|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-784 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1597.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 1 MNPERPERIEIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMNDNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQM 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 81 LKLPDGTVKVLVEGIRRAKITTLSDNGEYFQAKAEYLETPAVDEREQEVLNRTTINQFEGYIKLNKKIPPEVLTSLHAIE 160
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 161 ESAKLADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 241 LGEMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVL 320
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 321 DTDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSMNIPAP 480
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 481 LLDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 561 MDSTIKHIEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQA 640
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 641 AMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLK 720
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1130902148 721 EKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLALQNSPFGMEVVTDK 784
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
2-775 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1504.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 2 NPERPERIEIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMNDNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQML 81
Cdd:COG0466 5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 82 KLPDGTVKVLVEGIRRAKITTLSDNGEYFQAKAEYLETPAVDEREQEVLNRTTINQFEGYIKLNKKIPPEVLTSLHAIEE 161
Cdd:COG0466 85 KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 162 SAKLADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKEL 241
Cdd:COG0466 165 PGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 242 GEMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVLD 321
Cdd:COG0466 245 GEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 322 TDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGS 401
Cdd:COG0466 325 EDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 402 MPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSM-NIPAP 480
Cdd:COG0466 405 MPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAP 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 481 LLDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
Cdd:COG0466 485 LLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 561 MDSTiKHIEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQA 640
Cdd:COG0466 565 EGKK-KKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 641 AMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLK 720
Cdd:COG0466 644 ALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLK 723
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 721 EKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLALQNSP 775
Cdd:COG0466 724 EKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-771 |
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: 1142.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 12 PVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMN-DNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQMLKLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRlKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 88 VKVLVEGIRRAKITTLSDNGEYFQAKAEYLET--PAVDEREQEVLNRTTINQFEGYIKLNK--KIPPEVLTSLHAIEESA 163
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 164 KLADTIASHMPLK-LKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 243 EMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVLDT 322
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 323 DHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 482 LDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLLM 561
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 562 DSTIKH-----IEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQE 636
Cdd:TIGR00763 561 QGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 637 SIQAAMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPI 716
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 717 GGLKEKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLAL 771
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
313-493 |
8.77e-124 |
|
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: 368.42 E-value: 8.77e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 313 LVKAQEVLDTDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATS 472
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1130902148 473 NSM-NIPAPLLDRMEVIRLSGY 493
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
570-771 |
7.09e-122 |
|
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: 364.25 E-value: 7.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 570 INEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQAAMTVVRARA 649
Cdd:pfam05362 2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 650 DKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLKEKLLAAHRG 729
Cdd:pfam05362 82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1130902148 730 GIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLAL 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
10-62 |
8.67e-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: 50.51 E-value: 8.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 10 EIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMND--NKQIMLVAQKDASTDE 62
Cdd:smart00464 1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRsqPYVIVFLLQDDPTETP 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-784 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1597.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 1 MNPERPERIEIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMNDNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQM 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 81 LKLPDGTVKVLVEGIRRAKITTLSDNGEYFQAKAEYLETPAVDEREQEVLNRTTINQFEGYIKLNKKIPPEVLTSLHAIE 160
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 161 ESAKLADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 241 LGEMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVL 320
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 321 DTDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSMNIPAP 480
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 481 LLDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 561 MDSTIKHIEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQA 640
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 641 AMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLK 720
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1130902148 721 EKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLALQNSPFGMEVVTDK 784
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
2-775 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1504.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 2 NPERPERIEIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMNDNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQML 81
Cdd:COG0466 5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 82 KLPDGTVKVLVEGIRRAKITTLSDNGEYFQAKAEYLETPAVDEREQEVLNRTTINQFEGYIKLNKKIPPEVLTSLHAIEE 161
Cdd:COG0466 85 KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 162 SAKLADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKEL 241
Cdd:COG0466 165 PGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 242 GEMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVLD 321
Cdd:COG0466 245 GEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 322 TDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGS 401
Cdd:COG0466 325 EDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 402 MPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSM-NIPAP 480
Cdd:COG0466 405 MPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAP 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 481 LLDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560
Cdd:COG0466 485 LLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 561 MDSTiKHIEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQA 640
Cdd:COG0466 565 EGKK-KKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 641 AMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLK 720
Cdd:COG0466 644 ALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLK 723
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 721 EKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLALQNSP 775
Cdd:COG0466 724 EKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-771 |
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: 1142.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 12 PVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMN-DNKQIMLVAQKDASTDEPGVNDLFSVGTVASVLQMLKLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRlKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 88 VKVLVEGIRRAKITTLSDNGEYFQAKAEYLET--PAVDEREQEVLNRTTINQFEGYIKLNK--KIPPEVLTSLHAIEESA 163
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 164 KLADTIASHMPLK-LKDKQAVLEMSDVTERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 243 EMDDAPDEMESLKRKIDAAKMPKEAKEKTEAELQKLKMMSPMSAEATVVRSYIDWMVQVPWNSRSKVKKDLVKAQEVLDT 322
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 323 DHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 482 LDRMEVIRLSGYTEDEKLNIAKQHLLPKQIERNALKPSELTIHDSAIMGIIRYYTREAGVRSLEREISKLCRKAVKQLLM 561
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 562 DSTIKH-----IEINEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQE 636
Cdd:TIGR00763 561 QGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 637 SIQAAMTVVRARADKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPI 716
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 717 GGLKEKLLAAHRGGIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLAL 771
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
313-493 |
8.77e-124 |
|
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: 368.42 E-value: 8.77e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 313 LVKAQEVLDTDHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATS 472
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1130902148 473 NSM-NIPAPLLDRMEVIRLSGY 493
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
570-771 |
7.09e-122 |
|
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: 364.25 E-value: 7.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 570 INEDNLKDYLGVRKVDYGRADTENRVGMVTGLAWTEVGGDLLTIETASVPGKGKLTFTGSLGEVMQESIQAAMTVVRARA 649
Cdd:pfam05362 2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 650 DKLGINGDFYEKRDMHVHVPEGATPKDGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLKEKLLAAHRG 729
Cdd:pfam05362 82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1130902148 730 GIKTVLIPDENKRDLEEIPENIVADLDIHPVKTIEEVLSLAL 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
10-201 |
1.10e-55 |
|
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: 189.47 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 10 EIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMNDNKQ--IMLVAQKDASTDEPGVNDLFSVGTVASVLQMLKLPDGT 87
Cdd:pfam02190 1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 88 VKVLVEGIRRAKITTL-SDNGEYFQAKAEYLETPAVDerEQEVLNRTTINQFEGYIKLNKKI-PPEVLTSLHAIEESAKL 165
Cdd:pfam02190 81 YKVLVEGLERVRIVELvKKEEPYLRAEVEDLPEDSDE--LSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1130902148 166 ADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMME 201
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
352-493 |
6.70e-25 |
|
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: 100.36 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 352 LCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDeaeirghrrTYIGSMPGKLIQKMAKVGVKNP-LFLLDEIDKM-- 428
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1130902148 429 -----SSDMRGDPASALLEVLDPEQNiafndhylevdyDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGY 493
Cdd:pfam00004 72 srgsgGDSESRRVVNQLLTELDGFTS------------SNSKVIVIAATNRPdKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
615-770 |
2.46e-24 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 101.59 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 615 TASVPGKGKLTFTGS--LGEVMQESIQAAMTVVRARADKlgingDFYEKrDMHVHVPEGATPKDGPSAGIAMCTALVSSL 692
Cdd:COG1750 51 TVTYPGSGRVYVSTSplTGPDTQASARIAALVASLLAGV-----DLSSY-DVYISIESDSPIVGGPSAGGAMTVATYAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 693 TGNPVRSDVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPDEN------------KRDLEEIPENIvaDLDIHPV 760
Cdd:COG1750 125 LGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQailtgyntqvgeTVDLVEYGKEL--GVKVIEV 202
|
170
....*....|
gi 1130902148 761 KTIEEVLSLA 770
Cdd:COG1750 203 STIADALQYF 212
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
10-203 |
8.89e-23 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 96.48 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 10 EIPVLPLrDVVVYPHMVIPLfvgreksiHCLEA--------AMNDNKQIMlVAQKDASTDEPGVNDLFSVGTVASVLQML 81
Cdd:COG2802 6 ELPLFPL-GAVLFPGGRLPL--------HIFEPryldmvrdCLAGDRPFG-VVLIREGREVGGPPPLYDVGTLARITDFE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 82 KLPDGTVKVLVEGIRRAKITTLSDNGE-YFQAKAEYLETPA---VDEREQEVLNRTtINQFEGYIKLNKkippevLTSLH 157
Cdd:COG2802 76 ELEDGRLDITLRGVQRFRILEELQEDDpYRVAEVEWLPDEPdlpVPEELEALRERL-LRLLRRYPELAG------LEADP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1130902148 158 AIEESAKLADTIASHMPLKLKDKQAVLEMSDVTERLEYLMAMMESE 203
Cdd:COG2802 149 DLDDPEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
677-772 |
1.32e-12 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 69.84 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 677 GPSAGIAMCTALVSSLTGNPVRS--DVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPDENkrdLEEIPENIVAD 754
Cdd:COG3480 240 GPSAGLMFALGIYDQLTPGDLTGgkKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---CAEAVGTIPTG 316
|
90
....*....|....*...
gi 1130902148 755 LDIHPVKTIEEVLSlALQ 772
Cdd:COG3480 317 LKVVPVDTLDDALD-ALE 333
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
331-488 |
2.36e-12 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 65.25 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 331 KERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMA---LGGVRDEAEIRGHRRTYIgsmpgKLI 407
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLylnASDLLEGLVVAELFGHFL-----VRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 408 QKMAKVGVKNPLFLLDEIDKMSSDMRgdpaSALLEVLdpeqniafnDHYLEVDYDLSDVMFVATSNSMN---IPAPLLDR 484
Cdd:cd00009 76 LFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNRPLlgdLDRALYDR 142
|
....
gi 1130902148 485 MEVI 488
Cdd:cd00009 143 LDIR 146
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
330-481 |
2.77e-12 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 65.38 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 330 VKERILEYLAVQSRVSKI------KGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAeirghrRTYIGSMP 403
Cdd:cd19481 1 LKASLREAVEAPRRGSRLrryglgLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 404 GKLIQKMAKvgVKNPLFLLDEIDKMSSDmRGDPA---------SALLEVLDPEQNiafndhylevdydLSDVMFVATSN- 473
Cdd:cd19481 75 RKIFERARR--LAPCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNr 138
|
....*....
gi 1130902148 474 -SMNIPAPL 481
Cdd:cd19481 139 pDLLDPALL 147
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
326-515 |
7.54e-12 |
|
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: 68.01 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 326 GLERVKERILEYLAVQSRVSKIKGPI-------LCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEaeirghrrtY 398
Cdd:COG0464 161 GLEEVKEELRELVALPLKRPELREEYglppprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 399 IGSMPGKL--IQKMAKvGVKNPLFLLDEIDKMSSDmRGdpasallEVLDPEQNIAFNdhYL--EVDYDLSDVMFVATSNS 474
Cdd:COG0464 232 VGETEKNLreVFDKAR-GLAPCVLFIDEADALAGK-RG-------EVGDGVGRRVVN--TLltEMEELRSDVVVIAATNR 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1130902148 475 M-NIPAPLLDRM-EVIRLSGYTEDEKLNIAKQHLLPKQIERNA 515
Cdd:COG0464 301 PdLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDEDV 343
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
676-769 |
2.77e-11 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 67.28 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 676 DGPSAGIAMCTALVSSLTGNPVRSDVAMTGEITLRGQVLPIGGLKEKL-----LAAHRG--GIKTVLIPDENKRDL---E 745
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARGltGKQGVIIPAANVKNLmlrD 671
|
90 100
....*....|....*....|....*
gi 1130902148 746 EIPENIVADL-DIHPVKTIEEVLSL 769
Cdd:COG1067 672 EVVEAVKAGQfHIYAVEHVDEAIEL 696
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
352-485 |
4.44e-11 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 61.15 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 352 LCLVGPPGVGKTSLGQSIAKAT-GRKYVRMALGgvRD--EAEIRGHRRtyIGSMPGKLIQKMAKVGVKNP-LFLLDEIDK 427
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLT--RDttEEDLFGRRN--IDPGGASWVDGPLVRAAREGeIAVLDEINR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1130902148 428 MSSDMrgdpASALLEVLDpEQNIAFNDHYLEVDYDLSDVMFVATSNS-----MNIPAPLLDRM 485
Cdd:pfam07728 78 ANPDV----LNSLLSLLD-ERRLLLPDGGELVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
326-505 |
8.96e-11 |
|
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: 63.65 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 326 GLERVKERILeyLAVQSRvskikGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMalggvrdeaeirghrRTYIGSMPGK 405
Cdd:COG0714 16 GQEELIELVL--IALLAG-----GHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 406 LI-------QKMAKVGVKNPLF----LLDEIDkmssdmRGDPA--SALLEVLDpeqniafnDHYLEVD---YDLSDVMFV 469
Cdd:COG0714 73 ILgtyiydqQTGEFEFRPGPLFanvlLADEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1130902148 470 -ATSNSM------NIPAPLLDRMeVIRLS-GY-TEDEKLNIAKQH 505
Cdd:COG0714 139 iATQNPIeqegtyPLPEAQLDRF-LLKLYiGYpDAEEEREILRRH 182
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
10-62 |
8.67e-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: 50.51 E-value: 8.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1130902148 10 EIPVLPLRDVVVYPHMVIPLFVGREKSIHCLEAAMND--NKQIMLVAQKDASTDE 62
Cdd:smart00464 1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRsqPYVIVFLLQDDPTETP 55
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
356-534 |
3.60e-06 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 50.05 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 356 GPPGVGKTSLGQSIAKATGRKYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--KMAKVGVKNPLFLLDEI---DKM 428
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 429 SSDmrgdpasALLEVLdpEQNIafndhylevdydlsdVMFVA--TSN-SMNIPAPLLDRMEVIRLSGYTEDEKLNIAKQH 505
Cdd:COG2256 121 QQD-------ALLPHV--EDGT---------------ITLIGatTENpSFEVNSALLSRCRVFVLKPLSEEDLEQLLERA 176
|
170 180
....*....|....*....|....*....
gi 1130902148 506 LlpKQIERNaLKPSELTIHDSAIMGIIRY 534
Cdd:COG2256 177 L--ADDERG-LGGYKLELDDEALEALARL 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-485 |
5.09e-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: 46.98 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 348 KGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL----IQKMAKV-----GVKNP 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgELRLRLAlalarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1130902148 419 LFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNdhylevdydlsDVMFVATSNSMNIPAPLLDRM 485
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK-----------NLTVILTTNDEKDLGPALLRR 136
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
356-497 |
7.52e-06 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.93 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 356 GPPGVGKTSLGQSIAKATGRKYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--KMAKVGVKNPLFLLDEI---DKM 428
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEeaRQRRSAGRRTILFIDEIhrfNKA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1130902148 429 SSDmrgdpasALLEVLdpEQNiafndhylevdydlsDVMFVA--TSN-SMNIPAPLLDRMEVIRLSGYTEDE 497
Cdd:PRK13342 108 QQD-------ALLPHV--EDG---------------TITLIGatTENpSFEVNPALLSRAQVFELKPLSEED 155
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
323-592 |
1.18e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.57 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 323 DHYGLERVKE---RILEYLAVQSRVSKIKGP----ILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVrdeaeirghr 395
Cdd:COG1223 3 DVVGQEEAKKklkLIIKELRRRENLRKFGLWpprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 396 rtyIGSMPGKLIQKMAKV--------GVknplFLLDEIDKMSSDmRGDPA---------SALLevldpeqniafndhyLE 458
Cdd:COG1223 72 ---IGSYLGETARNLRKLfdfarrapCV----IFFDEFDAIAKD-RGDQNdvgevkrvvNALL---------------QE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 459 VDYDLSDVMFVATSNSMNI--PApLLDRM-EVIRLSGYTEDEKLNIAKQHL--LPKQIERNALKPSELTihdSAIMGiir 533
Cdd:COG1223 129 LDGLPSGSVVIAATNHPELldSA-LWRRFdEVIEFPLPDKEERKEILELNLkkFPLPFELDLKKLAKKL---EGLSG--- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1130902148 534 yytreagvrsleREISKLCRKAVKQLLMDstiKHIEINEDNLKDYLGVRKVDYGRADTE 592
Cdd:COG1223 202 ------------ADIEKVLKTALKKAILE---DREKVTKEDLEEALKQRKERKKEPKKE 245
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
348-469 |
1.82e-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: 42.62 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 348 KGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPG------KLIQkMAKVGVKNP-LF 420
Cdd:cd00267 24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrQRVA-LARALLLNPdLL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1130902148 421 LLDEIDK-MSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFV 469
Cdd:cd00267 103 LLDEPTSgLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
247-371 |
3.62e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 43.70 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 247 APDEMESLKRKIDAAKMPKEAKE-KTEAELQKLKMMSPMSAEATVVRSYIDWMVqvpwnsRSKVKKDLvkAQEVLDT--D 323
Cdd:COG1419 63 APAAASAAAEEEELEELRRELAElKELLEEQLSGLAGESARLPPELAELLERLL------EAGVSPEL--ARELLEKlpE 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1130902148 324 HYGLERVKERILEYLAvqSRVSKIKGPIL------CLVGPPGVGKTSlgqSIAK 371
Cdd:COG1419 135 DLSAEEAWRALLEALA--RRLPVAEDPLLdeggviALVGPTGVGKTT---TIAK 183
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
347-378 |
2.02e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 39.79 E-value: 2.02e-03
10 20 30
....*....|....*....|....*....|..
gi 1130902148 347 IKGPILCLVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
352-378 |
2.15e-03 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 39.73 E-value: 2.15e-03
10 20
....*....|....*....|....*..
gi 1130902148 352 LCLVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
354-378 |
2.30e-03 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 39.46 E-value: 2.30e-03
10 20
....*....|....*....|....*
gi 1130902148 354 LVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:cd00464 4 LIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
305-503 |
2.98e-03 |
|
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: 40.98 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 305 SRSKVKKDLVKAQEVLDtDHYGLERVKERILEY---LAVQSRVSKIKGPI------LCLVGPPGVGKTslgqSIAKATGR 375
Cdd:TIGR03922 260 AAERKAKLLAEAEAELA-EQIGLERVKRQVAALkssTAMALARAERGLPVaqtsnhMLFAGPPGTGKT----TIARVVAK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 376 KYVrmALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV--GVKNPLFLLDEIDKMSSDMRGDPasallevlDPEQNIAFN 453
Cdd:TIGR03922 335 IYC--GLGVLRKPLVREVSRADLIGQYIGESEAKTNEIidSALGGVLFLDEAYTLVETGYGQK--------DPFGLEAID 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 454 D--HYLEVDYDLSDVMFVATSNSMNipaPLLDRME--------VIRLSGYTEDEKLNIAK 503
Cdd:TIGR03922 405 TllARMENDRDRLVVIGAGYRKDLD---KFLEVNEglrsrftrVIEFPSYSPDELVEIAR 461
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
210-287 |
3.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 210 EKRIRNRVKKQMEKS--QREYYLNEQMKAIQKELGEMDDAPDEMESLKRKIDaaKMPKEAKEKTEAELQKLKMMSPMSAE 287
Cdd:PRK12704 76 ELRERRNELQKLEKRllQKEENLDRKLELLEKREEELEKKEKELEQKQQELE--KKEEELEELIEEQLQELERISGLTAE 153
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
318-564 |
3.58e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 40.37 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 318 EVLDTDHYGLERVKERILEYLAVQSR---------VSKIKGpILcLVGPPGVGKTSLGQSIAKATGRKYVRMALggvrde 388
Cdd:COG1222 74 DVTFDDIGGLDEQIEEIREAVELPLKnpelfrkygIEPPKG-VL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 389 AEIrghRRTYIGSMPGKL--IQKMAKvgVKNP--LFlLDEIDKMSSdMRGDPAS---------ALLEVLDpeqniafndh 455
Cdd:COG1222 146 SEL---VSKYIGEGARNVreVFELAR--EKAPsiIF-IDEIDAIAA-RRTDDGTsgevqrtvnQLLAELD---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 456 ylEVDyDLSDVMFVATSNSMNI--PAPL----LDRmeVIRLSGYTEDEKLNIAKQHLLPKQIERNaLKPSEL-TIHDSAI 528
Cdd:COG1222 209 --GFE-SRGDVLIIAATNRPDLldPALLrpgrFDR--VIEVPLPDEEAREEILKIHLRDMPLADD-VDLDKLaKLTEGFS 282
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1130902148 529 MGIIRYYTREAGVRSLEREISKLC----RKAVKQLLMDST 564
Cdd:COG1222 283 GADLKAIVTEAGMFAIREGRDTVTmedlEKAIEKVKKKTE 322
|
|
| AAA_PrkA |
pfam08298 |
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ... |
323-372 |
4.26e-03 |
|
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.
Pssm-ID: 116881 Cd Length: 358 Bit Score: 40.13 E-value: 4.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1130902148 323 DHYGLERVKERILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKA 372
Cdd:pfam08298 59 DFFGMEETIERIVNYFRHAAQGLEERKQILYLLGPVGGGKSSLAERLKKL 108
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
325-383 |
4.32e-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: 38.64 E-value: 4.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1130902148 325 YGLERVKERILEYLavqSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALG 383
Cdd:pfam13191 3 VGREEELEQLLDAL---DRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
346-456 |
5.54e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.90 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 346 KIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR---GHRRTY--IGSMPGKLIqkmakvgvknplf 420
Cdd:PRK04195 37 KPKKALL-LYGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVIErvaGEAATSgsLFGARRKLI------------- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1130902148 421 LLDEIDKMSSdmRGDP--ASALLEVLDPEQN----IAfNDHY 456
Cdd:PRK04195 103 LLDEVDGIHG--NEDRggARAILELIKKAKQpiilTA-NDPY 141
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
323-390 |
5.73e-03 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 40.02 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 323 DHYGLERVKERI---LEYLAVQSRVSKIKGPI---LCLVGPPGVGKTSLGQSIA--------KATGRKYVRMALG----G 384
Cdd:PRK10733 153 DVAGCDEAKEEVaelVEYLREPSRFQKLGGKIpkgVLMVGPPGTGKTLLAKAIAgeakvpffTISGSDFVEMFVGvgasR 232
|
....*.
gi 1130902148 385 VRDEAE 390
Cdd:PRK10733 233 VRDMFE 238
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
247-371 |
9.79e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 38.86 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 247 APDEMESLKRKIDAAKMPKEAKEKTEAELQKLK-----MMSPMSAEAT--VVRSYIDWMVqvpwnsRSKVKKDLVK--AQ 317
Cdd:TIGR03499 85 LPAPQEEPAAPAAQAAEPLLPEEELRKELEALRellerLLAGLAWLQRppERAKLYERLL------EAGVSEELARelLE 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130902148 318 EVLDTDHygLERVKERILEYLAVQSRVSKIKGPIL------CLVGPPGVGKTSlgqSIAK 371
Cdd:TIGR03499 159 KLPEDAD--AEDAWRWLREALEGMLPVKPEEDPILeqggviALVGPTGVGKTT---TLAK 213
|
|
| |
