|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
33-799 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1343.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 33 PLLPLRDMVMFPRMVTPLFVGRDRSIEAIEVALETGEPLITVAQRDVDVAEPGPEDLFTFGTEVEIGRMLRMPDGTISML 112
Cdd:COG0466 15 PLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 113 SQGLRRLQIVEYVQLEPYIRVRALPIYEVADKTPLTEALMRAVLALFEKVVQLNRSLPQDAYVFAMNVDGPGWLADLMAQ 192
Cdd:COG0466 95 VEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLADFIAS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 193 VLDLEVTERQEVLETIAPASRLQYISVLLAKELDVLELEDHIHAQVQQELDKSQREYFLREQMKVIQSELGEGDVYTQEV 272
Cdd:COG0466 175 HLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDDGEDEI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 273 NELRDRIAEMELPDETRARADKELGRLSSMPPMSPETGMIRTYLDWLIDLPWSETTEDNLDVGHVDQVLESRHYGLPKAK 352
Cdd:COG0466 255 EELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 353 DRILEYIAVRRLAaDKMRSPILCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEAEIRGHRRTYIGSLPGRIIQTM 432
Cdd:COG0466 335 ERILEYLAVRKLK-KKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 433 RRAGTLNPLFMLDEVDKIGADFRGDPAAALLEVLDPEQNFAFSDHYLEVPYDLSKVLFITTANILSPVPPALQDRMEVIE 512
Cdd:COG0466 414 KKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIE 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 513 FPGYIDEEKLEIARRFLIPRQLEEHGLDEHPVAFTKSALQSLIREYTYEAGVRNLEREIASLCRKVARRLAEGKSPPQRI 592
Cdd:COG0466 494 LSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTI 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 593 QANMLAKHLGPPQFIRNMAEEHDGVGIAMGVAWTEAGGDLTPVEVALMPGKGNLLLTGRLGDIMQESAQAALSYTRSRSE 672
Cdd:COG0466 574 TPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 673 ELGIEAGVFDQTDIHVHLPEGAIPKDGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLPVGGLKEKMLAAYRAG 752
Cdd:COG0466 654 ELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAG 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1490707203 753 IETIIIPKSNKKDLDEIPRRVQRKLNIVLVEQMDKVLDVALISFPSP 799
Cdd:COG0466 734 IKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEP 780
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
33-793 |
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: 989.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 33 PLLPLRDMVMFPRMVTPLFVGRDRSIEAIEVALETGEPLITV-AQRDVDVAEPGPEDLFTFGTEVEIGRMLRMPD---GT 108
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLfLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 109 ISMLSQGLRRLQIVEYVQLEPYIRVRALPIYE--VADKTPLTEALMRAVLALFEKVVQLNRS--LPQDAYVFAMNVDGPG 184
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKLfrEQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 185 WLADLMAQVLDL-EVTERQEVLETIAPASRLQYISVLLAKELDVLELEDHIHAQVQQELDKSQREYFLREQMKVIQSELG 263
Cdd:TIGR00763 161 RLADFVAASLQLkEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 264 EGDVYTQEVNELRDRIAEMELPDETRARADKELGRLSSMPPMSPETGMIRTYLDWLIDLPWSETTEDNLDVGHVDQVLES 343
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 344 RHYGLPKAKDRILEYIAVRRLAaDKMRSPILCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEAEIRGHRRTYIGS 423
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLR-GKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 424 LPGRIIQTMRRAGTLNPLFMLDEVDKIGADFRGDPAAALLEVLDPEQNFAFSDHYLEVPYDLSKVLFITTANILSPVPPA 503
Cdd:TIGR00763 400 MPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 504 LQDRMEVIEFPGYIDEEKLEIARRFLIPRQLEEHGLDEHPVAFTKSALQSLIREYTYEAGVRNLEREIASLCRKVARRLA 583
Cdd:TIGR00763 480 LLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 584 EGKS------PPQRIQANMLAKHLGPPQFIRNMAEEHDGVGIAMGVAWTEAGGDLTPVEVALMPGKGNLLLTGRLGDIMQ 657
Cdd:TIGR00763 560 EQGEkkkseaESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 658 ESAQAALSYTRSRSEELGIEAGVFDQTDIHVHLPEGAIPKDGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLP 737
Cdd:TIGR00763 640 ESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLP 719
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490707203 738 VGGLKEKMLAAYRAGIETIIIPKSNKKDLDEIPRRVQRKLNIVLVEQMDKVLDVAL 793
Cdd:TIGR00763 720 IGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
30-798 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 806.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 30 IEAPLLPLRDMVMFPRMVTPLFVGRDRSIEAIEVALETGEPLITVAQRDVDVAEPGPEDLFTFGTEVEIGRMLRMPDGTI 109
Cdd:PRK10787 9 IEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 110 SMLSQGLRRLQIVEYVQLEPYIRVRA--LPIYEVADKTplTEALMRAVLALFEKVVQLNRSLPQDAYVFAMNVDGPGWLA 187
Cdd:PRK10787 89 KVLVEGLQRARISALSDNGEHFSAKAeyLESPTIDERE--QEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 188 DLMAQVLDLEVTERQEVLETIAPASRLQYISVLLAKELDVLELEDHIHAQVQQELDKSQREYFLREQMKVIQSELGEGDV 267
Cdd:PRK10787 167 DTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 268 YTQEVNELRDRIAEMELPDETRARADKELGRLSSMPPMSPETGMIRTYLDWLIDLPWSETTEDNLDVGHVDQVLESRHYG 347
Cdd:PRK10787 247 APDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 348 LPKAKDRILEYIAVRRLAAdKMRSPILCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEAEIRGHRRTYIGSLPGR 427
Cdd:PRK10787 327 LERVKDRILEYLAVQSRVN-KIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 428 IIQTMRRAGTLNPLFMLDEVDKIGADFRGDPAAALLEVLDPEQNFAFSDHYLEVPYDLSKVLFITTANILSpVPPALQDR 507
Cdd:PRK10787 406 LIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 508 MEVIEFPGYIDEEKLEIARRFLIPRQLEEHGLDEHPVAFTKSALQSLIREYTYEAGVRNLEREIASLCRKVARRLAEGKS 587
Cdd:PRK10787 485 MEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKS 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 588 PPQ-RIQANMLAKHLGPPQFIRNMAEEHDGVGIAMGVAWTEAGGDLTPVEVALMPGKGNLLLTGRLGDIMQESAQAALSY 666
Cdd:PRK10787 565 LKHiEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTV 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 667 TRSRSEELGIEAGVFDQTDIHVHLPEGAIPKDGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLPVGGLKEKML 746
Cdd:PRK10787 645 VRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLL 724
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1490707203 747 AAYRAGIETIIIPKSNKKDLDEIPRRVQRKLNIVLVEQMDKVLDVALISFPS 798
Cdd:PRK10787 725 AAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPS 776
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
334-516 |
3.06e-118 |
|
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: 354.56 E-value: 3.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 334 VGHVDQVLESRHYGLPKAKDRILEYIAVRRLAAdKMRSPILCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEAEI 413
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKG-SMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 414 RGHRRTYIGSLPGRIIQTMRRAGTLNPLFMLDEVDKIGADFRGDPAAALLEVLDPEQNFAFSDHYLEVPYDLSKVLFITT 493
Cdd:cd19500 80 RGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIAT 159
|
170 180
....*....|....*....|...
gi 1490707203 494 ANILSPVPPALQDRMEVIEFPGY 516
Cdd:cd19500 160 ANSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
592-794 |
9.06e-108 |
|
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: 328.43 E-value: 9.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 592 IQANMLAKHLGPPQFIRNMAEEHDGVGIAMGVAWTEAGGDLTPVEVALMPGKGNLLLTGRLGDIMQESAQAALSYTRSRS 671
Cdd:pfam05362 2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 672 EELGIEAGVFDQTDIHVHLPEGAIPKDGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLPVGGLKEKMLAAYRA 751
Cdd:pfam05362 82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490707203 752 GIETIIIPKSNKKDLDEIPRRVQRKLNIVLVEQMDKVLDVALI 794
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
31-223 |
1.12e-46 |
|
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: 164.82 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 31 EAPLLPLRDMVMFPRMVTPLFVGRDRSIEAIEVALETGEP--LITVAQRDVDVAEPGPEDLFTFGTEVEIGRMLRMPDGT 108
Cdd:pfam02190 1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 109 ISMLSQGLRRLQIVEYV-QLEPYIRVRALPIyeVADKTPLTEALMRAVLALFEKVVQLNRSL-PQDAYVFAMNVDGPGWL 186
Cdd:pfam02190 81 YKVLVEGLERVRIVELVkKEEPYLRAEVEDL--PEDSDELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490707203 187 ADLMAQVLDLEVTERQEVLETIAPASRLQYISVLLAK 223
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
374-516 |
2.17e-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: 104.98 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 374 LCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDeaeirghrrTYIGSLPGRIIQTMRRAGTLNP-LFMLDEVDKI-- 450
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490707203 451 -----GADFRGDPAAALLEVLDPEQNfafsdhylevpyDLSKVLFITTANILSPVPPALQDRMEVIEFPGY 516
Cdd:pfam00004 72 srgsgGDSESRRVVNQLLTELDGFTS------------SNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
619-794 |
8.03e-20 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 88.50 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 619 IAMGVAWTEAG--GDLTpVEVAlMPGKGNLLLTGR--LGDIMQESAQAALSYTrsrseelGIEAGV-FDQTDIHVHLPEG 693
Cdd:COG1750 33 YAPAVSGTGEGvvINIT-VTVT-YPGSGRVYVSTSplTGPDTQASARIAALVA-------SLLAGVdLSSYDVYISIESD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 694 AIPKDGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLPVGGLKEKMLAAYRAGIETIIIPKSNKkdLDEIPRRV 773
Cdd:COG1750 104 SPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQA--ILTGYNTQ 181
|
170 180
....*....|....*....|.
gi 1490707203 774 QRKlnIVLVEQMDKVLDVALI 794
Cdd:COG1750 182 VGE--TVDLVEYGKELGVKVI 200
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
351-513 |
1.72e-18 |
|
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: 83.10 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 351 AKDRILEYIAVRRLAADKMRSPI-----LCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEaeirghrrtYIGSLP 425
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLglpkgILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK---------YVGESE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 426 GRIIQTMRRAGTLNP-LFMLDEVDKIGADfRGDPA---------AALLEVLDPEQNfafsdhylevpydLSKVLFITTAN 495
Cdd:cd19481 72 KNLRKIFERARRLAPcILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATN 137
|
170 180
....*....|....*....|.
gi 1490707203 496 ILSPVPPALQDR---MEVIEF 513
Cdd:cd19481 138 RPDLLDPALLRPgrfDEVIEF 158
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
191-581 |
1.36e-16 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 82.65 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 191 AQVLDLEVTERQEVLETIAPASRLQYISVLLAKELDVLELEDHIHAQVQQELDKSQREYFLREQMKVIQSELGEGDVYTQ 270
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 271 EVNELRDRIAEMELPDETRARADKELGRLSSMPPMSPETGMIRTYLDWLIDLPWSETTEDNLDVGHVDQVLESRHY---- 346
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 347 GLPKAKDRILEYIA-----VRRLAADKMRSPI-LCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEaeirghrrtY 420
Cdd:COG0464 161 GLEEVKEELRELVAlplkrPELREEYGLPPPRgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 421 IGSLPGRIIQTMRRAGTLNP--LFmLDEVDKIGADfRGDPA--------AALLEVLDpeqnfafsdhylEVPYDlskVLF 490
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPcvLF-IDEADALAGK-RGEVGdgvgrrvvNTLLTEME------------ELRSD---VVV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 491 ITTANILSPVPPALQDRM-EVIEFPGYIDEEKLEIARRFLIPRQLEEhgldehPVAFTKSALQSliREYTYeagvrnleR 569
Cdd:COG0464 295 IAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDE------DVDLEELAEAT--EGLSG--------A 358
|
410
....*....|..
gi 1490707203 570 EIASLCRKVARR 581
Cdd:COG0464 359 DIRNVVRRAALQ 370
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
352-516 |
2.60e-13 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 67.94 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 352 KDRILEYIAVRRLAADKMRSPILcFVGPPGTGKTSLGRSIAEALGRK---FVRVSLGGVRDEAEIRGHRRTYIgslpgRI 428
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLL-LYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELFGHFL-----VR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 429 IQTMRRAGTLNPLFMLDEVDKIGADFRgdpaAALLEVLDPEQNFAFSdhylevpYDLSKVLFITTANILSPVPPALQDRM 508
Cdd:cd00009 75 LLFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVLETLNDLRID-------RENVRVIGATNRPLLGDLDRALYDRL 143
|
....*...
gi 1490707203 509 EVIEFPGY 516
Cdd:cd00009 144 DIRIVIPL 151
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
374-508 |
2.04e-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: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 374 LCFVGPPGTGKTSLGRSIAEAL-GRKFVRVSLGGVRDEAEIRGHRRtYIGSLPGRIIQTMRRAGTLNPLFMLDEVDKIGA 452
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRN-IDPGGASWVDGPLVRAAREGEIAVLDEINRANP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 453 DFrgdpAAALLEVLDpEQNFAFSDHYLEVPYDLSKVLFITTAN----ILSPVPPALQDRM 508
Cdd:pfam07728 81 DV----LNSLLSLLD-ERRLLLPDGGELVKAAPDGFRLIATMNpldrGLNELSPALRSRF 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
376-581 |
7.71e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 57.20 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 376 FVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEaeirghrrtYIGSLPGRIIQTMRRAGTLNPLFMLDEVDKIGADfR 455
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 456 GDPAA---------ALLEVLDpeqnfafsdhylevpYDLSKVLFITTANILSPVPPALQDRM-EVIEFPGYIDEEKLEIA 525
Cdd:COG1223 110 GDQNDvgevkrvvnALLQELD---------------GLPSGSVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490707203 526 RRFLIPRQLeehgldehPVAFTKSALQSLIREYTYeagvrnleREIASLCRKVARR 581
Cdd:COG1223 175 ELNLKKFPL--------PFELDLKKLAKKLEGLSG--------ADIEKVLKTALKK 214
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
362-556 |
9.32e-09 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 58.53 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 362 RRLAADKMRSPILCfvGPPGTGKTSLGRSIAEALGRKFVRVS--LGGVrdeAEIRghrrtyigslpgRIIQT--MRRAGT 437
Cdd:COG2256 42 RAIEAGRLSSMILW--GPPGTGKTTLARLIANATDAEFVALSavTSGV---KDIR------------EVIEEarERRAYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 438 LNPLFMLDEV---DKIGADfrgdpaaALLEVLdpEQNfafsdhylevpydlsKVLFI--TTANilsP---VPPALQDRME 509
Cdd:COG2256 105 RRTILFVDEIhrfNKAQQD-------ALLPHV--EDG---------------TITLIgaTTEN---PsfeVNSALLSRCR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490707203 510 VIEFPGYIDEEKLEIARRFLiprQLEEHGLDEHPVAFTKSALQSLIR 556
Cdd:COG2256 158 VFVLKPLSEEDLEQLLERAL---ADDERGLGGYKLELDDEALEALAR 201
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
699-791 |
3.61e-07 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 52.89 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 699 GPSAGITIATALISAFTNQ--TVRHDVGMTGEITLRGRVLPVGGLKEKMLAAYRAGIETIIIPKSNkkdLDEIPRRVQRK 776
Cdd:COG3480 240 GPSAGLMFALGIYDQLTPGdlTGGKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---CAEAVGTIPTG 316
|
90
....*....|....*
gi 1490707203 777 LNIVLVEQMDKVLDV 791
Cdd:COG3480 317 LKVVPVDTLDDALDA 331
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
351-556 |
4.29e-07 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 53.16 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 351 AKDRILeyiavRRL-AADKMRSPILCfvGPPGTGKTSLGRSIAEALGRKFVRVS--LGGVrdeAEIRghrrtyigslpgR 427
Cdd:PRK13342 22 GPGKPL-----RRMiEAGRLSSMILW--GPPGTGKTTLARIIAGATDAPFEALSavTSGV---KDLR------------E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 428 IIQT--MRRAGTLNPLFMLDEV---DKIGADfrgdpaaALLEVLdpEQNfafsdhylevpydlsKVLFI--TTANilsP- 499
Cdd:PRK13342 80 VIEEarQRRSAGRRTILFIDEIhrfNKAQQD-------ALLPHV--EDG---------------TITLIgaTTEN---Ps 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490707203 500 --VPPALQDRMEVIEFPGYIDEEKLEIARRFLiprQLEEHGLdehpVAFTKSALQSLIR 556
Cdd:PRK13342 133 feVNPALLSRAQVFELKPLSEEDIEQLLKRAL---EDKERGL----VELDDEALDALAR 184
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
351-528 |
5.19e-07 |
|
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: 52.09 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 351 AKDRILEYIavrrLAADKMRSPILcFVGPPGTGKTSLGRSIAEALGRKFVRVslggvrdeaeirghrRTYIGSLPGRIIQ 430
Cdd:COG0714 16 GQEELIELV----LIALLAGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSDILG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 431 TM---RRAGT--------LNPLFMLDEVDkigadfRGDPA--AALLEVLDpeqnfafsDHYLEVP---YDLSKVLF-ITT 493
Cdd:COG0714 76 TYiydQQTGEfefrpgplFANVLLADEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLvIAT 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490707203 494 ANILS-----PVPPALQDR--MEV-IEFPGyiDEEKLEIARRF 528
Cdd:COG0714 142 QNPIEqegtyPLPEAQLDRflLKLyIGYPD--AEEEREILRRH 182
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
33-86 |
1.60e-06 |
|
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: 47.05 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1490707203 33 PLLPLRDMVMFPRMVTPLFVGRDRSIEAIEVALETGEP-LITVAQRDVDVAEPGP 86
Cdd:smart00464 3 PLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyVIVFLLQDDPTETPEP 57
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
347-457 |
2.84e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 50.00 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 347 GLPKAKDRILEYIAVRRLAADKMRS----P---ILcFVGPPGTGKTSLGRSIAEALGRKFVRVSLggvrdeAEIrghRRT 419
Cdd:COG1222 82 GLDEQIEEIREAVELPLKNPELFRKygiePpkgVL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL---VSK 151
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1490707203 420 YIGSLPGRIIQTMRRAGTLNP--LFmLDEVDKIGADfRGD 457
Cdd:COG1222 152 YIGEGARNVREVFELAREKAPsiIF-IDEIDAIAAR-RTD 189
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
370-528 |
8.38e-06 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 48.45 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 370 RSPILCFVGP-PGTGKTSLGRSIAEALGRKFVRVS-----LGGVRDEAEirghrrtyigslpgRIIQTMRRAGTlNPLFM 443
Cdd:PHA02544 41 RIPNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNgsdcrIDFVRNRLT--------------RFASTVSLTGG-GKVII 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 444 LDEVDKIGADFRGDPAAALLEvldpeqnfAFSDHylevpydlskVLFITTANILSPVPPALQDRMEVIEFPGYIDEEKLE 523
Cdd:PHA02544 106 IDEFDRLGLADAQRHLRSFME--------AYSKN----------CSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIE 167
|
....*
gi 1490707203 524 IARRF 528
Cdd:PHA02544 168 MMKQM 172
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
698-766 |
1.35e-05 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 48.79 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 698 DGPSAGITIATALISAFTNQTVRHDVGMTGEITLRGRVLPVGGLKEKmlaayragIE-----------T----IIIPKSN 762
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEK--------IEgffdvckarglTgkqgVIIPAAN 663
|
....
gi 1490707203 763 KKDL 766
Cdd:COG1067 664 VKNL 667
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
336-499 |
3.37e-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: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 336 HVDQVLESRHYGLPKAKDRILEyiAVRRLAA---DKMRSPI-LCFVGPPGTGKTSLGRSIAEAL---GRKFVRVSLGgvr 408
Cdd:cd19499 4 NLEERLHERVVGQDEAVKAVSD--AIRRARAglsDPNRPIGsFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 409 deAEIRGHR-RTYIGSLPG--------RIIQTMRRagtlNP--LFMLDEVDKIGADFRGdpaaALLEVLDpeqNFAFSD- 476
Cdd:cd19499 79 --EYMEKHSvSRLIGAPPGyvgyteggQLTEAVRR----KPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDs 145
|
170 180
....*....|....*....|...
gi 1490707203 477 HYLEVpyDLSKVLFITTANILSP 499
Cdd:cd19499 146 HGRTV--DFKNTIIIMTSNHFRP 166
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
323-554 |
5.56e-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: 46.76 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 323 PW---SETTEDNL-DVGHVDQVLE---------SRHYGLPKAKDRILEY-----IAVRRLA---ADKMRSPILCFVGPPG 381
Cdd:TIGR03922 243 PWdpsSAPSRAEFvDPAAAERKAKllaeaeaelAEQIGLERVKRQVAALksstaMALARAErglPVAQTSNHMLFAGPPG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 382 TGKTSLGRSIAEALgrkfvrVSLGGVRDEaEIRGHRRT-----YIGSLPGRIIQTMRRAgtLNPLFMLDEVDKIGADFRG 456
Cdd:TIGR03922 323 TGKTTIARVVAKIY------CGLGVLRKP-LVREVSRAdligqYIGESEAKTNEIIDSA--LGGVLFLDEAYTLVETGYG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 457 DP----AAALLEVLDPEQNFAFSDHYLEVPY--DLSKVLfittanilsPVPPALQDRM-EVIEFPGYIDEEKLEIARRFL 529
Cdd:TIGR03922 394 QKdpfgLEAIDTLLARMENDRDRLVVIGAGYrkDLDKFL---------EVNEGLRSRFtRVIEFPSYSPDELVEIARRMA 464
|
250 260
....*....|....*....|....*..
gi 1490707203 530 IPRQ--LEEHGLDEHPVAFTKSALQSL 554
Cdd:TIGR03922 465 TERDsvLDDAAADALLEAATTLAQDTT 491
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
351-447 |
6.72e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 46.59 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 351 AKDRILEyiavRRLAADKMRSPIlcFVGPPGTGKTSLGRSIAEALGRKFVRVS--LGGVRD-EAEIRghrrtyigslpgR 427
Cdd:PRK13341 38 GEGRLLR----RAIKADRVGSLI--LYGPPGVGKTTLARIIANHTRAHFSSLNavLAGVKDlRAEVD------------R 99
|
90 100
....*....|....*....|
gi 1490707203 428 IIQTMRRAGTLNPLFmLDEV 447
Cdd:PRK13341 100 AKERLERHGKRTILF-IDEV 118
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
374-400 |
8.03e-05 |
|
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: 43.96 E-value: 8.03e-05
10 20
....*....|....*....|....*..
gi 1490707203 374 LCFVGPPGTGKTSLGRSIAEALGRKFV 400
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
370-504 |
1.53e-04 |
|
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: 42.75 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 370 RSPILCFVGPPGTGKTSLGRSIAEALGR---KFVRVSLGGVRDEA-EIRGHRRTYIGSLPGRIIQTMRRA-----GTLNP 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVlDQLLLIIVGGKKASGSGELRLRLAlalarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490707203 441 LFMLDEVDKigadfrgdpaaALLEVLDPEQNFAFSDHYLEVPYDLSKVLFITTANILSPVPPAL 504
Cdd:smart00382 81 VLILDEITS-----------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
377-400 |
2.03e-04 |
|
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: 42.54 E-value: 2.03e-04
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
369-400 |
5.72e-04 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 41.33 E-value: 5.72e-04
10 20 30
....*....|....*....|....*....|..
gi 1490707203 369 MRSPILCFVGPPGTGKTSLGRSIAEALGRKFV 400
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
376-531 |
6.22e-04 |
|
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: 41.41 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 376 FVGPPGTGKTSLGRSIAEALG---RKFVRVslggvrdEAeirghrRTY---------IGSLPGRI------IQTMRRAGT 437
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI-------DM------SEYmeehsvsrlIGAPPGYVgyeeggQLTEAVRRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 438 LNPLFMLDEVDKIGAD-FRgdpaaALLEVLDpeqNFAFSDHYlEVPYDLSKVLFITTANILSPVPpalQDRMEVIEFPGY 516
Cdd:pfam07724 75 PYSIVLIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNFGSEKI---SDASRLGDSPDY 142
|
170
....*....|....*..
gi 1490707203 517 --IDEEKLEIARRFLIP 531
Cdd:pfam07724 143 elLKEEVMDLLKKGFIP 159
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
350-513 |
6.33e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 42.99 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 350 KAKDRILEYIavRRLAADKMRSPILcFVGPPGTGKTSLgrsiAEALGRKF------VRVSlggvrDEaeirghrRTYigs 423
Cdd:PRK04195 21 KAKEQLREWI--ESWLKGKPKKALL-LYGPPGVGKTSL----AHALANDYgwevieLNAS-----DQ-------RTA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 424 lpGRIIQTMRRAGTLNPLF-------MLDEVDKI--GADFRGdpAAALLEVLDPeqnfafsdhylevpydlSKVLFITTA 494
Cdd:PRK04195 79 --DVIERVAGEAATSGSLFgarrkliLLDEVDGIhgNEDRGG--ARAILELIKK-----------------AKQPIILTA 137
|
170 180
....*....|....*....|
gi 1490707203 495 N-ILSPVPPALQDRMEVIEF 513
Cdd:PRK04195 138 NdPYDPSLRELRNACLMIEF 157
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
151-529 |
1.48e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 42.06 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 151 LMRAVLALFEKVVQLNRSLPQDAYVFAMNVDGPGWLADLMAQVLDLEVTERQEVLETIAPASRLQYISVLLAKELDVLEL 230
Cdd:COG1401 1 LLRPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 231 EDhihaqvqqELDKSQREYFLREQMKVIQSELGEGDVYTQEVNELRDRIAEMELPDETRARADKELGRLSSMPPMSPETG 310
Cdd:COG1401 81 LD--------LEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 311 MIRTYLDWLIDLPWSETTEDNLDVGHVDQVLESRHYG--LPKAKDRILEYIA------VRRLAADKMRSPILCFVGPPGT 382
Cdd:COG1401 153 EVLEALEAELEELLAAPEDLSADALAAELSAAEELYSedLESEDDYLKDLLRekfeetLEAFLAALKTKKNVILAGPPGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 383 GKTSLGRSIAEALG----RKFVRVSlggVR----DEAEIRGHR-RTYIGSL---PGRIIQTMRRA--GTLNPLFM-LDE- 446
Cdd:COG1401 233 GKTYLARRLAEALGgednGRIEFVQ---FHpswsYEDFLLGYRpSLDEGKYeptPGIFLRFCLKAekNPDKPYVLiIDEi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 447 ----VDKIGADF--------RGDPAAALLEVLDPEQNFafsdhylEVPydlSKVLFITTANI----LSPVPPALQDRMEV 510
Cdd:COG1401 310 nranVEKYFGELlsllesdkRGEELSIELPYSGEGEEF-------SIP---PNLYIIGTMNTddrsLALSDKALRRRFTF 379
|
410
....*....|....*....
gi 1490707203 511 IEFPGYIDEEKLEIARRFL 529
Cdd:COG1401 380 EFLDPDLDKLSNEEVVDLL 398
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
319-403 |
3.02e-03 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 39.59 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 319 LIDLPWSETTEDNLDVGHVDQVlesrhyGLPKAKDRILEYIAVRRLAAD---KMRSP---ILCFvGPPGTGKTSLGRSIA 392
Cdd:cd19525 4 MIELIMSEIMDHGPPINWADIA------GLEFAKKTIKEIVVWPMLRPDiftGLRGPpkgILLF-GPPGTGKTLIGKCIA 76
|
90
....*....|.
gi 1490707203 393 EALGRKFVRVS 403
Cdd:cd19525 77 SQSGATFFSIS 87
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
378-415 |
4.47e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 39.02 E-value: 4.47e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1490707203 378 GPPGTGKTSLGRSIAEALGRKFvrVSLGGV-RDEAEIRG 415
Cdd:PRK04182 7 GPPGSGKTTVARLLAEKLGLKH--VSAGEIfRELAKERG 43
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
376-450 |
4.63e-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: 38.81 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 376 FVGPPGTGKTSLGRSIAEALGRKFVRVSlggvrdeaeirGHrrTYIGSLPGRIIQTMR----RAGTLNP-LFMLDEVDKI 450
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEAGANFLSIS-----------GP--SIVSKYLGESEKNLReifeEARSHAPsIIFIDEIDAL 105
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
378-452 |
5.06e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 38.47 E-value: 5.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490707203 378 GPPGTGKTSLGRSIAEALGRKFVRVSlggvrdEAEIrghRRTYIGSLPGRIIQTMRRAGTLNP--LFMlDEVDKIGA 452
Cdd:cd19502 44 GPPGTGKTLLAKAVANHTDATFIRVV------GSEL---VQKYIGEGARLVRELFEMAREKAPsiIFI-DEIDAIGA 110
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
203-393 |
5.07e-03 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 40.42 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 203 EVLETIAPASRlQYIS--VLLAKELDVLeleDHIHAQV---QQELDKSQRE--YFLREQMKVIQSELGEGDVYTQEvnEL 275
Cdd:CHL00095 368 KALEAAAKLSD-QYIAdrFLPDKAIDLL---DEAGSRVrliNSRLPPAAREldKELREILKDKDEAIREQDFETAK--QL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 276 RDRiaEMELPDETRA--RADKELGRLSSMPPMSPETGMIRTYLDWlIDLPWSETTEDNLD-VGHVDQVLESRHYGLPKAK 352
Cdd:CHL00095 442 RDR--EMEVRAQIAAiiQSKKTEEEKRLEVPVVTEEDIAEIVSAW-TGIPVNKLTKSESEkLLHMEETLHKRIIGQDEAV 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490707203 353 DRILeyIAVRRlAADKMRSP-------ILCfvGPPGTGKTSLGRSIAE 393
Cdd:CHL00095 519 VAVS--KAIRR-ARVGLKNPnrpiasfLFS--GPTGVGKTELTKALAS 561
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
374-457 |
7.46e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 38.12 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490707203 374 LCFVGPPGTGKTSLGRSIAEALGRKFVRVSLGGVRDEaeirghrrtYIGSLPGRIIQTMRRAGTLNP-LFMLDEVDKI-- 450
Cdd:cd19507 34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAIAPcVLWIDEIEKGfs 104
|
....*..
gi 1490707203 451 GADFRGD 457
Cdd:cd19507 105 NADSKGD 111
|
|
| |
