|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
20-782 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1446.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 20 RDVVVYPHTVMPLFVGRTRSIKALEVAMAKDQKVFLVAQRDAKQDDPGQEGLFVIGTVATVLQLLKLPDGTLKVLVEGEY 99
Cdd:COG0466 20 RDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKVLVEGLQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 100 RAHLDEFIEVDEIHTAQVSLLEEEGVGERELEVLGRSLISQFEQYVKLNKKIPPEVLSSMAGTEDPSRLADSIAAHLSLK 179
Cdd:COG0466 100 RARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLADFIASHLPLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 180 TEDRQKLLEQANLRERLEQLMALLEFEIDLLQVEKRIRGRVKRQMEKSQREYYLNEQMKAIQKELGDLEDGGNELDELEK 259
Cdd:COG0466 180 IEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDDGEDEIEELRE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 260 RIKESGMTEEAHDKAMSELSKLKNMSPMSSEATVCRNYIDALISVPWKKRSKTRSDLSKAEDVLEADHYGLEEVKERILE 339
Cdd:COG0466 260 KIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 340 YLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEAEIRGHRRTYIGSMPGKIIQKLSKAEVK 419
Cdd:COG0466 340 YLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTK 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 420 NPLFLLDEIDKMAQDFRGDPASALLEVLDPEQNHTFNDHYLEVDYDLSDVMFIATANSL-NIPGPLLDRMEVIRIPGYTE 498
Cdd:COG0466 420 NPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAPLLDRMEIIELSGYTE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 499 DEKLNIAKRYLLPKQIKANGLKKNELAVEDEALISIIRHYTREAGVRSLEREISKVCRKVVKQILLKreDKETLKLTAKE 578
Cdd:COG0466 500 EEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEG--KKKKVTITPKN 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 579 LEDYLGVQRYRYGEAEEKDQVGLVTGLAWTEVGGELLTIEAATTKGKGKVQRTGKLGDVMQESIQAAVTVVRSRAEMLSI 658
Cdd:COG0466 578 LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 659 PEESFEKLDVHIHVPEGATPKDGPSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIRTV 738
Cdd:COG0466 658 DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTV 737
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 2546230300 739 LIPEENRRELKEIPENILKDLDVQPVRWIEDVLKVALTESPGDL 782
Cdd:COG0466 738 ILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPL 781
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
20-779 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1147.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 20 RDVVVYPHTVMPLFVGRTRSIKALEVAMAKDQKVFLVAQRDAKQDDPGQEGLFVIGTVATVLQLLKLPDGTLKVLVEGEY 99
Cdd:PRK10787 17 RDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 100 RAHLDEFIEVDEIHTAQVSLLEEEGVGERELEVLGRSLISQFEQYVKLNKKIPPEVLSSMAGTEDPSRLADSIAAHLSLK 179
Cdd:PRK10787 97 RARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 180 TEDRQKLLEQANLRERLEQLMALLEFEIDLLQVEKRIRGRVKRQMEKSQREYYLNEQMKAIQKELGDLEDGGNELDELEK 259
Cdd:PRK10787 177 LADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 260 RIKESGMTEEAHDKAMSELSKLKNMSPMSSEATVCRNYIDALISVPWKKRSKTRSDLSKAEDVLEADHYGLEEVKERILE 339
Cdd:PRK10787 257 KIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 340 YLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEAEIRGHRRTYIGSMPGKIIQKLSKAEVK 419
Cdd:PRK10787 337 YLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 420 NPLFLLDEIDKMAQDFRGDPASALLEVLDPEQNHTFNDHYLEVDYDLSDVMFIATANSLNIPGPLLDRMEVIRIPGYTED 499
Cdd:PRK10787 417 NPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTED 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 500 EKLNIAKRYLLPKQIKANGLKKNELAVEDEALISIIRHYTREAGVRSLEREISKVCRKVVKQILLKREDKEtLKLTAKEL 579
Cdd:PRK10787 497 EKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSLKH-IEINGDNL 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 580 EDYLGVQRYRYGEAEEKDQVGLVTGLAWTEVGGELLTIEAATTKGKGKVQRTGKLGDVMQESIQAAVTVVRSRAEMLSIP 659
Cdd:PRK10787 576 HDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGIN 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 660 EESFEKLDVHIHVPEGATPKDGPSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIRTVL 739
Cdd:PRK10787 656 PDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVL 735
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2546230300 740 IPEENRRELKEIPENILKDLDVQPVRWIEDVLKVALTESP 779
Cdd:PRK10787 736 IPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEP 775
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
20-775 |
0e+00 |
|
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273258 [Multi-domain] Cd Length: 775 Bit Score: 1024.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 20 RDVVVYPHTVMPLFVGRTRSIKALEVAMAKDQK-VFLVAQRDAKQDDPGQEGLFVIGTVATVLQLLKLPD---GTLKVLV 95
Cdd:TIGR00763 6 RRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPyLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtATYKVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 96 EGEYRAHLDEFIEVDEIHTAQVSLLEEEGVG--ERELEVLGRSLISQFEQYVKLNK--KIPPEVLSSMAGTEDPSRLADS 171
Cdd:TIGR00763 86 EGLRRIRIKELSDKGGYLVVRVDNLKEEPFDkdDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPGRLADF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 172 IAAHLSLK-TEDRQKLLEQANLRERLEQLMALLEFEIDLLQVEKRIRGRVKRQMEKSQREYYLNEQMKAIQKELGDLEDG 250
Cdd:TIGR00763 166 VAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 251 GNELDELEKRIKESGMTEEAHDKAMSELSKLKNMSPMSSEATVCRNYIDALISVPWKKRSKTRSDLSKAEDVLEADHYGL 330
Cdd:TIGR00763 246 KDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 331 EEVKERILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEAEIRGHRRTYIGSMPGKII 410
Cdd:TIGR00763 326 KKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRII 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 411 QKLSKAEVKNPLFLLDEIDKMAQDFRGDPASALLEVLDPEQNHTFNDHYLEVDYDLSDVMFIATANSLN-IPGPLLDRME 489
Cdd:TIGR00763 406 QGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPLLDRME 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 490 VIRIPGYTEDEKLNIAKRYLLPKQIKANGLKKNELAVEDEALISIIRHYTREAGVRSLEREISKVCRKVVKQILL----K 565
Cdd:TIGR00763 486 VIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekK 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 566 REDKETLKLTAKELEDYLGVQRYRYGEAEEKDQVGLVTGLAWTEVGGELLTIEAATTKGKGKVQRTGKLGDVMQESIQAA 645
Cdd:TIGR00763 566 KSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIA 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 646 VTVVRSRAEMLSIPEESFEKLDVHIHVPEGATPKDGPSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKE 725
Cdd:TIGR00763 646 LTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKE 725
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 2546230300 726 KLLAAHRGGIRTVLIPEENRRELKEIPENILKDLDVQPVRWIEDVLKVAL 775
Cdd:TIGR00763 726 KTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
316-496 |
7.80e-125 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 371.51 E-value: 7.80e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 316 LSKAEDVLEADHYGLEEVKERILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEAEIR 395
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 396 GHRRTYIGSMPGKIIQKLSKAEVKNPLFLLDEIDKMAQDFRGDPASALLEVLDPEQNHTFNDHYLEVDYDLSDVMFIATA 475
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 2546230300 476 NSL-NIPGPLLDRMEVIRIPGY 496
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
573-777 |
6.29e-121 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 362.33 E-value: 6.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 573 KLTAKELEDYLGVQRYRYGEAEEKDQVGLVTGLAWTEVGGELLTIEAATTKGKGKVQRTGKLGDVMQESIQAAVTVVRSR 652
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 653 AEMLSIPEESFEKLDVHIHVPEGATPKDGPSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHR 732
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2546230300 733 GGIRTVLIPEENRRELKEIPENILKDLDVQPVRWIEDVLKVALTE 777
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
20-204 |
4.13e-45 |
|
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.
Pssm-ID: 426647 [Multi-domain] Cd Length: 195 Bit Score: 160.58 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 20 RDVVVYPHTVMPLFVGRTRSIKALEVAMAKDQK--VFLVAQRDAKQDDPGQEGLFVIGTVATVLQLLKLPDGTLKVLVEG 97
Cdd:pfam02190 8 RNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTYKVLVEG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 98 EYRAHLDEFIEVDE-IHTAQVSLLEEEgvGERELEVLGRSLISQFEQYVKLNKKI-PPEVLSSMAGTEDPSRLADSIAAH 175
Cdd:pfam02190 88 LERVRIVELVKKEEpYLRAEVEDLPED--SDELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRLADLVAAI 165
|
170 180
....*....|....*....|....*....
gi 2546230300 176 LSLKTEDRQKLLEQANLRERLEQLMALLE 204
Cdd:pfam02190 166 LPLSPEEKQELLETLDVKERLEKVLELLN 194
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
355-496 |
3.43e-26 |
|
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: 104.21 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 355 LCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDeaeirghrrTYIGSMPGKIIQKLSKAEVKNP-LFLLDEIDKMA- 432
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAg 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2546230300 433 ------QDFRGDPASALLEVLDPEQNHTfndhylevdydlSDVMFIATANSL-NIPGPLLDRMEVIRIPGY 496
Cdd:pfam00004 72 srgsggDSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPdKLDPALLGRFDRIIEFPL 130
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
21-206 |
2.85e-23 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 98.02 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 21 DVVVYPHTVMPL--FVGRTRsikalevAMAKD----QKVFLVAQRDAKQDDPGQEGLFVIGTVATVLQLLKLPDGTLKVL 94
Cdd:COG2802 13 GAVLFPGGRLPLhiFEPRYL-------DMVRDclagDRPFGVVLIREGREVGGPPPLYDVGTLARITDFEELEDGRLDIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 95 VEGEYRAHLDEFIEVDE-IHTAQVSLLEEEGVGER--ELEVLGRSLISQFEQYVKLNKkippevLSSMAGTEDPSRLADS 171
Cdd:COG2802 86 LRGVQRFRILEELQEDDpYRVAEVEWLPDEPDLPVpeELEALRERLLRLLRRYPELAG------LEADPDLDDPEWLSNR 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2546230300 172 IAAHLSLKTEDRQKLLEQANLRERLEQLMALLEFE 206
Cdd:COG2802 160 LAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
611-774 |
7.45e-22 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 94.66 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 611 GGELLTIEA-ATTKGKGKV--QRTGKLGDVMQESIQAAVTVVRSRAEMlsipeeSFEKLDVHIHVPEGATPKDGPSAGIG 687
Cdd:COG1750 42 EGVVINITVtVTYPGSGRVyvSTSPLTGPDTQASARIAALVASLLAGV------DLSSYDVYISIESDSPIVGGPSAGGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 688 MCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIRTVLIPEENR-RELKEIPENILKDL------- 759
Cdd:COG1750 116 MTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAiLTGYNTQVGETVDLveygkel 195
|
170
....*....|....*..
gi 2546230300 760 --DVQPVRWIEDVLKVA 774
Cdd:COG1750 196 gvKVIEVSTIADALQYF 212
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
329-583 |
7.37e-14 |
|
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: 74.18 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 329 GLEEVKERILEYLAVQKRVKKLK-------GPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEaeirghrrtY 401
Cdd:COG0464 161 GLEEVKEELRELVALPLKRPELReeyglppPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 402 IGSMPGKIIQKLSKAEVKNP--LFlLDEIDKMAQDfRGdpasallEVLDPEQNHTFNdhYL--EVDYDLSDVMFIATANS 477
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPcvLF-IDEADALAGK-RG-------EVGDGVGRRVVN--TLltEMEELRSDVVVIAATNR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 478 -LNIPGPLLDRM-EVIRIPGYTEDEKLNIAKRYLLPKQIKANglkknelaVEDEALISIIRHYTreaGvrsleREISKVC 555
Cdd:COG0464 301 pDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDED--------VDLEELAEATEGLS---G-----ADIRNVV 364
|
250 260
....*....|....*....|....*...
gi 2546230300 556 RKVVKQILlkREDKETlkLTAKELEDYL 583
Cdd:COG0464 365 RRAALQAL--RLGREP--VTTEDLLEAL 388
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
333-476 |
1.28e-12 |
|
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: 66.15 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 333 VKERILEYLAVQKRVKKL------KGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEAeirghrRTYIGSMP 406
Cdd:cd19481 1 LKASLREAVEAPRRGSRLrryglgLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2546230300 407 GKIIQKLSKAevKNPLFLLDEIDKMAQDfRGDPA---------SALLEVLDPEQNhtfndhylevdydLSDVMFIATAN 476
Cdd:cd19481 75 RKIFERARRL--APCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATN 137
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
334-496 |
2.66e-12 |
|
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: 65.25 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 334 KERILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKATNRK---FLRMALGGVRDEAEIRGHRRTYIgsmpgKII 410
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELFGHFL-----VRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 411 QKLSKAEVKNPLFLLDEIDKMAQDFRgdpaSALLEVLdpeqnHTFNDHYLEVDydlsDVMFIATANSLN---IPGPLLDR 487
Cdd:cd00009 76 LFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVL-----ETLNDLRIDRE----NVRVIGATNRPLlgdLDRALYDR 142
|
....*....
gi 2546230300 488 MEVIRIPGY 496
Cdd:cd00009 143 LDIRIVIPL 151
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
326-597 |
5.80e-11 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 63.36 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 326 DHYGLEEVKE---RILEYLAVQKRVKKLKGPV---LCLVGPPGVGKTSLGQSIAKATNRKFLRMALGGVRDEaeirghrr 399
Cdd:COG1223 3 DVVGQEEAKKklkLIIKELRRRENLRKFGLWPprkILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 400 tYIGSMPGKIIQKLSKAEVKNPLFLLDEIDKMAQDfRGDPAsallevLDPEQNHTFNDHYLEVDYDLSDVMFIATANSLN 479
Cdd:COG1223 75 -YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-RGDQN------DVGEVKRVVNALLQELDGLPSGSVVIAATNHPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 480 ipgpLLDRM------EVIRIPGYTEDEKLNIAKRYLlpkqikanglkkNELAVEDEALISIIrhytreagVRSLE----R 549
Cdd:COG1223 147 ----LLDSAlwrrfdEVIEFPLPDKEERKEILELNL------------KKFPLPFELDLKKL--------AKKLEglsgA 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2546230300 550 EISKVCRKVVKQILLkrEDKEtlKLTAKELEDYLGVQRYRYGEAEEKD 597
Cdd:COG1223 203 DIEKVLKTALKKAIL--EDRE--KVTKEDLEEALKQRKERKKEPKKEG 246
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
682-775 |
1.03e-09 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 61.60 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 682 PSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIRTVLIPEENRRELKEipenilKDLDV 761
Cdd:COG1066 366 PAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGEIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKLKP------KGIEI 439
|
90
....*....|....
gi 2546230300 762 QPVRWIEDVLKVAL 775
Cdd:COG1066 440 IGVSTLEEALEALF 453
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
359-536 |
1.06e-09 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 61.25 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 359 GPPGVGKTSLGQSIAKATNRKFLRM--ALGGVrdeAEIRghrrtyigsmpgKIIQ--KLSKAEVKNPLFLLDEI---DKM 431
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEeaRQRRSAGRRTILFIDEIhrfNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 432 AQDfrgdpasALLEVLdpEQNHtfndhylevdydlsdVMFIA--TAN-SLNIPGPLLDRMEVIRIPGYTEDEKLNIAKRY 508
Cdd:PRK13342 108 QQD-------ALLPHV--EDGT---------------ITLIGatTENpSFEVNPALLSRAQVFELKPLSEEDIEQLLKRA 163
|
170 180
....*....|....*....|....*...
gi 2546230300 509 LlpkqikaNGLKKNELAVEDEALISIIR 536
Cdd:PRK13342 164 L-------EDKERGLVELDDEALDALAR 184
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
355-488 |
1.80e-09 |
|
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: 56.53 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 355 LCLVGPPGVGKTSLGQSIAKAT-NRKFLRMALGgvRD--EAEIRGHRRtYIGSMPGKIIQKLSKAEVKNPLFLLDEIDKM 431
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLT--RDttEEDLFGRRN-IDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2546230300 432 AQDFrgdpASALLEVLDPEQNHTfNDHYLEVDYDLSDVMFIATANSLNIPG-----PLLDRM 488
Cdd:pfam07728 79 NPDV----LNSLLSLLDERRLLL-PDGGELVKAAPDGFRLIATMNPLDRGLnelspALRSRF 135
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
359-536 |
1.87e-09 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 60.84 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 359 GPPGVGKTSLGQSIAKATNRKFLRM--ALGGVrdeAEIRghrrtyigsmpgKIIQ--KLSKAEVKNPLFLLDEI---DKM 431
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 432 AQDfrgdpasALLEVLdpEQNHtfndhylevdydlsdVMFIA--TAN-SLNIPGPLLDRMEVIRIPGYTEDEKLNIAKRY 508
Cdd:COG2256 121 QQD-------ALLPHV--EDGT---------------ITLIGatTENpSFEVNSALLSRCRVFVLKPLSEEDLEQLLERA 176
|
170 180
....*....|....*....|....*...
gi 2546230300 509 LlpkQIKANGLKKNELAVEDEALISIIR 536
Cdd:COG2256 177 L---ADDERGLGGYKLELDDEALEALAR 201
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
321-571 |
2.76e-09 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 59.63 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 321 DVLEADHYGLEEVKERILEYLAV-QKRVKKL--------KGpVLcLVGPPGVGKTSLGQSIAKATNRKFLRMALggvrde 391
Cdd:COG1222 74 DVTFDDIGGLDEQIEEIREAVELpLKNPELFrkygieppKG-VL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 392 AEIrghRRTYIGSMPGKIIQKLSKAEVKNP--LFlLDEIDKMAQDfRGDPAS---------ALLEVLDpeqnhtfndhyl 460
Cdd:COG1222 146 SEL---VSKYIGEGARNVREVFELAREKAPsiIF-IDEIDAIAAR-RTDDGTsgevqrtvnQLLAELD------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 461 EVDyDLSDVMFIATANSLNI-------PGPlLDRmeVIRIPGYTEDEKLNIAKRYLLPKQIkANGLKKNELAVEDEALI- 532
Cdd:COG1222 209 GFE-SRGDVLIIAATNRPDLldpallrPGR-FDR--VIEVPLPDEEAREEILKIHLRDMPL-ADDVDLDKLAKLTEGFSg 283
|
250 260 270
....*....|....*....|....*....|....*....
gi 2546230300 533 SIIRHYTREAGVRSLEREISKVCRKVVKQILLKREDKET 571
Cdd:COG1222 284 ADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKVKKKTE 322
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
329-507 |
5.47e-09 |
|
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: 58.26 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 329 GLEEVKERILeyLAVqkrvkKLKGPVLcLVGPPGVGKTSLGQSIAKATNRKFLRMalggvrdeaeirghrRTYIGSMPGK 408
Cdd:COG0714 16 GQEELIELVL--IAL-----LAGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 409 II------QKLSKAE-VKNPLF----LLDEIDkmaqdfRGDPA--SALLEVLDpeqnhtfnDHYLEVD---YDLSDVMF- 471
Cdd:COG0714 73 ILgtyiydQQTGEFEfRPGPLFanvlLADEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLv 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2546230300 472 IATANSL------NIPGPLLDRMEV-IRIpGY-TEDEKLNIAKR 507
Cdd:COG0714 139 IATQNPIeqegtyPLPEAQLDRFLLkLYI-GYpDAEEEREILRR 181
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
704-773 |
4.88e-08 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 55.59 E-value: 4.88e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2546230300 704 DVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIRTVLIPEENRRELKE-IPEnilkDLDVQPVRWIEDVLKV 773
Cdd:COG3480 265 KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAVGtIPT----GLKVVPVDTLDDALDA 331
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-488 |
3.60e-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: 50.45 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 351 KGPVLCLVGPPGVGKTSLGQSIAKATNRKFLRM-------ALGGVRDEAEIRGHRRTYIGSMPGKIIQKL-SKAEVKNP- 421
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLAlALARKLKPd 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2546230300 422 LFLLDEIDKMAqdfrgDPASALLEVLDPEQNHTFNDHYLEvdydlsDVMFIATANSLNIPGPLLDRM 488
Cdd:smart00382 81 VLILDEITSLL-----DAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPALLRR 136
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
680-748 |
1.03e-06 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 52.26 E-value: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2546230300 680 DGPSAGIGMCTALVSVYTSIPVRSDVAMTGEITLRGEVLPIGGLKEKL-----LAAHRG--GIRTVLIPEENRREL 748
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARGltGKQGVIIPAANVKNL 667
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
325-494 |
1.20e-05 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 48.88 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 325 ADHYGLEEVKERI---LEYLAVQKRVKKLKGPV---LCLVGPPGVGKTSLGQSIAKATNRKFLRMAlggVRDEAEIrghr 398
Cdd:PRK10733 152 ADVAGCDEAKEEVaelVEYLREPSRFQKLGGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM---- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 399 rtYIGSMPGKIIQKLSKAEVKNP-LFLLDEIDKMAQDfRGdpasALLEVLDPEQNHTFNDHYLEVD-YDLSD-VMFIATA 475
Cdd:PRK10733 225 --FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGRQ-RG----AGLGGGHDEREQTLNQMLVEMDgFEGNEgIIVIAAT 297
|
170 180
....*....|....*....|....*
gi 2546230300 476 NSLNIPGPLL------DRMEVIRIP 494
Cdd:PRK10733 298 NRPDVLDPALlrpgrfDRQVVVGLP 322
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
354-491 |
3.32e-05 |
|
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: 45.25 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 354 VLCLVGPPGVGKTSLGQSIAKA---TNRKFLRMALGgvrdeAEIRGHR-RTYIGSMPGKI----IQKLSKAEVKNP--LF 423
Cdd:cd19499 43 SFLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMS-----EYMEKHSvSRLIGAPPGYVgyteGGQLTEAVRRKPysVV 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2546230300 424 LLDEIDKMAQDFRGdpasALLEVLDpeqNHTFNDHYlEVDYDLSDVMFIATANslNIPGPLLDRMEVI 491
Cdd:cd19499 118 LLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSN--HFRPEFLNRIDEI 175
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
305-539 |
7.26e-05 |
|
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 188437 [Multi-domain] Cd Length: 557 Bit Score: 46.38 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 305 PWKKRS-KTRSDLS-------KAEDVLEAD-----HYGLEEVKERILEY---LAVQKRVKKLKGPV------LCLVGPPG 362
Cdd:TIGR03922 243 PWDPSSaPSRAEFVdpaaaerKAKLLAEAEaelaeQIGLERVKRQVAALkssTAMALARAERGLPVaqtsnhMLFAGPPG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 363 VGKTSLGQSIAKatnrkfLRMALGGVRDEAEIRGHRRTYIGSMPGKIIQKLSK---AEVKNPLFlLDEIDKMAQDFRGDP 439
Cdd:TIGR03922 323 TGKTTIARVVAK------IYCGLGVLRKPLVREVSRADLIGQYIGESEAKTNEiidSALGGVLF-LDEAYTLVETGYGQK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 440 asallevlDPEQNHTFNDHYLEVDYDLSDVMFIATANSLNIpgpllDRM------------EVIRIPGYTEDEKLNIAKR 507
Cdd:TIGR03922 396 --------DPFGLEAIDTLLARMENDRDRLVVIGAGYRKDL-----DKFlevneglrsrftRVIEFPSYSPDELVEIARR 462
|
250 260 270
....*....|....*....|....*....|..
gi 2546230300 508 YllpkqikangLKKNELAVEDEALISIIRHYT 539
Cdd:TIGR03922 463 M----------ATERDSVLDDAAADALLEAAT 484
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
268-374 |
9.44e-05 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 45.63 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 268 EEAHDKAMSELSKLKNM---------SPMSSEATVCRNYIDALIsvpwkkrsktRSDLSK--AEDVLE--ADHYGLEEVK 334
Cdd:COG1419 73 EEELEELRRELAELKELleeqlsglaGESARLPPELAELLERLL----------EAGVSPelARELLEklPEDLSAEEAW 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2546230300 335 ERILEYLAvqKRVKKLKGP------VLCLVGPPGVGKTSlgqSIAK 374
Cdd:COG1419 143 RALLEALA--RRLPVAEDPlldeggVIALVGPTGVGKTT---TIAK 183
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
325-384 |
1.35e-04 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410909 [Multi-domain] Cd Length: 171 Bit Score: 43.38 E-value: 1.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2546230300 325 ADHYGLEEVKERILEYLAVQKRVKK--------LKGpVLcLVGPPGVGKTSLGQSIAKATNRKFLRMA 384
Cdd:cd19501 4 KDVAGCEEAKEELKEVVEFLKNPEKftklgakiPKG-VL-LVGPPGTGKTLLAKAVAGEAGVPFFSIS 69
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
20-65 |
2.46e-04 |
|
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.
Pssm-ID: 197740 [Multi-domain] Cd Length: 92 Bit Score: 40.88 E-value: 2.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2546230300 20 RDVVVYPHTVMPLFVGRTRSIKALEVAMAKDQK--VFLVAQRDAKQDD 65
Cdd:smart00464 8 RRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyvIVFLLQDDPTETP 55
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
325-519 |
8.85e-04 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 42.29 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 325 ADHYGLEEVKERILEYLAVQKRVKKLKGPVLcLVGPPGVGKTSLGQSIAKATNRKfLRMALGGVRDEaeirghrrtyigs 404
Cdd:TIGR00635 4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 405 mPGKIIQKLSKAEVKNPLFlLDEIDKMAQdfrgdpasALLEVLDPeqnhTFNDHYLE-----------VDYDLSDVMFI- 472
Cdd:TIGR00635 69 -PGDLAAILTNLEEGDVLF-IDEIHRLSP--------AVEELLYP----AMEDFRLDivigkgpsarsVRLDLPPFTLVg 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2546230300 473 ATANSLNIPGPLLDRMEVI-RIPGYTEDEKLNIAKRY--LLPKQIKANGL 519
Cdd:TIGR00635 135 ATTRAGMLTSPLRDRFGIIlRLEFYTVEELAEIVSRSagLLNVEIEPEAA 184
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
153-374 |
1.11e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 42.19 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 153 PEVLSSMAGTEDPSRLADSIAAhLSLKTEDRQKLLEQANLRERLEQLMALLEFEIDLLQVEKRIRGRVKRQMEKSQREY- 231
Cdd:PRK05703 55 ETPKKNPVLREEKRKPAKSILS-LQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELd 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 232 YLNEQMKAIQK----ELGDLEDGGN---ELDELEKRIKESGMTEEAHDKAMSELSklknmspmsseatvcrnyidalisv 304
Cdd:PRK05703 134 ELRDELKELKNlledQLSGLRQVERippEFAELYKRLKRSGLSPEIAEKLLKLLL------------------------- 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 305 pwkkrsktrsdlskaEDVLEADHYGLEEVKERILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSlgqSIAK 374
Cdd:PRK05703 189 ---------------EHMPPRERTAWRYLLELLANMIPVRVEDILKQGGVVALVGPTGVGKTT---TLAK 240
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
357-476 |
1.96e-03 |
|
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: 39.87 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 357 LVGPPGVGKTSLGQSIAKatnrkflrmaLGGVRDEAEIRGHRRTY---------IGSMPGKIIQ----KLSKAEVKNPLF 423
Cdd:pfam07724 8 FLGPTGVGKTELAKALAE----------LLFGDERALIRIDMSEYmeehsvsrlIGAPPGYVGYeeggQLTEAVRRKPYS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2546230300 424 --LLDEIDKMAQD-FRgdpasALLEVLDpeqNHTFNDHYlEVDYDLSDVMFIATAN 476
Cdd:pfam07724 78 ivLIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGN 124
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
167-290 |
2.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 167 RLADSI--AAHLSLKTEDRQKLLEQanlRERLEQLMALLEFEI-----DLLQVEKRIRgrvkrqmeksQREYYLNEQMKA 239
Cdd:PRK12704 38 EEAKRIleEAKKEAEAIKKEALLEA---KEEIHKLRNEFEKELrerrnELQKLEKRLL----------QKEENLDRKLEL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2546230300 240 IQKELGDLEDGGNELDELEKRIKEsgMTEEAHDKAMSELSKLKNMSPMSSE 290
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEK--KEEELEELIEEQLQELERISGLTAE 153
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
257-596 |
2.14e-03 |
|
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: 41.43 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 257 LEKRIKESGMTEEAHDKAMSELSKLKnmspmsseaTVCRNYIDALISVpwkKRSKTRSDLSKAEDVLEADHYGLEEVKER 336
Cdd:TIGR01243 397 LRRFIREGKINFEAEEIPAEVLKELK---------VTMKDFMEALKMV---EPSAIREVLVEVPNVRWSDIGGLEEVKQE 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 337 ILEY----LAVQKRVKKL-----KGpvLCLVGPPGVGKTSLGQSIAKATNRKFLrmalggvrdeaEIRGHR--RTYIGSM 405
Cdd:TIGR01243 465 LREAvewpLKHPEIFEKMgirppKG--VLLFGPPGTGKTLLAKAVATESGANFI-----------AVRGPEilSKWVGES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 406 PGKIIQKLSKAEVKNP-LFLLDEIDKMAQDFRGDPASALlevldpeQNHTFNDHYLEVD--YDLSDVMFIATANSLNIPG 482
Cdd:TIGR01243 532 EKAIREIFRKARQAAPaIIFFDEIDAIAPARGARFDTSV-------TDRIVNQLLTEMDgiQELSNVVVIAATNRPDILD 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 483 PLLDRM----EVIRIPGYTEDEKLNIAKRYllpkqikangLKKNELA--VEDEALISIIRHYTREagvrslerEISKVCR 556
Cdd:TIGR01243 605 PALLRPgrfdRLILVPPPDEEARKEIFKIH----------TRSMPLAedVDLEELAEMTEGYTGA--------DIEAVCR 666
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2546230300 557 KVVKQIL---LKREDKETLKLTAKELEDYLGVQRYRYGEAEEK 596
Cdd:TIGR01243 667 EAAMAALresIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKK 709
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
355-381 |
2.74e-03 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 39.34 E-value: 2.74e-03
10 20
....*....|....*....|....*..
gi 2546230300 355 LCLVGPPGVGKTSLGQSIAKATNRKFL 381
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
357-381 |
2.82e-03 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 39.08 E-value: 2.82e-03
10 20
....*....|....*....|....*
gi 2546230300 357 LVGPPGVGKTSLGQSIAKATNRKFL 381
Cdd:cd00464 4 LIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
162-202 |
3.21e-03 |
|
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.
Pssm-ID: 197740 [Multi-domain] Cd Length: 92 Bit Score: 37.42 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2546230300 162 TEDPSRLADSIAAHLSLKTEDRQKLLEQANLRERLEQLMAL 202
Cdd:smart00464 52 TETPEPLSDTIAALMPLELHEKQELLELEGTNKRLEKVIKL 92
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
350-381 |
3.33e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 39.40 E-value: 3.33e-03
10 20 30
....*....|....*....|....*....|..
gi 2546230300 350 LKGPVLCLVGPPGVGKTSLGQSIAKATNRKFL 381
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
355-390 |
4.19e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 40.81 E-value: 4.19e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2546230300 355 LCLVGPPGVGKTSLGQSIAKATNRKFLRM--ALGGVRD 390
Cdd:PRK13341 55 LILYGPPGVGKTTLARIIANHTRAHFSSLnaVLAGVKD 92
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
330-487 |
4.33e-03 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410937 [Multi-domain] Cd Length: 159 Bit Score: 38.63 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 330 LEEVKERILEYLAVQKR--VKKLKGpvLCLVGPPGVGKTSLGQSIAKATNRKFLrmalggvrdeaEIRGHR--RTYIGSM 405
Cdd:cd19529 5 LKEAVEWPLLKPEVFKRlgIRPPKG--ILLYGPPGTGKTLLAKAVATESNANFI-----------SVKGPEllSKWVGES 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 406 PGKIIQKLSKAEVKNP-LFLLDEIDKMAQDFRGDPASALLEvldpeqnHTFNDHYLEVD--YDLSDVMFIATANSLNIPG 482
Cdd:cd19529 72 EKAIREIFRKARQVAPcVIFFDEIDSIAPRRGTTGDSGVTE-------RVVNQLLTELDglEEMNGVVVIAATNRPDIID 144
|
....*
gi 2546230300 483 PLLDR 487
Cdd:cd19529 145 PALLR 149
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
329-432 |
5.14e-03 |
|
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: 38.43 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 329 GLEEVKERILEYLAVQKR---------VKKLKGpVLcLVGPPGVGKTSLGQSIAKATNRKFLrmalggVRDEAEIrghrr 399
Cdd:cd19503 4 GLDEQIASLKELIELPLKypelfralgLKPPRG-VL-LHGPPGTGKTLLARAVANEAGANFL------SISGPSI----- 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 2546230300 400 tyIGSMPGKIIQKL----SKAEVKNP-LFLLDEIDKMA 432
Cdd:cd19503 71 --VSKYLGESEKNLreifEEARSHAPsIIFIDEIDALA 106
|
|
| AAA_PrkA |
pfam08298 |
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ... |
325-375 |
5.25e-03 |
|
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.
Pssm-ID: 116881 Cd Length: 358 Bit Score: 39.75 E-value: 5.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2546230300 325 ADHYGLEEVKERILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSLGQSIAKA 375
Cdd:pfam08298 58 ADFFGMEETIERIVNYFRHAAQGLEERKQILYLLGPVGGGKSSLAERLKKL 108
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
359-477 |
5.55e-03 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 40.21 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 359 GPPGVGKTSLGQSIAKATNRKFLRMalggvrDEAEIrGHRRT---YIGSMPGKIIQK----LSKAEVKNP--LFLLDEID 429
Cdd:PRK11034 495 GPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVGFDqgglLTDAVIKHPhaVLLLDEIE 567
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2546230300 430 KMAQDFrgdpASALLEVLDpeqNHTFNDHYLEvDYDLSDVMFIATANS 477
Cdd:PRK11034 568 KAHPDV----FNLLLQVMD---NGTLTDNNGR-KADFRNVVLVMTTNA 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-282 |
5.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 169 ADSIAAHLSLKTEDRQKL-LEQANLRERLEQLMALLEF---EIDLLQVEKRIRgrvkrqmeksqreyylneqmkAIQKEL 244
Cdd:COG4913 619 LAELEEELAEAEERLEALeAELDALQERREALQRLAEYswdEIDVASAEREIA---------------------ELEAEL 677
|
90 100 110
....*....|....*....|....*....|....*...
gi 2546230300 245 GDLEDGGNELDELEKRIKEsgmTEEAHDKAMSELSKLK 282
Cdd:COG4913 678 ERLDASSDDLAALEEQLEE---LEAELEELEEELDELK 712
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
132-264 |
8.71e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 132 VLGRSLISQFEQYVKLNKKIppEVLSSMAGTED--PSRLADSIA---AHLSLKTEDRQKL----LEQANLRERLEQLMAL 202
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQI--AELADLLSLERqgNQDLQDSVAnlrASLSAAEAERSRLqallAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2546230300 203 LEFEIDllqVEKRIRGRVKRQMEksqreyYLNEQMKAIQKELGDLEDGgneLDELEKRIKES 264
Cdd:PRK09039 121 LAQELD---SEKQVSARALAQVE------LLNQQIAALRRQLAALEAA---LDASEKRDRES 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-278 |
9.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 181 EDRQKLLEQA--NLRERLEQL-MALLEFEIDLLQVEKRIRGRVKRQME-KSQREYylneqmKAIQKELGDLEDggnELDE 256
Cdd:COG1579 37 EDELAALEARleAAKTELEDLeKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEY------EALQKEIESLKR---RISD 107
|
90 100
....*....|....*....|..
gi 2546230300 257 LEKRIKESGMTEEAHDKAMSEL 278
Cdd:COG1579 108 LEDEILELMERIEELEEELAEL 129
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
108-263 |
9.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 108 EVDEIHTAQVSLLEEEGVGERELEVLGRSLISQFEQYVKLNKKI-------PPEVLSSmagTEDPSRLADSIAAHLSLKT 180
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrqpPLALLLS---PEDFLDAVRRLQYLKYLAP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2546230300 181 EDRQKLLEQANLRERLEQLMALLEFEIDLLQVEKRIRGRVKRQMEKSQREY-----YLNEQMKAIQKELGDLEDGGNELD 255
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERqkllaRLEKELAELAAELAELQQEAEELE 226
|
....*...
gi 2546230300 256 ELEKRIKE 263
Cdd:COG4942 227 ALIARLEA 234
|
|
| |
