|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
11-778 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1477.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 11 IPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQILLVAQKEAATNDPSIQDLYEVGTVASILQLLKLPDGTLKV 90
Cdd:COG0466 14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 91 LVEGLYRAEIKKFSEND-YFIADSQYMQTPEVDEREQEVLVRTVISQFEGFIKLNKKIPPEVLTSLNGIDNADRLADTIA 169
Cdd:COG0466 94 LVEGLQRARIKEFVQEEpYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLADFIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 170 AHMPLKLHDKQQALEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKELGELDDAPDE 249
Cdd:COG0466 174 SHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDDGEDE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 250 FEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVLNEDHYGLERV 329
Cdd:COG0466 254 IEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 330 KERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSLPGRLIQKM 409
Cdd:COG0466 334 KERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 410 AKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSM-NIPGPLLDRMEVIR 488
Cdd:COG0466 414 KKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAPLLDRMEIIE 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 489 LSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAILLNtEITSIT 568
Cdd:COG0466 494 LSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEG-KKKKVT 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 569 INQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKAAMTVVRTRA 648
Cdd:COG0466 573 ITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 649 DKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQRG 728
Cdd:COG0466 653 EELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 732
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1255102412 729 GIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLALQNNPHGIE 778
Cdd:COG0466 733 GIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLP 782
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-783 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1426.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 1 MNLERSERIGIPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQILLVAQKEAATNDPSIQDLYEVGTVASILQL 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 81 LKLPDGTLKVLVEGLYRAEIKKFSEN-DYFIADSQYMQTPEVDEREQEVLVRTVISQFEGFIKLNKKIPPEVLTSLNGID 159
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNgEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 160 NADRLADTIAAHMPLKLHDKQQALEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKE 239
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 240 LGELDDAPDEFEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVL 319
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 320 NEDHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIG 399
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 400 SLPGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSMNIPGP 479
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 480 LLDRMEVIRLSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAIL 559
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 560 LNTEITSITINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKA 639
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 640 AMTVVRTRADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLK 719
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1255102412 720 EKLLAAQRGGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLALQNNPHGIERVTPQ 783
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-770 |
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: 1103.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 12 PVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQI-LLVAQKEAATNDPSIQDLYEVGTVASILQLLKLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYlGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 88 LKVLVEGLYRAEIKKFSEN-DYFIADSQYMQT--PEVDEREQEVLVRTVISQFEGFIKLNK--KIPPEVLTSLNGIDNAD 162
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKgGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 163 RLADTIAAHMPLKLHDKQQA-LEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKELG 241
Cdd:TIGR00763 161 RLADFVAASLQLKEKDELQEvLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 242 ELDDAPDEFEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVLNE 321
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 322 DHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSL 401
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 402 PGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSMN-IPGPL 480
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 481 LDRMEVIRLSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAILL 560
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 561 N-----TEITSITINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQE 635
Cdd:TIGR00763 561 QgekkkSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 636 SIKAAMTVVRTRADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPI 715
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1255102412 716 GGLKEKLLAAQRGGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLAL 770
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
312-492 |
1.12e-121 |
|
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: 363.03 E-value: 1.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 312 LAKAEKVLNEDHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIR 391
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 392 GHRRTYIGSLPGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATS 471
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1255102412 472 NSM-NIPGPLLDRMEVIRLSGY 492
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
568-770 |
3.13e-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: 362.71 E-value: 3.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 568 TINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKAAMTVVRTR 647
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 648 ADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQR 727
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1255102412 728 GGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLAL 770
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
10-62 |
3.34e-08 |
|
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: 51.67 E-value: 3.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1255102412 10 GIPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQ--ILLVAQKEAATND 62
Cdd:smart00464 1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyvIVFLLQDDPTETP 55
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
351-444 |
9.93e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 38.22 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 351 LCLVGPPGVGKTSLGQSIARAT---GRK--YTRMAlggvRDEAEIRGHRRtyIGSLpGRLIQKMAKVgvknPLFLLDEID 425
Cdd:NF038214 93 VLLLGPPGTGKTHLAIALGYAAcrqGYRvrFTTAA----DLVEQLAQARA--DGRL-GRLLRRLARY----DLLIIDELG 161
|
90
....*....|....*....
gi 1255102412 426 KMSFDmrGDPASALLEVLD 444
Cdd:NF038214 162 YLPFS--REGANLLFELIA 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
11-778 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1477.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 11 IPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQILLVAQKEAATNDPSIQDLYEVGTVASILQLLKLPDGTLKV 90
Cdd:COG0466 14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 91 LVEGLYRAEIKKFSEND-YFIADSQYMQTPEVDEREQEVLVRTVISQFEGFIKLNKKIPPEVLTSLNGIDNADRLADTIA 169
Cdd:COG0466 94 LVEGLQRARIKEFVQEEpYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLADFIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 170 AHMPLKLHDKQQALEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKELGELDDAPDE 249
Cdd:COG0466 174 SHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDDGEDE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 250 FEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVLNEDHYGLERV 329
Cdd:COG0466 254 IEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 330 KERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSLPGRLIQKM 409
Cdd:COG0466 334 KERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 410 AKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSM-NIPGPLLDRMEVIR 488
Cdd:COG0466 414 KKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAPLLDRMEIIE 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 489 LSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAILLNtEITSIT 568
Cdd:COG0466 494 LSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEG-KKKKVT 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 569 INQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKAAMTVVRTRA 648
Cdd:COG0466 573 ITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 649 DKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQRG 728
Cdd:COG0466 653 EELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 732
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1255102412 729 GIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLALQNNPHGIE 778
Cdd:COG0466 733 GIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLP 782
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-783 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1426.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 1 MNLERSERIGIPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQILLVAQKEAATNDPSIQDLYEVGTVASILQL 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 81 LKLPDGTLKVLVEGLYRAEIKKFSEN-DYFIADSQYMQTPEVDEREQEVLVRTVISQFEGFIKLNKKIPPEVLTSLNGID 159
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNgEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 160 NADRLADTIAAHMPLKLHDKQQALEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKE 239
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 240 LGELDDAPDEFEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVL 319
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 320 NEDHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIG 399
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 400 SLPGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSMNIPGP 479
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 480 LLDRMEVIRLSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAIL 559
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 560 LNTEITSITINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKA 639
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 640 AMTVVRTRADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLK 719
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1255102412 720 EKLLAAQRGGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLALQNNPHGIERVTPQ 783
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-770 |
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: 1103.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 12 PVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQI-LLVAQKEAATNDPSIQDLYEVGTVASILQLLKLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYlGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 88 LKVLVEGLYRAEIKKFSEN-DYFIADSQYMQT--PEVDEREQEVLVRTVISQFEGFIKLNK--KIPPEVLTSLNGIDNAD 162
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKgGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 163 RLADTIAAHMPLKLHDKQQA-LEIIDISKRLEFLMTMMESEIDLLQVEKRIRSRVKKQMEKSQREYYLNEQMKAIQKELG 241
Cdd:TIGR00763 161 RLADFVAASLQLKEKDELQEvLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 242 ELDDAPDEFEGLKIKIEESKMPKEAKEKTEQELHKLKMMSPMSAEATVVRSYIDWMITVPWSKRTKVKKDLAKAEKVLNE 321
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 322 DHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSL 401
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 402 PGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATSNSMN-IPGPL 480
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 481 LDRMEVIRLSGYTEDEKLNIAKQHLMDKQVKRNGLKPSEVTIEDSAIVGIIRYYTREAGVRNLEREISKLCRKAVKAILL 560
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 561 N-----TEITSITINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQE 635
Cdd:TIGR00763 561 QgekkkSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 636 SIKAAMTVVRTRADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPI 715
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1255102412 716 GGLKEKLLAAQRGGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLAL 770
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
312-492 |
1.12e-121 |
|
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: 363.03 E-value: 1.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 312 LAKAEKVLNEDHYGLERVKERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIR 391
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 392 GHRRTYIGSLPGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLDPEQNNAFNDHYMEVDYDLSDVMFVATS 471
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1255102412 472 NSM-NIPGPLLDRMEVIRLSGY 492
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
568-770 |
3.13e-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: 362.71 E-value: 3.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 568 TINQDNLRYYLGVQRFDYGKADVSNRVGQVTGLAWTSVGGDLLTIETESMLGKGKLTQTGSLGDVMQESIKAAMTVVRTR 647
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 648 ADKLGINSDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQR 727
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1255102412 728 GGIKTVVIPKENERDLEEILDNVKAHLDIHPVRWIDEVLSLAL 770
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
11-200 |
8.34e-56 |
|
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: 189.85 E-value: 8.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 11 IPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQ--ILLVAQKEAATNDPSIQDLYEVGTVASILQLLKLPDGTL 88
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 89 KVLVEGLYRAEIKKF--SENDYFIAdsQYMQTPEVDEREQEVLVRTVISQFEGFIKLNKKI-PPEVLTSLNGIDNADRLA 165
Cdd:pfam02190 82 KVLVEGLERVRIVELvkKEEPYLRA--EVEDLPEDSDELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRLA 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1255102412 166 DTIAAHMPLKLHDKQQALEIIDISKRLEFLMTMME 200
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
351-492 |
1.15e-22 |
|
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: 94.20 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 351 LCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDeaeirghrrTYIGSLPGRLIQKMAKVGVKNP-LFLLDEIDKM-- 427
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1255102412 428 -----SFDMRGDPASALLEVLDPEQNNAfndhymevdydlSDVMFVATSNSM-NIPGPLLDRMEVIRLSGY 492
Cdd:pfam00004 72 srgsgGDSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPdKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
630-769 |
1.17e-20 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 91.19 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 630 GDVMQESIKAAMTVVRTRAdklGINSDFYekrDIHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLR 709
Cdd:COG1750 69 GPDTQASARIAALVASLLA---GVDLSSY---DVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPD 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 710 GEVLPIGGLKEKLLAAQRGGIKTVVIPKEN------ERDLEEILDNVKA----HLDIHPVRWIDEVLSLA 769
Cdd:COG1750 143 GSIGPVGGVYEKLEAAASAGAKYFLIPKGQailtgyNTQVGETVDLVEYgkelGVKVIEVSTIADALQYF 212
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
11-202 |
1.03e-19 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 87.62 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 11 IPVLPLrDVVVYPHMVIPL--FVGRDKsiRCLEAAMDNDKQI---LLVAQKEAATNDPsiqdLYEVGTVASILQLLKLPD 85
Cdd:COG2802 7 LPLFPL-GAVLFPGGRLPLhiFEPRYL--DMVRDCLAGDRPFgvvLIREGREVGGPPP----LYDVGTLARITDFEELED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 86 GTLKVLVEGLYRAEIKKFSEND--YFIADSQYM-QTPEVDEREQEVLVRT-VISQFEGFIKLNKkippevLTSLNGIDNA 161
Cdd:COG2802 80 GRLDITLRGVQRFRILEELQEDdpYRVAEVEWLpDEPDLPVPEELEALRErLLRLLRRYPELAG------LEADPDLDDP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1255102412 162 DRLADTIAAHMPLKLHDKQQALEIIDISKRLEFLMTMMESE 202
Cdd:COG2802 154 EWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
504-768 |
1.04e-13 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 74.98 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 504 HLMDKQVKRNGLKPsevtIEDSAIVGIIRYYTREAG-----------VRNLEREISKLCRKAVKAIllnteITSITINQ- 571
Cdd:COG1067 405 RFIASICREEGLRP----FDRSAVARLIEYSSRLAEdqeklstrfaeIADLLREADYWARKAGAEL-----ITAEHVEQa 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 572 -DNLRYYLGVQR------FDYGKADVS---NRVGQVTGLAWTSVG------------------GDLLTIETESMLG---- 619
Cdd:COG1067 476 lDAKEYRSNRIEekiqesILDGTILIDtegEKVGQINGLSVLDLGdysfgrpsritatvylgkGGVIDIEREVELSgpih 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 620 -KGKLTQTGSLGDV-MQE---SIKAAMTvvrtradklginsdF---YEkrdihvHVpegatpkDGPSAGIAMCTALVSSL 691
Cdd:COG1067 556 sKGVLILSGYLGARyAQDkplSLSASLV--------------FeqsYG------GV-------DGDSASSAELYALLSAL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 692 TGNPVRADVAMTGEITLRGEVLPIGGLKEKL-----LAAQRG--GIKTVVIPKENERDL---EEILDNVKA---HldIHP 758
Cdd:COG1067 609 SGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARGltGKQGVIIPAANVKNLmlrDEVVEAVKAgqfH--IYA 686
|
330
....*....|
gi 1255102412 759 VRWIDEVLSL 768
Cdd:COG1067 687 VEHVDEAIEL 696
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
677-770 |
3.73e-12 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 69.31 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 677 PSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQRGGIKTVVIPKENERDLEeildnvKAHLDI 756
Cdd:COG1066 366 PAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGEIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKLK------PKGIEI 439
|
90
....*....|....
gi 1255102412 757 HPVRWIDEVLSLAL 770
Cdd:COG1066 440 IGVSTLEEALEALF 453
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
330-487 |
4.55e-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: 64.47 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 330 KERILEYLAVQNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMA---LGGVRDEAEIRGHRRTYIGSLPGRLI 406
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLylnASDLLEGLVVAELFGHFLVRLLFELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 407 QKMakvgvKNPLFLLDEIDKMSFDMRgdpaSALLEVLdpeqnnafnDHYMEVDYDLSDVMFVATSNSMN---IPGPLLDR 483
Cdd:cd00009 81 EKA-----KPGVLFIDEIDSLSRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNRPLlgdLDRALYDR 142
|
....
gi 1255102412 484 MEVI 487
Cdd:cd00009 143 LDIR 146
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
329-472 |
7.71e-11 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 61.14 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 329 VKERILEYLAVQ------NRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAeirghrRTYIGSLP 402
Cdd:cd19481 1 LKASLREAVEAPrrgsrlRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1255102412 403 GRLIQKMAKvgVKNPLFLLDEIDKMSFDmRGDPA---------SALLEVLDPEQNnafndhymevdydLSDVMFVATSN 472
Cdd:cd19481 75 RKIFERARR--LAPCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATN 137
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
325-504 |
2.22e-10 |
|
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: 62.49 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 325 GLERVKERILeyLAVqnrvnKLRGPILcLVGPPGVGKTSLGQSIARATGRKYTRMalggvrdeaeirghrRTYIGSLPGR 404
Cdd:COG0714 16 GQEELIELVL--IAL-----LAGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 405 LI-------QKMAKVGVKNPLF----LLDEIDkmsfdmRGDPA--SALLEVLDpeqnnafnDHYMEVD---YDLSDVMFV 468
Cdd:COG0714 73 ILgtyiydqQTGEFEFRPGPLFanvlLADEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1255102412 469 -ATSNSM------NIPGPLLDRMeVIRLS-GY-TEDEKLNIAKQH 504
Cdd:COG0714 139 iATQNPIeqegtyPLPEAQLDRF-LLKLYiGYpDAEEEREILRRH 182
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
325-510 |
2.82e-10 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 63.01 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 325 GLERVKERILEYLAVQNRVNKLRGPI-------LCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEaeirghrrtY 397
Cdd:COG0464 161 GLEEVKEELRELVALPLKRPELREEYglppprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 398 IGSLPgrliQKMAKV-----GVKNPLFLLDEIDKMsFDMRGdpasallEVLDPEQNNAFNdhYM--EVDYDLSDVMFVAT 470
Cdd:COG0464 232 VGETE----KNLREVfdkarGLAPCVLFIDEADAL-AGKRG-------EVGDGVGRRVVN--TLltEMEELRSDVVVIAA 297
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1255102412 471 SNSM-NIPGPLLDRM-EVIRLSGYTEDEKLNIAKQHLMDKQV 510
Cdd:COG0464 298 TNRPdLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPL 339
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
676-771 |
5.75e-10 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 61.75 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 676 GPSAGIAMCTALVSSLTGNPVR--ADVAMTGEITLRGEVLPIGGLKEKLLAAQRGGIKTVVIPKENErdlEEILDNVKAH 753
Cdd:COG3480 240 GPSAGLMFALGIYDQLTPGDLTggKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNC---AEAVGTIPTG 316
|
90
....*....|....*...
gi 1255102412 754 LDIHPVRWIDEVLSlALQ 771
Cdd:COG3480 317 LKVVPVDTLDDALD-ALE 333
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
351-484 |
1.93e-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: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 351 LCLVGPPGVGKTSLGQSIARAT-GRKYTRMALGgvRD--EAEIRGHRRtyIGSLPGRLIQKMAKVGVKNP-LFLLDEIDK 426
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLT--RDttEEDLFGRRN--IDPGGASWVDGPLVRAAREGeIAVLDEINR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 427 msfdmrgdpasALLEVLDpEQNNAFNDHYM-------EVDYDLSDVMFVATSNS-----MNIPGPLLDRM 484
Cdd:pfam07728 78 -----------ANPDVLN-SLLSLLDERRLllpdggeLVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
10-62 |
3.34e-08 |
|
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: 51.67 E-value: 3.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1255102412 10 GIPVLPLRDVVVYPHMVIPLFVGRDKSIRCLEAAMDNDKQ--ILLVAQKEAATND 62
Cdd:smart00464 1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyvIVFLLQDDPTETP 55
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
347-484 |
1.03e-06 |
|
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: 48.91 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 347 RGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSLPG----------RLIQKMAKvGVKN 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKkasgsgelrlRLALALAR-KLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1255102412 417 PLFLLDEIDKMSfdmrgDPASALLEVLDPEQNNAFNDHYMEvdydlsDVMFVATSNSMNIPGPLLDRM 484
Cdd:smart00382 80 DVLILDEITSLL-----DAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPALLRR 136
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
355-533 |
1.61e-06 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 51.21 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 355 GPPGVGKTSLGQSIARATGRKYTRM--ALGGVrdeAEIRghrrtyigslpgRLIQ--KMAKVGVKNPLFLLDEI---DKM 427
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 428 SFDmrgdpasALLevldpeqnnafndHYMEvdydlsD--VMFVA--TSN-SMNIPGPLLDRMEVIRLSGYTEDEKLNIAK 502
Cdd:COG2256 121 QQD-------ALL-------------PHVE------DgtITLIGatTENpSFEVNSALLSRCRVFVLKPLSEEDLEQLLE 174
|
170 180 190
....*....|....*....|....*....|.
gi 1255102412 503 QHLMDKQvkrNGLKPSEVTIEDSAIVGIIRY 533
Cdd:COG2256 175 RALADDE---RGLGGYKLELDDEALEALARL 202
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
303-502 |
2.35e-06 |
|
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: 51.00 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 303 SKRTKVKKDLAKAEKVLNEdHYGLERVKERI--LEYLAVQNRVNKLRG-PI------LCLVGPPGVGKTslgqSIARATG 373
Cdd:TIGR03922 259 AAAERKAKLLAEAEAELAE-QIGLERVKRQVaaLKSSTAMALARAERGlPVaqtsnhMLFAGPPGTGKT----TIARVVA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 374 RKYTrmALGGVRDEAEIRGHRRTYIGslpgrliQKMAKVGVKNPLFLLDEIDKMSFdmrGDPASALLEVL----DPEQNN 449
Cdd:TIGR03922 334 KIYC--GLGVLRKPLVREVSRADLIG-------QYIGESEAKTNEIIDSALGGVLF---LDEAYTLVETGygqkDPFGLE 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1255102412 450 AFND--HYMEVDYDLSDVMFVATSNSMNipgPLLDRME--------VIRLSGYTEDEKLNIAK 502
Cdd:TIGR03922 402 AIDTllARMENDRDRLVVIGAGYRKDLD---KFLEVNEglrsrftrVIEFPSYSPDELVEIAR 461
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
321-571 |
1.16e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.57 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 321 EDHYGLERVKERILEYLAVQNRVNKLRG-------PILcLVGPPGVGKTSLGQSIARATGRKYtrmalggvrdeAEIRGH 393
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKELRRRENLRKfglwpprKIL-FYGPPGTGKTMLAEALAGELKLPL-----------LTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 394 rrTYIGSLPG-------RLIQKMAKVGVknpLFLLDEIDKMSFDmRGDPAsallevLDPEQNNAFNDHYMEVDYDLSDVM 466
Cdd:COG1223 70 --SLIGSYLGetarnlrKLFDFARRAPC---VIFFDEFDAIAKD-RGDQN------DVGEVKRVVNALLQELDGLPSGSV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 467 FVATSNSMNipgpLLDRM------EVIRLSGYTEDEKLNIAKQHLMDkqvkrnglKPSEVTIEDSAIVGIIRyytreaGV 540
Cdd:COG1223 138 VIAATNHPE----LLDSAlwrrfdEVIEFPLPDKEERKEILELNLKK--------FPLPFELDLKKLAKKLE------GL 199
|
250 260 270
....*....|....*....|....*....|....*..
gi 1255102412 541 RNleREISKLCRKAVK-AIL-----LNTEITSITINQ 571
Cdd:COG1223 200 SG--ADIEKVLKTALKkAILedrekVTKEDLEEALKQ 234
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
355-533 |
3.03e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 47.00 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 355 GPPGVGKTSLGQSIARATGRKYTRM--ALGGVrdeAEIRghrrtyigslpgRLIQ--KMAKVGVKNPLFLLDEI---DKM 427
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEeaRQRRSAGRRTILFIDEIhrfNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 428 SFDmrgdpasALLevldpeqnnafndHYMEVDydlsDVMFVA--TSN-SMNIPGPLLDRMEVIRLSGYTEDEKLNIAKQH 504
Cdd:PRK13342 108 QQD-------ALL-------------PHVEDG----TITLIGatTENpSFEVNPALLSRAQVFELKPLSEEDIEQLLKRA 163
|
170 180
....*....|....*....|....*....
gi 1255102412 505 LMDKQvkrNGLkpseVTIEDSAIVGIIRY 533
Cdd:PRK13342 164 LEDKE---RGL----VELDDEALDALARL 185
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
673-739 |
7.05e-05 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 42.82 E-value: 7.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1255102412 673 PKDGPSAGIAMCTALVSSLTGNPVRADVAMTGEITLRGEVLPIGGLKEKLLAAQRGGIKTVVIPKEN 739
Cdd:pfam13541 55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
347-425 |
3.28e-04 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 41.85 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 347 RGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRGHRRTYIGSLPG------RLIQkMAKVGVKNP-LF 419
Cdd:cd00267 24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrQRVA-LARALLLNPdLL 102
|
....*.
gi 1255102412 420 LLDEID 425
Cdd:cd00267 103 LLDEPT 108
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
351-444 |
8.37e-04 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 41.69 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 351 LCLVGPPGVGKTSLGQSIARA---TGRK--YTRMA-LGgvrdeAEIRGHRRTyiGSLpGRLIQKMAKVgvknPLFLLDEI 424
Cdd:COG1484 102 LILLGPPGTGKTHLAIALGHEacrAGYRvrFTTAPdLV-----NELKEARAD--GRL-ERLLKRLAKV----DLLILDEL 169
|
90 100
....*....|....*....|
gi 1255102412 425 DKMSFDMRGdpASALLEVLD 444
Cdd:COG1484 170 GYLPLDAEG--AELLFELIS 187
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
324-444 |
1.33e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 324 YGLERVKERILEYLavqNRVNKLRGPILCLVGPPGVGKTSLGQSIARATGRKYTRMALGGVRDEAEIRG-----HRRTYI 398
Cdd:pfam13191 3 VGREEELEQLLDAL---DRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPllealTREGLL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1255102412 399 GSLPGRLIQKMAKVGVKNPLFLLDEIDKMSFDMRGDPASALLEVLD 444
Cdd:pfam13191 80 RQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
264-362 |
3.18e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 40.62 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 264 KEAKEKTEQELHKLK---------MMSPMSAEATVVRSYIDWMItvpwskRTKVKKDLAK--AEKVLNedHYGLERVKER 332
Cdd:COG1419 73 EEELEELRRELAELKelleeqlsgLAGESARLPPELAELLERLL------EAGVSPELARelLEKLPE--DLSAEEAWRA 144
|
90 100 110
....*....|....*....|....*....|....*.
gi 1255102412 333 ILEYLAvqNRVNKLRGPIL------CLVGPPGVGKT 362
Cdd:COG1419 145 LLEALA--RRLPVAEDPLLdeggviALVGPTGVGKT 178
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
184-347 |
4.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 184 EIIDISKRLEFLMTMMEsEIDLLQVEKRIRSRVKKQMEKSQREyyLNEQMKAIQKELGELDDAPDEFEGLKIKIEESKMP 263
Cdd:PRK03918 222 ELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRE--LEERIEELKKEIEELEEKVKELKELKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 264 KEAKEKTEQELHKL-KMMSPMSAEATVVRSYIdwmitvpwSKRTKVKKDLAKAEKVLNEDHYGLERVKERILEY---LAV 339
Cdd:PRK03918 299 SEFYEEYLDELREIeKRLSRLEEEINGIEERI--------KELEEKEERLEELKKKLKELEKRLEELEERHELYeeaKAK 370
|
....*...
gi 1255102412 340 QNRVNKLR 347
Cdd:PRK03918 371 KEELERLK 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
207-286 |
6.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 207 QVEKRIRSRVKK--QMEKS--QREYYLNEQMKAIQKELGELDDAPDEFEGLKIKIEESKmpKEAKEKTEQELHKLKMMSP 282
Cdd:PRK12704 72 EFEKELRERRNElqKLEKRllQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE--EELEELIEEQLQELERISG 149
|
....
gi 1255102412 283 MSAE 286
Cdd:PRK12704 150 LTAE 153
|
|
| MCM_arch |
cd17761 |
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ... |
324-448 |
7.80e-03 |
|
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork
Pssm-ID: 350667 [Multi-domain] Cd Length: 308 Bit Score: 39.36 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 324 YGLERVKERILEYLAVQNRVN-----KLRGPI-LCLVGPPGVGKTSLGQSIAR-------ATGRKYTRMALGG--VRDEA 388
Cdd:cd17761 12 YGHEDVKEAIALQLFGGVPKVlpdgtRIRGDIhILLVGDPGTAKSQLLKYVSKvapravyTTGKGSTAAGLTAavVRDEG 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 389 EirghRRTYIGSlpGRLIqkMAKVGVKnplfLLDEIDKMSFDMRgdpaSALLEVLdpEQN 448
Cdd:cd17761 92 T----GEWYLEA--GALV--LADKGIA----VVDEIDKMRKEDR----SALHEAM--EQQ 133
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
351-444 |
9.93e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 38.22 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255102412 351 LCLVGPPGVGKTSLGQSIARAT---GRK--YTRMAlggvRDEAEIRGHRRtyIGSLpGRLIQKMAKVgvknPLFLLDEID 425
Cdd:NF038214 93 VLLLGPPGTGKTHLAIALGYAAcrqGYRvrFTTAA----DLVEQLAQARA--DGRL-GRLLRRLARY----DLLIIDELG 161
|
90
....*....|....*....
gi 1255102412 426 KMSFDmrGDPASALLEVLD 444
Cdd:NF038214 162 YLPFS--REGANLLFELIA 178
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