334 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 196 IRKTKNNPILLGEPGVGKTAIVEALAQRIikkdvpkslqnkKVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIIL 275
Cdd:cd19522 29 IRRPWKGVLMVGPPGTGKTLLAKAVATEC------------GTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1204950885 276 FIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYRKY----------FEKDAALQRRFQ 334
Cdd:cd19522 97 FIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLE 165
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
170-224 |
1.66e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 41.51 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1204950885 170 TLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRI 224
Cdd:PRK12402 6 TEKYRPALLEDILGQDEVVERLSRAVDSPNLPHLLVQGPPGSGKTAAVRALAREL 60
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
571-699 |
2.09e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 41.40 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 571 ESVIGQDKALSALARAIKRNKAGlnadnkpiGSFLFLGPTGVGKTQSAKALAKFL----FDDEKAMIRFDMSEF--MEKH 644
Cdd:PRK14970 17 DDVVGQSHITNTLLNAIENNHLA--------QALLFCGPRGVGKTTCARILARKInqpgYDDPNEDFSFNIFELdaASNN 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1204950885 645 SVsrllgappgyighEEGGELTEAVRRKP----YSVLLFDEVEKAHKDVFNVLLGILDD 699
Cdd:PRK14970 89 SV-------------DDIRNLIDQVRIPPqtgkYKIYIIDEVHMLSSAAFNAFLKTLEE 134
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
564-684 |
2.40e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 40.06 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 564 EVEKHLKESVIGQDKALSALARAIkRNKAGLNADNKPI------GSFLFLGPTGVGKTQSAKALAKFLfddEKAMIRFDM 637
Cdd:cd19498 4 EIVSELDKYIIGQDEAKRAVAIAL-RNRWRRMQLPEELrdevtpKNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1204950885 638 SEFMEKhsvsrllgappGYIGHEeggelTEAVRRKPYSVLLF-DEVEK 684
Cdd:cd19498 80 TKFTEV-----------GYVGRD-----VESIIRDLVEGIVFiDEIDK 111
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
412-517 |
2.44e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.87 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 412 LRKVRKDIETLEVENEALKMENDEKnQKRLDEIAKELANLKEKQNALNSQFENEKSVFDGISAKKKEIDllknEASLAKA 491
Cdd:COG4026 137 LLELKEKIDEIAKEKEKLTKENEEL-ESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL----KKRLLEV 211
|
90 100
....*....|....*....|....*.
gi 1204950885 492 RGEFQKAAELEYGKIPSLEKEVEILE 517
Cdd:COG4026 212 FSLEELWKELFPEELPEEDFIYFATE 237
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
387-574 |
3.03e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 387 PDKAIDLIDEAAAELKMQIESEPSSL-------RKVRKDIETLEVENEALKMENDEKNQKRLDEIAKELANLKEKQNALN 459
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKklieeteNLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 460 SQFENEKSV-------FDGISAKKKEIDLLKNEASLAKARGEFQKAAELEygkIPSLEKEVEILEDKWKKMSENGVLLKN 532
Cdd:pfam02463 231 YLKLNEERIdllqellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE---KKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1204950885 533 QVDEDLVAGILSKWTGISVQKMLTSEKQKFLEVEKHLKESVI 574
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
175-308 |
3.05e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 39.47 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 175 EGKLDPVIGREEEIERLMQILIR-----KTKNNPI----LLGEPGVGKTAIVEALAqRIIKKDvpkslqNKKVIALDMSA 245
Cdd:cd19499 7 ERLHERVVGQDEAVKAVSDAIRRaraglSDPNRPIgsflFLGPTGVGKTELAKALA-ELLFGD------EDNLIRIDMSE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1204950885 246 LI----------AGAKYRGEFE-DRLkavVNEVIKSENIILFIDEIhtivgagaSEGSMDAANILKPALARGEL 308
Cdd:cd19499 80 YMekhsvsrligAPPGYVGYTEgGQL---TEAVRRKPYSVVLLDEI--------EKAHPDVQNLLLQVLDDGRL 142
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
204-285 |
3.54e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410928 [Multi-domain] Cd Length: 166 Bit Score: 38.94 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRiikkdvpkslQNKKVIALDMSALIAgaKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLTD--KWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
..
gi 1204950885 284 VG 285
Cdd:cd19520 107 LR 108
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
563-642 |
4.28e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 40.36 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 563 LEVEKH---LKESVIGQDKALSALARAikrnkaglnADNKPIGSFLFLGPTGVGKTQSAKALAKFLFDD--EKAMIRFDM 637
Cdd:PRK12402 4 LWTEKYrpaLLEDILGQDEVVERLSRA---------VDSPNLPHLLVQGPPGSGKTAAVRALARELYGDpwENNFTEFNV 74
|
....*
gi 1204950885 638 SEFME 642
Cdd:PRK12402 75 ADFFD 79
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
569-631 |
4.29e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 40.27 E-value: 4.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1204950885 569 LKESVIGQDKALSALARAIKRNKAGlNAdnkpigsFLFLGPTGVGKTQSAKALAKFLFDDEKA 631
Cdd:PRK07399 2 LFANLIGQPLAIELLTAAIKQNRIA-PA-------YLFAGPEGVGRKLAALCFIEGLLSQGSP 56
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
181-224 |
6.31e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 39.83 E-value: 6.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1204950885 181 VIGREEEIERLMQILIRKTKNNP----ILLGEPGVGKTAIVEALAQRI 224
Cdd:COG1474 28 LPHREEEIEELASALRPALRGERpsnvLIYGPTGTGKTAVAKYVLEEL 75
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
204-334 |
6.79e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 38.10 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 204 ILLGEPGVGKTAIVEALAQRIikkdvpkslqnkKVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTI 283
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES------------GSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1204950885 284 V---GAGASEGS----------MDAAnilkPALARGELHTIGATTLKEyrkyfEKDAALQRRFQ 334
Cdd:cd19509 104 LserGSGEHEASrrvkteflvqMDGV----LNKPEDRVLVLGATNRPW-----ELDEAFLRRFE 158
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
341-624 |
7.97e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 39.49 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 341 PSVNEALAMlrgIKEKLEihhnvtiNDsalvaAAKLSKRYIADR-FLPDKAIDL---IDEAAAELKMQIESEpsSLRKVR 416
Cdd:PRK05703 9 KDMREALKQ---IKEELG-------AD-----AVILSNKKVRKGgFLGKKLVEVtaaVDEDETPKKNPVLRE--EKRKPA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 417 KDIETLEVENEALKMENDEKNQKRLDEIAkeLANLKEKQNALNSQFENEKSVFDGISAKKKEIDLLKNEASLAKARGEFQ 496
Cdd:PRK05703 72 KSILSLQALLEKRPSRTNSQDALLQAENA--LPEWKKELEKPSEPKEEEPKAAAESKVVQKELDELRDELKELKNLLEDQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 497 KAAELEYGKIPSLEKEVeiledkWKKMSENGVllknqvDEDLVAGILSkwtgisvqkmLTSEKQKflEVEKHLKESVigq 576
Cdd:PRK05703 150 LSGLRQVERIPPEFAEL------YKRLKRSGL------SPEIAEKLLK----------LLLEHMP--PRERTAWRYL--- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1204950885 577 dkaLSALARAIKRNKAGLNADNKPIgsfLFLGPTGVGKTQS-AKALAKF 624
Cdd:PRK05703 203 ---LELLANMIPVRVEDILKQGGVV---ALVGPTGVGKTTTlAKLAARY 245
|
|
| COG1672 |
COG1672 |
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only]; |
182-279 |
9.16e-03 |
|
Predicted ATPase, archaeal AAA+ ATPase superfamily [General function prediction only];
Pssm-ID: 441278 [Multi-domain] Cd Length: 324 Bit Score: 39.13 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204950885 182 IGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIV-EALAQRI-IKKDVPKS--LQNKKVIALDMSALIAGAKYRGEFE 257
Cdd:COG1672 3 FDREEELEELEKLYESDGGELVVVYGRRRVGKTSLIkEFLKEKPaIYFDAREEseRESLRDFSEALAEALGDPLSKKEFE 82
|
90 100
....*....|....*....|....
gi 1204950885 258 DRLKA--VVNEVIKSENIILFIDE 279
Cdd:COG1672 83 SWEEAfeYLAELAEGKRLVIVIDE 106
|
|
| |
